Full text data of CAP1
CAP1
(CAP)
[Confidence: low (only semi-automatic identification from reviews)]
Adenylyl cyclase-associated protein 1; CAP 1
Adenylyl cyclase-associated protein 1; CAP 1
UniProt
Q01518
ID CAP1_HUMAN Reviewed; 475 AA.
AC Q01518; Q53HR7; Q5T0S1; Q5T0S2; Q6I9U6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-OCT-2010, sequence version 5.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Adenylyl cyclase-associated protein 1;
DE Short=CAP 1;
GN Name=CAP1; Synonyms=CAP;
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 1), AND VARIANTS GLY-229; GLY-236;
RP SER-245; GLY-247; ASP-249 AND ALA-256.
RX PubMed=1406678;
RA Matviw H., Yu G., Young D.;
RT "Identification of a human cDNA encoding a protein that is
RT structurally and functionally related to the yeast adenylyl cyclase-
RT associated CAP proteins.";
RL Mol. Cell. Biol. 12:5033-5040(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLY-229; GLY-236;
RP SER-245; GLY-247; ASP-249 AND ALA-256.
RA Kawamukai M., O'Neill K., Rodgers L., Riggs M., Schaller H.C.,
RA Chalfie M., Field J., Wigler M.;
RT "Genes from metazoans encoding homologs of yeast adenylyl cyclase-
RT associated proteins.";
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP SPLICING.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
RC TISSUE=Kidney;
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 [8]
RP PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-308 AND
RP SER-310, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307; SER-308 AND
RP SER-310, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
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).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-290; SER-295;
RP SER-301; SER-308 AND SER-310, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 319-475.
RX PubMed=15311924; DOI=10.1021/bi049071r;
RA Dodatko T., Fedorov A.A., Grynberg M., Patskovsky Y., Rozwarski D.A.,
RA Jaroszewski L., Aronoff-Spencer E., Kondraskina E., Irving T.,
RA Godzik A., Almo S.C.;
RT "Crystal structure of the actin binding domain of the cyclase-
RT associated protein.";
RL Biochemistry 43:10628-10641(2004).
CC -!- FUNCTION: Directly regulates filament dynamics and has been
CC implicated in a number of complex developmental and morphological
CC processes, including mRNA localization and the establishment of
CC cell polarity.
CC -!- SUBUNIT: Homodimer. Binds actin monomers.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q01518-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q01518-2; Sequence=VSP_036038;
CC -!- SIMILARITY: Belongs to the CAP family.
CC -!- SIMILARITY: Contains 1 C-CAP/cofactor C-like domain.
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DR EMBL; M98474; AAA35648.1; -; mRNA.
DR EMBL; L12168; AAA35507.1; -; mRNA.
DR EMBL; BT007152; AAP35816.1; -; mRNA.
DR EMBL; CR457409; CAG33690.1; -; mRNA.
DR EMBL; AK222513; BAD96233.1; -; mRNA.
DR EMBL; AL512599; CAI11021.1; -; Genomic_DNA.
DR EMBL; AL512599; CAI11022.1; -; Genomic_DNA.
DR EMBL; BC013963; AAH13963.1; -; mRNA.
DR EMBL; BC095440; AAH95440.1; -; mRNA.
DR PIR; A48120; A48120.
DR RefSeq; NP_001099000.1; NM_001105530.1.
DR RefSeq; NP_006358.1; NM_006367.3.
DR RefSeq; XP_005270424.1; XM_005270367.1.
DR RefSeq; XP_005270425.1; XM_005270368.1.
DR RefSeq; XP_005270426.1; XM_005270369.1.
DR RefSeq; XP_005270427.1; XM_005270370.1.
DR RefSeq; XP_005270428.1; XM_005270371.1.
DR RefSeq; XP_005270429.1; XM_005270372.1.
DR RefSeq; XP_005270430.1; XM_005270373.1.
DR RefSeq; XP_005270431.1; XM_005270374.1.
DR RefSeq; XP_005270432.1; XM_005270375.1.
DR UniGene; Hs.370581; -.
DR PDB; 1K8F; X-ray; 2.80 A; A/B/C/D=319-475.
DR PDBsum; 1K8F; -.
DR ProteinModelPortal; Q01518; -.
DR SMR; Q01518; 44-215, 319-475.
DR IntAct; Q01518; 5.
DR MINT; MINT-3024327; -.
DR STRING; 9606.ENSP00000361878; -.
DR PhosphoSite; Q01518; -.
DR DMDM; 308153681; -.
DR OGP; Q01518; -.
DR REPRODUCTION-2DPAGE; IPI00639931; -.
DR PaxDb; Q01518; -.
DR PRIDE; Q01518; -.
DR Ensembl; ENST00000340450; ENSP00000344832; ENSG00000131236.
DR Ensembl; ENST00000372792; ENSP00000361878; ENSG00000131236.
DR Ensembl; ENST00000372797; ENSP00000361883; ENSG00000131236.
DR Ensembl; ENST00000372798; ENSP00000361884; ENSG00000131236.
DR Ensembl; ENST00000372802; ENSP00000361888; ENSG00000131236.
DR Ensembl; ENST00000372805; ENSP00000361891; ENSG00000131236.
DR GeneID; 10487; -.
DR KEGG; hsa:10487; -.
DR UCSC; uc001cez.4; human.
DR CTD; 10487; -.
DR GeneCards; GC01P040505; -.
DR HGNC; HGNC:20040; CAP1.
DR HPA; HPