Full text data of ANXA7
ANXA7
(ANX7, SNX)
[Confidence: high (present in two of the MS resources)]
Annexin A7 (Annexin VII; Annexin-7; Synexin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Annexin A7 (Annexin VII; Annexin-7; Synexin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00002460
IPI00002460 annexin VII isoform 2 annexin VII isoform 2 membrane 1 3 n/a 2 4 n/a 2 1 9 n/a n/a 1 1 n/a n/a n/a n/a 5 4 3 integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00002460 annexin VII isoform 2 annexin VII isoform 2 membrane 1 3 n/a 2 4 n/a 2 1 9 n/a n/a 1 1 n/a n/a n/a n/a 5 4 3 integral membrane protein n/a found at its expected molecular weight found at molecular weight
Comments
Isoform P20073-2 was detected.
Isoform P20073-2 was detected.
UniProt
P20073
ID ANXA7_HUMAN Reviewed; 488 AA.
AC P20073; Q5F2H3; Q5T0M6; Q5T0M7;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 3.
DT 22-JAN-2014, entry version 143.
DE RecName: Full=Annexin A7;
DE AltName: Full=Annexin VII;
DE AltName: Full=Annexin-7;
DE AltName: Full=Synexin;
GN Name=ANXA7; Synonyms=ANX7, SNX; ORFNames=OK/SW-cl.95;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2542947; DOI=10.1073/pnas.86.10.3798;
RA Burns A.L., Magendzo K., Shirvan A., Srivastava M., Rojas E.,
RA Alijani M.R., Pollard H.B.;
RT "Calcium channel activity of purified human synexin and structure of
RT the human synexin gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3798-3802(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=7515686; DOI=10.1021/bi00188a019;
RA Shirvan A., Srivastava M., Wang M.G., Cultraro C., Magendzo K.,
RA McBride O.W., Pollard H.B., Burns A.L.;
RT "Divergent structure of the human synexin (annexin VII) gene and
RT assignment to chromosome 10.";
RL Biochemistry 33:6888-6901(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 145-166 (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fibroblast;
RX PubMed=1825209;
RA Magendzo K., Shirvan A., Cultraro C., Srivastava M., Pollard H.B.,
RA Burns A.L.;
RT "Alternative splicing of human synexin mRNA in brain, cardiac, and
RT skeletal muscle alters the unique N-terminal domain.";
RL J. Biol. Chem. 266:3228-3232(1991).
RN [10]
RP INTERACTION WITH PDCD6.
RX PubMed=18256029; DOI=10.1074/jbc.M800717200;
RA Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
RA Maki M.;
RT "Identification of Alix-type and non-Alix-type ALG-2-binding sites in
RT human phospholipid scramblase 3: differential binding to an
RT alternatively spliced isoform and amino acid-substituted mutants.";
RL J. Biol. Chem. 283:9623-9632(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Calcium/phospholipid-binding protein which promotes
CC membrane fusion and is involved in exocytosis.
CC -!- SUBUNIT: Interacts with PDCD6.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Annexin VIIb;
CC IsoId=P20073-1; Sequence=Displayed;
CC Name=2; Synonyms=Annexin VIIa;
CC IsoId=P20073-2; Sequence=VSP_011843;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in brain, heart and
CC skeletal muscle. Isoform 2 is more abundant in liver, lung,
CC kidney, spleen, fibroblasts and placenta.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for
CC calcium and phospholipid.
CC -!- SIMILARITY: Belongs to the annexin family.
CC -!- SIMILARITY: Contains 4 annexin repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI52483.1; Type=Erroneous gene model prediction;
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DR EMBL; J04543; AAA36616.1; -; mRNA.
DR EMBL; AB062429; BAB93492.1; -; mRNA.
DR EMBL; BT007187; AAP35851.1; -; mRNA.
DR EMBL; CR407686; CAG28614.1; -; mRNA.
DR EMBL; AL512656; CAI15290.1; -; Genomic_DNA.
DR EMBL; AL353731; CAI15290.1; JOINED; Genomic_DNA.
DR EMBL; AL512656; CAI15291.1; -; Genomic_DNA.
DR EMBL; AL353731; CAI15291.1; JOINED; Genomic_DNA.
DR EMBL; AL353731; CAI52483.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL353731; CAI52484.1; -; Genomic_DNA.
DR EMBL; AL512656; CAI52484.1; JOINED; Genomic_DNA.
DR EMBL; AL353731; CAI52485.1; -; Genomic_DNA.
DR EMBL; AL512656; CAI52485.1; JOINED; Genomic_DNA.
DR EMBL; CH471083; EAW54493.1; -; Genomic_DNA.
DR EMBL; CH471083; EAW54494.1; -; Genomic_DNA.
DR EMBL; BC002632; AAH02632.1; -; mRNA.
DR PIR; A54467; LUHU7.
DR RefSeq; NP_001147.1; NM_001156.3.
DR RefSeq; NP_004025.1; NM_004034.2.
DR UniGene; Hs.631827; -.
DR ProteinModelPortal; P20073; -.
DR SMR; P20073; 174-488.
DR IntAct; P20073; 114.
DR MINT; MINT-4999305; -.
DR STRING; 9606.ENSP00000362010; -.
DR PhosphoSite; P20073; -.
DR DMDM; 215274186; -.
DR REPRODUCTION-2DPAGE; IPI00002460; -.
DR PaxDb; P20073; -.
DR PRIDE; P20073; -.
DR DNASU; 310; -.
DR Ensembl; ENST00000372919; ENSP00000362010; ENSG00000138279.
DR Ensembl; ENST00000372921; ENSP00000362012; ENSG00000138279.
DR GeneID; 310; -.
DR KEGG; hsa:310; -.
DR UCSC; uc001jtz.2; human.
DR CTD; 310; -.
DR GeneCards; GC10M075135; -.
DR HGNC; HGNC:545; ANXA7.
DR HPA; CAB004312; -.
DR MIM; 186360; gene.
DR neXtProt; NX_P20073; -.
DR PharmGKB; PA24835; -.
DR eggNOG; NOG267770; -.
DR HOGENOM; HOG000158803; -.
DR HOVERGEN; HBG061815; -.
DR InParanoid; P20073; -.
DR KO; K17095; -.
DR OMA; FSQMYQK; -.
DR OrthoDB; EOG74XS72; -.
DR PhylomeDB; P20073; -.
DR ChiTaRS; ANXA7; human.
DR GeneWiki; ANXA7; -.
DR GenomeRNAi; 310; -.
DR NextBio; 1253; -.
DR PRO; PR:P20073; -.
DR ArrayExpress; P20073; -.
DR Bgee; P20073; -.
DR CleanEx; HS_ANXA7; -.
DR Genevestigator; P20073; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:BHF-UCL.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0009992; P:cellular water homeostasis; IEA:Ensembl.
DR GO; GO:0007599; P:hemostasis; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR GO; GO:0035176; P:social behavior; IEP:UniProtKB.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR013286; AnnexinVII.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR01871; ANNEXINVII.
DR SMART; SM00335; ANX; 4.
DR PROSITE; PS00223; ANNEXIN; 4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Annexin; Calcium;
KW Calcium/phospholipid-binding; Complete proteome;
KW Direct protein sequencing; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 488 Annexin A7.
FT /FTId=PRO_0000067499.
FT REPEAT 5 9 1.
FT REPEAT 10 14 2.
FT REPEAT 16 20 3.
FT REPEAT 189 254 Annexin 1.
FT REPEAT 266 326 Annexin 2.
FT REPEAT 349 409 Annexin 3.
FT REPEAT 425 485 Annexin 4.
FT REGION 1 143 Repeat-rich region.
FT REGION 5 20 3 X 5 AA tandem repeats of G-Y-P-P-X.
FT MOD_RES 233 233 N6-acetyllysine.
FT VAR_SEQ 146 167 Missing (in isoform 2).
FT /FTId=VSP_011843.
FT VARIANT 441 441 R -> Q (in dbSNP:rs3750575).
FT /FTId=VAR_048253.
SQ SEQUENCE 488 AA; 52739 MW; BFC688479D8CC2A0 CRC64;
MSYPGYPPTG YPPFPGYPPA GQESSFPPSG QYPYPSGFPP MGGGAYPQVP SSGYPGAGGY
PAPGGYPAPG GYPGAPQPGG APSYPGVPPG QGFGVPPGGA GFSGYPQPPS QSYGGGPAQV
PLPGGFPGGQ MPSQYPGGQP TYPSQINTDS FSSYPVFSPV SLDYSSEPAT VTQVTQGTIR
PAANFDAIRD AEILRKAMKG FGTDEQAIVD VVANRSNDQR QKIKAAFKTS YGKDLIKDLK
SELSGNMEEL ILALFMPPTY YDAWSLRKAM QGAGTQERVL IEILCTRTNQ EIREIVRCYQ
SEFGRDLEKD IRSDTSGHFE RLLVSMCQGN RDENQSINHQ MAQEDAQRLY QAGEGRLGTD
ESCFNMILAT RSFPQLRATM EAYSRMANRD LLSSVSREFS GYVESGLKTI LQCALNRPAF
FAERLYYAMK GAGTDDSTLV RIVVTRSEID LVQIKQMFAQ MYQKTLGTMI AGDTSGDYRR
LLLAIVGQ
//
ID ANXA7_HUMAN Reviewed; 488 AA.
AC P20073; Q5F2H3; Q5T0M6; Q5T0M7;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 3.
DT 22-JAN-2014, entry version 143.
DE RecName: Full=Annexin A7;
DE AltName: Full=Annexin VII;
DE AltName: Full=Annexin-7;
DE AltName: Full=Synexin;
GN Name=ANXA7; Synonyms=ANX7, SNX; ORFNames=OK/SW-cl.95;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2542947; DOI=10.1073/pnas.86.10.3798;
RA Burns A.L., Magendzo K., Shirvan A., Srivastava M., Rojas E.,
RA Alijani M.R., Pollard H.B.;
RT "Calcium channel activity of purified human synexin and structure of
RT the human synexin gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3798-3802(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=7515686; DOI=10.1021/bi00188a019;
RA Shirvan A., Srivastava M., Wang M.G., Cultraro C., Magendzo K.,
RA McBride O.W., Pollard H.B., Burns A.L.;
RT "Divergent structure of the human synexin (annexin VII) gene and
RT assignment to chromosome 10.";
RL Biochemistry 33:6888-6901(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 145-166 (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fibroblast;
RX PubMed=1825209;
RA Magendzo K., Shirvan A., Cultraro C., Srivastava M., Pollard H.B.,
RA Burns A.L.;
RT "Alternative splicing of human synexin mRNA in brain, cardiac, and
RT skeletal muscle alters the unique N-terminal domain.";
RL J. Biol. Chem. 266:3228-3232(1991).
RN [10]
RP INTERACTION WITH PDCD6.
RX PubMed=18256029; DOI=10.1074/jbc.M800717200;
RA Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
RA Maki M.;
RT "Identification of Alix-type and non-Alix-type ALG-2-binding sites in
RT human phospholipid scramblase 3: differential binding to an
RT alternatively spliced isoform and amino acid-substituted mutants.";
RL J. Biol. Chem. 283:9623-9632(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Calcium/phospholipid-binding protein which promotes
CC membrane fusion and is involved in exocytosis.
CC -!- SUBUNIT: Interacts with PDCD6.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Annexin VIIb;
CC IsoId=P20073-1; Sequence=Displayed;
CC Name=2; Synonyms=Annexin VIIa;
CC IsoId=P20073-2; Sequence=VSP_011843;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in brain, heart and
CC skeletal muscle. Isoform 2 is more abundant in liver, lung,
CC kidney, spleen, fibroblasts and placenta.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for
CC calcium and phospholipid.
CC -!- SIMILARITY: Belongs to the annexin family.
CC -!- SIMILARITY: Contains 4 annexin repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI52483.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; J04543; AAA36616.1; -; mRNA.
DR EMBL; AB062429; BAB93492.1; -; mRNA.
DR EMBL; BT007187; AAP35851.1; -; mRNA.
DR EMBL; CR407686; CAG28614.1; -; mRNA.
DR EMBL; AL512656; CAI15290.1; -; Genomic_DNA.
DR EMBL; AL353731; CAI15290.1; JOINED; Genomic_DNA.
DR EMBL; AL512656; CAI15291.1; -; Genomic_DNA.
DR EMBL; AL353731; CAI15291.1; JOINED; Genomic_DNA.
DR EMBL; AL353731; CAI52483.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL353731; CAI52484.1; -; Genomic_DNA.
DR EMBL; AL512656; CAI52484.1; JOINED; Genomic_DNA.
DR EMBL; AL353731; CAI52485.1; -; Genomic_DNA.
DR EMBL; AL512656; CAI52485.1; JOINED; Genomic_DNA.
DR EMBL; CH471083; EAW54493.1; -; Genomic_DNA.
DR EMBL; CH471083; EAW54494.1; -; Genomic_DNA.
DR EMBL; BC002632; AAH02632.1; -; mRNA.
DR PIR; A54467; LUHU7.
DR RefSeq; NP_001147.1; NM_001156.3.
DR RefSeq; NP_004025.1; NM_004034.2.
DR UniGene; Hs.631827; -.
DR ProteinModelPortal; P20073; -.
DR SMR; P20073; 174-488.
DR IntAct; P20073; 114.
DR MINT; MINT-4999305; -.
DR STRING; 9606.ENSP00000362010; -.
DR PhosphoSite; P20073; -.
DR DMDM; 215274186; -.
DR REPRODUCTION-2DPAGE; IPI00002460; -.
DR PaxDb; P20073; -.
DR PRIDE; P20073; -.
DR DNASU; 310; -.
DR Ensembl; ENST00000372919; ENSP00000362010; ENSG00000138279.
DR Ensembl; ENST00000372921; ENSP00000362012; ENSG00000138279.
DR GeneID; 310; -.
DR KEGG; hsa:310; -.
DR UCSC; uc001jtz.2; human.
DR CTD; 310; -.
DR GeneCards; GC10M075135; -.
DR HGNC; HGNC:545; ANXA7.
DR HPA; CAB004312; -.
DR MIM; 186360; gene.
DR neXtProt; NX_P20073; -.
DR PharmGKB; PA24835; -.
DR eggNOG; NOG267770; -.
DR HOGENOM; HOG000158803; -.
DR HOVERGEN; HBG061815; -.
DR InParanoid; P20073; -.
DR KO; K17095; -.
DR OMA; FSQMYQK; -.
DR OrthoDB; EOG74XS72; -.
DR PhylomeDB; P20073; -.
DR ChiTaRS; ANXA7; human.
DR GeneWiki; ANXA7; -.
DR GenomeRNAi; 310; -.
DR NextBio; 1253; -.
DR PRO; PR:P20073; -.
DR ArrayExpress; P20073; -.
DR Bgee; P20073; -.
DR CleanEx; HS_ANXA7; -.
DR Genevestigator; P20073; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:BHF-UCL.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0009992; P:cellular water homeostasis; IEA:Ensembl.
DR GO; GO:0007599; P:hemostasis; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR GO; GO:0035176; P:social behavior; IEP:UniProtKB.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR013286; AnnexinVII.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR01871; ANNEXINVII.
DR SMART; SM00335; ANX; 4.
DR PROSITE; PS00223; ANNEXIN; 4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Annexin; Calcium;
KW Calcium/phospholipid-binding; Complete proteome;
KW Direct protein sequencing; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 488 Annexin A7.
FT /FTId=PRO_0000067499.
FT REPEAT 5 9 1.
FT REPEAT 10 14 2.
FT REPEAT 16 20 3.
FT REPEAT 189 254 Annexin 1.
FT REPEAT 266 326 Annexin 2.
FT REPEAT 349 409 Annexin 3.
FT REPEAT 425 485 Annexin 4.
FT REGION 1 143 Repeat-rich region.
FT REGION 5 20 3 X 5 AA tandem repeats of G-Y-P-P-X.
FT MOD_RES 233 233 N6-acetyllysine.
FT VAR_SEQ 146 167 Missing (in isoform 2).
FT /FTId=VSP_011843.
FT VARIANT 441 441 R -> Q (in dbSNP:rs3750575).
FT /FTId=VAR_048253.
SQ SEQUENCE 488 AA; 52739 MW; BFC688479D8CC2A0 CRC64;
MSYPGYPPTG YPPFPGYPPA GQESSFPPSG QYPYPSGFPP MGGGAYPQVP SSGYPGAGGY
PAPGGYPAPG GYPGAPQPGG APSYPGVPPG QGFGVPPGGA GFSGYPQPPS QSYGGGPAQV
PLPGGFPGGQ MPSQYPGGQP TYPSQINTDS FSSYPVFSPV SLDYSSEPAT VTQVTQGTIR
PAANFDAIRD AEILRKAMKG FGTDEQAIVD VVANRSNDQR QKIKAAFKTS YGKDLIKDLK
SELSGNMEEL ILALFMPPTY YDAWSLRKAM QGAGTQERVL IEILCTRTNQ EIREIVRCYQ
SEFGRDLEKD IRSDTSGHFE RLLVSMCQGN RDENQSINHQ MAQEDAQRLY QAGEGRLGTD
ESCFNMILAT RSFPQLRATM EAYSRMANRD LLSSVSREFS GYVESGLKTI LQCALNRPAF
FAERLYYAMK GAGTDDSTLV RIVVTRSEID LVQIKQMFAQ MYQKTLGTMI AGDTSGDYRR
LLLAIVGQ
//
MIM
186360
*RECORD*
*FIELD* NO
186360
*FIELD* TI
*186360 ANNEXIN A7; ANXA7
;;ANNEXIN VII; ANX7;;
SYNEXIN; SNX
*FIELD* TX
DESCRIPTION
read more
Synexin is a calcium-dependent membrane-binding protein that not only
fuses membranes but also acts as a voltage-dependent calcium channel.
CLONING
Burns et al. (1989) isolated and sequenced a set of overlapping cDNA
clones for human synexin. Its derived amino acid sequence shows strong
homology in the C-terminal domain with a previously identified class of
calcium-dependent membrane-binding proteins, including endonexin II
(131230), lipocortin I (151690), calpactin I heavy chain (114085), and
others.
Magendzo et al. (1991) cloned 3 variants of synexin cDNA from a human
fibroblast cDNA library. Sequence analysis indicated that the variants
were formed by alternative splicing and use of alternate polyadenylation
signals. Northern blot analysis of fibroblasts revealed transcripts of
2.0 and 2.4 kb. Using primers designed to differentiate between these 2
forms by PCR, Magendzo et al. (1991) found the larger transcript,
containing a 66-bp exon, in human and monkey brain, heart, and skeletal
muscle. They found the variant lacking this exon in liver, lung, kidney,
spleen, fibroblasts, and placenta. Western blot analysis indicated the
presence of the larger protein in human skeletal muscle and the smaller
protein in lung.
GENE FUNCTION
The ANX7 gene is located on chromosome 10q21, a site long hypothesized
to harbor a tumor suppressor gene or genes associated with prostate and
other cancers. To test this hypothesis, Srivastava et al. (2001)
analyzed the action of the ANX7 gene on colony formation by human tumor
cell lines. They also examined the expression of the ANX7 protein in a
large number of prostate cancers using tumor tissue microarray
technology. Finally, they tested a panel of primary and metastatic
prostate cancers for evidence of loss of heterozygosity (LOH). They
found that human tumor cell proliferation and colony formation were
markedly reduced when the wildtype ANX7 gene was transfected into 2
prostate tumor cell lines. Consistently, analysis of ANX7 protein
expression in human prostate tumor microarrays revealed a significantly
higher rate of loss of ANX7 expression in metastatic and local
recurrences of hormone refractory prostate cancer as compared with
primary tumors (P = 0.0001). Using 4 microsatellite markers at or near
the ANX7 locus and laser capture microdissected tumor cells, 35% of 20
primary prostate tumors showed LOH. The microsatellite marker closest to
the ANX7 locus showed the highest rate of LOH, including 1 homozygous
deletion. Srivastava et al. (2001) concluded that the ANX7 gene exhibits
many biologic and genetic properties expected of a tumor suppressor gene
and may play a role in prostate cancer progression.
Caohuy et al. (1996) present experimental evidence, based on studies of
recombinant human ANXA7 and isolated bovine chromaffin cells, that ANXA7
is a Ca(2+)-dependent GTP binding protein. ANXA7 was active in a
chromaffin granule aggregation assays in the presence of Ca(2+) and GTP,
and was deactivated upon GTP hydrolysis.
GENE STRUCTURE
Shirvan et al. (1994) determined that the synexin gene contains 14
exons, including an alternatively spliced cassette exon, and spans
approximately 34 kb of DNA. Only 5 of the 14 spliced exons are conserved
compared to other annexins; the differences are particularly pronounced
in the exons that encode the C-terminal third and fourth conserved
repeats in the gene product. Shirvan et al. (1994) concluded that the
ANXA7 gene may have diverged from the evolutionary pathway taken by both
ANXA1 and ANXA2.
Zhang-Keck et al. (1994) found that the mouse homolog also contains 14
exons; it spans approximately 30 kb of genomic DNA.
MAPPING
Shirvan et al. (1994) isolated genomic clones of the ANXA7 gene and
assigned the gene to 10q21.1-q21.2 by study of somatic cell hybrids and
by in situ hybridization.
By study of Chinese hamster/mouse somatic cell hybrids and by linkage
analyses in interspecific crosses, Zhang-Keck et al. (1994) demonstrated
that the functional synexin gene is located on mouse chromosome 14 and
that a pseudogene is located on chromosome 10.
ANIMAL MODEL
By gene targeting, Srivastava et al. (1999) developed Anxa7-null mice.
The null phenotype was lethal at embryonic day 10. Heterozygous mice
were viable and fertile, but showed a defect in insulin secretion and an
increased insulin content within isolated pancreatic islets.
Electrooptical recordings suggested that the mutation altered Ca(2+)
release by agonists of inositol trisphosphate.
Using mice with a different genetic background and an alternate strategy
to introduce the null mutation, Herr et al. (2001) developed Anxa7 -/-
mice that were viable, fertile, and showed no obvious defects. Analysis
of insulin secretion from isolated islets revealed no evidence for the
involvement of Anxa7 in Ca(2+)-dependent or cAMP-mediated exocytosis. In
cardiomyocytes, however, they found a functional role for Anxa7 in
electromechanical coupling. Cardiomyocytes from embryonic Anxa7-null
mice displayed intact Ca(2+) homeostasis and unremarkable
excitation-contraction coupling; however, adult Anxa7 -/- mice exhibited
a decrease in frequency-induced cell shortening.
To investigate the mechanism by which the ANX7 gene controls tumor
development, Srivastava et al. (2003) developed an Anx7 +/- knockout
mouse. As hypothesized, these heterozygous mice had a cancer-prone
phenotype. The emerging tumors expressed low levels of Anx7 protein.
Nonetheless, the wildtype Anx7 allele was detectable in tumor tissue
cells. Genome array analysis of hepatocellular carcinoma tissue
indicated that the Anx7 +/- genotype is accompanied by profound
reductions of expression of several other tumor suppressor genes, DNA
repair genes, and apoptosis-related genes. In situ analysis by tissue
imprinting from chromosomes in the primary tumor and spectral
karyotyping analysis of derived cell lines identified chromosomal
instability and clonal chromosomal aberrations. Furthermore, whereas 23%
of the mutant mice developed spontaneous neoplasms, all mice exhibited
growth anomalies, including gender-specific gigantism and organomegaly.
Srivastava et al. (2003) concluded that haploinsufficiency of Anx7
expression drives disease progression to cancer because of genomic
instability through a discrete signaling pathway involving other tumor
suppressor genes, DNA-repair genes, and apoptosis-related genes.
*FIELD* RF
1. Burns, A. L.; Magendzo, K.; Shirvan, A.; Srivastava, M.; Rojas,
E.; Alijani, M. R.; Pollard, H. B.: Calcium channel activity of purified
human synexin and structure of the human synexin gene. Proc. Nat.
Acad. Sci. 86: 3798-3802, 1989.
2. Caohuy, H.; Srivastava, M.; Pollard, H. B.: Membrane fusion protein
synexin (annexin VII) as a Ca(2+)/GTP sensor in exocytotic secretion. Proc.
Nat. Acad. Sci. 93: 10797-10802, 1996.
3. Herr, C.; Smyth, N.; Ullrich, S.; Yun, F.; Sasse, P.; Hescheler,
J.; Fleischmann, B.; Lasek, K.; Brixius, K.; Schwinger, R. H. G.;
Fassler, R.; Schroder, R.; Noegel, A. A.: Loss of annexin A7 leads
to alterations in frequency-induced shortening of isolated murine
cardiomyocytes. Molec. Cell. Biol. 21: 4119-4128, 2001.
4. Magendzo, K.; Shirvan, A.; Cultraro, C.; Srivastava, M.; Pollard,
H. B.; Burns, A. L.: Alternative splicing of human synexin mRNA in
brain, cardiac, and skeletal muscle alters the unique N-terminal domain. J.
Biol. Chem. 266: 3228-3232, 1991.
5. Shirvan, A.; Srivastava, M.; Wang, M. G.; Cultraro, C.; Magendzo,
K.; McBride, O. W.; Pollard, H. B.; Burns, A. L.: Divergent structure
of the human synexin (annexin VII) gene and assignment to chromosome
10. Biochemistry 33: 6888-6901, 1994.
6. Srivastava, M.; Atwater, I.; Glasman, M.; Leighton, X.; Goping,
G.; Caohuy, H.; Miller, G.; Pichel, J.; Westphal, H.; Mears, D.; Rojas,
E.; Pollard, H. B.: Defects in inositol 1,4,5-trisphosphate receptor
expression, Ca(2+) signaling, and insulin secretion in the anx7(+/-)
knockout mouse. Proc. Nat. Acad. Sci. 96: 13783-13788, 1999.
7. Srivastava, M.; Bubendorf, L.; Srikantan, V.; Fossom, L.; Nolan,
L.; Glasman, M.; Leighton, X.; Fehrle, W.; Pittaluga, S.; Raffeld,
M.; Koivisto, P.; Willi, N.; Gasser, T. C.; Kononen, J.; Sauter, G.;
Kallioniemi, O. P.; Srivastava, S.; Pollard, H. B.: ANX7, a candidate
tumor suppressor gene for prostate cancer. Proc. Nat. Acad. Sci. 98:
4575-4580, 2001.
8. Srivastava, M.; Montagna, C.; Leighton, X.; Glasman, M.; Naga,
S.; Eidelman, O.; Ried, T.; Pollard, H. B.: Haploinsufficiency of
Anx7 tumor suppressor gene and consequent genomic instability promotes
tumorigenesis in the Anx7(+/-) mouse. Proc. Nat. Acad. Sci. 100:
14287-14292, 2003.
9. Zhang-Keck, Z.-Y.; Srivastava, M.; Kozak, C. A.; Caohuy, H.; Shirvan,
A.; Burns, A. L.; Pollard, H. B.: Genomic organization and chromosomal
localization of the mouse synexin gene. Biochem. J. 301: 835-845,
1994.
*FIELD* CN
Victor A. McKusick - updated: 12/3/2004
Patricia A. Hartz - updated: 6/13/2002
Victor A. McKusick - updated: 5/14/2001
*FIELD* CD
Victor A. McKusick: 6/7/1989
*FIELD* ED
terry: 05/20/2010
terry: 5/20/2010
tkritzer: 12/8/2004
terry: 12/3/2004
carol: 6/19/2002
terry: 6/13/2002
mcapotos: 5/22/2001
mcapotos: 5/18/2001
terry: 5/14/2001
mgross: 9/17/1999
mark: 2/25/1998
carol: 11/18/1994
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 8/4/1989
carol: 6/7/1989
*RECORD*
*FIELD* NO
186360
*FIELD* TI
*186360 ANNEXIN A7; ANXA7
;;ANNEXIN VII; ANX7;;
SYNEXIN; SNX
*FIELD* TX
DESCRIPTION
read more
Synexin is a calcium-dependent membrane-binding protein that not only
fuses membranes but also acts as a voltage-dependent calcium channel.
CLONING
Burns et al. (1989) isolated and sequenced a set of overlapping cDNA
clones for human synexin. Its derived amino acid sequence shows strong
homology in the C-terminal domain with a previously identified class of
calcium-dependent membrane-binding proteins, including endonexin II
(131230), lipocortin I (151690), calpactin I heavy chain (114085), and
others.
Magendzo et al. (1991) cloned 3 variants of synexin cDNA from a human
fibroblast cDNA library. Sequence analysis indicated that the variants
were formed by alternative splicing and use of alternate polyadenylation
signals. Northern blot analysis of fibroblasts revealed transcripts of
2.0 and 2.4 kb. Using primers designed to differentiate between these 2
forms by PCR, Magendzo et al. (1991) found the larger transcript,
containing a 66-bp exon, in human and monkey brain, heart, and skeletal
muscle. They found the variant lacking this exon in liver, lung, kidney,
spleen, fibroblasts, and placenta. Western blot analysis indicated the
presence of the larger protein in human skeletal muscle and the smaller
protein in lung.
GENE FUNCTION
The ANX7 gene is located on chromosome 10q21, a site long hypothesized
to harbor a tumor suppressor gene or genes associated with prostate and
other cancers. To test this hypothesis, Srivastava et al. (2001)
analyzed the action of the ANX7 gene on colony formation by human tumor
cell lines. They also examined the expression of the ANX7 protein in a
large number of prostate cancers using tumor tissue microarray
technology. Finally, they tested a panel of primary and metastatic
prostate cancers for evidence of loss of heterozygosity (LOH). They
found that human tumor cell proliferation and colony formation were
markedly reduced when the wildtype ANX7 gene was transfected into 2
prostate tumor cell lines. Consistently, analysis of ANX7 protein
expression in human prostate tumor microarrays revealed a significantly
higher rate of loss of ANX7 expression in metastatic and local
recurrences of hormone refractory prostate cancer as compared with
primary tumors (P = 0.0001). Using 4 microsatellite markers at or near
the ANX7 locus and laser capture microdissected tumor cells, 35% of 20
primary prostate tumors showed LOH. The microsatellite marker closest to
the ANX7 locus showed the highest rate of LOH, including 1 homozygous
deletion. Srivastava et al. (2001) concluded that the ANX7 gene exhibits
many biologic and genetic properties expected of a tumor suppressor gene
and may play a role in prostate cancer progression.
Caohuy et al. (1996) present experimental evidence, based on studies of
recombinant human ANXA7 and isolated bovine chromaffin cells, that ANXA7
is a Ca(2+)-dependent GTP binding protein. ANXA7 was active in a
chromaffin granule aggregation assays in the presence of Ca(2+) and GTP,
and was deactivated upon GTP hydrolysis.
GENE STRUCTURE
Shirvan et al. (1994) determined that the synexin gene contains 14
exons, including an alternatively spliced cassette exon, and spans
approximately 34 kb of DNA. Only 5 of the 14 spliced exons are conserved
compared to other annexins; the differences are particularly pronounced
in the exons that encode the C-terminal third and fourth conserved
repeats in the gene product. Shirvan et al. (1994) concluded that the
ANXA7 gene may have diverged from the evolutionary pathway taken by both
ANXA1 and ANXA2.
Zhang-Keck et al. (1994) found that the mouse homolog also contains 14
exons; it spans approximately 30 kb of genomic DNA.
MAPPING
Shirvan et al. (1994) isolated genomic clones of the ANXA7 gene and
assigned the gene to 10q21.1-q21.2 by study of somatic cell hybrids and
by in situ hybridization.
By study of Chinese hamster/mouse somatic cell hybrids and by linkage
analyses in interspecific crosses, Zhang-Keck et al. (1994) demonstrated
that the functional synexin gene is located on mouse chromosome 14 and
that a pseudogene is located on chromosome 10.
ANIMAL MODEL
By gene targeting, Srivastava et al. (1999) developed Anxa7-null mice.
The null phenotype was lethal at embryonic day 10. Heterozygous mice
were viable and fertile, but showed a defect in insulin secretion and an
increased insulin content within isolated pancreatic islets.
Electrooptical recordings suggested that the mutation altered Ca(2+)
release by agonists of inositol trisphosphate.
Using mice with a different genetic background and an alternate strategy
to introduce the null mutation, Herr et al. (2001) developed Anxa7 -/-
mice that were viable, fertile, and showed no obvious defects. Analysis
of insulin secretion from isolated islets revealed no evidence for the
involvement of Anxa7 in Ca(2+)-dependent or cAMP-mediated exocytosis. In
cardiomyocytes, however, they found a functional role for Anxa7 in
electromechanical coupling. Cardiomyocytes from embryonic Anxa7-null
mice displayed intact Ca(2+) homeostasis and unremarkable
excitation-contraction coupling; however, adult Anxa7 -/- mice exhibited
a decrease in frequency-induced cell shortening.
To investigate the mechanism by which the ANX7 gene controls tumor
development, Srivastava et al. (2003) developed an Anx7 +/- knockout
mouse. As hypothesized, these heterozygous mice had a cancer-prone
phenotype. The emerging tumors expressed low levels of Anx7 protein.
Nonetheless, the wildtype Anx7 allele was detectable in tumor tissue
cells. Genome array analysis of hepatocellular carcinoma tissue
indicated that the Anx7 +/- genotype is accompanied by profound
reductions of expression of several other tumor suppressor genes, DNA
repair genes, and apoptosis-related genes. In situ analysis by tissue
imprinting from chromosomes in the primary tumor and spectral
karyotyping analysis of derived cell lines identified chromosomal
instability and clonal chromosomal aberrations. Furthermore, whereas 23%
of the mutant mice developed spontaneous neoplasms, all mice exhibited
growth anomalies, including gender-specific gigantism and organomegaly.
Srivastava et al. (2003) concluded that haploinsufficiency of Anx7
expression drives disease progression to cancer because of genomic
instability through a discrete signaling pathway involving other tumor
suppressor genes, DNA-repair genes, and apoptosis-related genes.
*FIELD* RF
1. Burns, A. L.; Magendzo, K.; Shirvan, A.; Srivastava, M.; Rojas,
E.; Alijani, M. R.; Pollard, H. B.: Calcium channel activity of purified
human synexin and structure of the human synexin gene. Proc. Nat.
Acad. Sci. 86: 3798-3802, 1989.
2. Caohuy, H.; Srivastava, M.; Pollard, H. B.: Membrane fusion protein
synexin (annexin VII) as a Ca(2+)/GTP sensor in exocytotic secretion. Proc.
Nat. Acad. Sci. 93: 10797-10802, 1996.
3. Herr, C.; Smyth, N.; Ullrich, S.; Yun, F.; Sasse, P.; Hescheler,
J.; Fleischmann, B.; Lasek, K.; Brixius, K.; Schwinger, R. H. G.;
Fassler, R.; Schroder, R.; Noegel, A. A.: Loss of annexin A7 leads
to alterations in frequency-induced shortening of isolated murine
cardiomyocytes. Molec. Cell. Biol. 21: 4119-4128, 2001.
4. Magendzo, K.; Shirvan, A.; Cultraro, C.; Srivastava, M.; Pollard,
H. B.; Burns, A. L.: Alternative splicing of human synexin mRNA in
brain, cardiac, and skeletal muscle alters the unique N-terminal domain. J.
Biol. Chem. 266: 3228-3232, 1991.
5. Shirvan, A.; Srivastava, M.; Wang, M. G.; Cultraro, C.; Magendzo,
K.; McBride, O. W.; Pollard, H. B.; Burns, A. L.: Divergent structure
of the human synexin (annexin VII) gene and assignment to chromosome
10. Biochemistry 33: 6888-6901, 1994.
6. Srivastava, M.; Atwater, I.; Glasman, M.; Leighton, X.; Goping,
G.; Caohuy, H.; Miller, G.; Pichel, J.; Westphal, H.; Mears, D.; Rojas,
E.; Pollard, H. B.: Defects in inositol 1,4,5-trisphosphate receptor
expression, Ca(2+) signaling, and insulin secretion in the anx7(+/-)
knockout mouse. Proc. Nat. Acad. Sci. 96: 13783-13788, 1999.
7. Srivastava, M.; Bubendorf, L.; Srikantan, V.; Fossom, L.; Nolan,
L.; Glasman, M.; Leighton, X.; Fehrle, W.; Pittaluga, S.; Raffeld,
M.; Koivisto, P.; Willi, N.; Gasser, T. C.; Kononen, J.; Sauter, G.;
Kallioniemi, O. P.; Srivastava, S.; Pollard, H. B.: ANX7, a candidate
tumor suppressor gene for prostate cancer. Proc. Nat. Acad. Sci. 98:
4575-4580, 2001.
8. Srivastava, M.; Montagna, C.; Leighton, X.; Glasman, M.; Naga,
S.; Eidelman, O.; Ried, T.; Pollard, H. B.: Haploinsufficiency of
Anx7 tumor suppressor gene and consequent genomic instability promotes
tumorigenesis in the Anx7(+/-) mouse. Proc. Nat. Acad. Sci. 100:
14287-14292, 2003.
9. Zhang-Keck, Z.-Y.; Srivastava, M.; Kozak, C. A.; Caohuy, H.; Shirvan,
A.; Burns, A. L.; Pollard, H. B.: Genomic organization and chromosomal
localization of the mouse synexin gene. Biochem. J. 301: 835-845,
1994.
*FIELD* CN
Victor A. McKusick - updated: 12/3/2004
Patricia A. Hartz - updated: 6/13/2002
Victor A. McKusick - updated: 5/14/2001
*FIELD* CD
Victor A. McKusick: 6/7/1989
*FIELD* ED
terry: 05/20/2010
terry: 5/20/2010
tkritzer: 12/8/2004
terry: 12/3/2004
carol: 6/19/2002
terry: 6/13/2002
mcapotos: 5/22/2001
mcapotos: 5/18/2001
terry: 5/14/2001
mgross: 9/17/1999
mark: 2/25/1998
carol: 11/18/1994
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 8/4/1989
carol: 6/7/1989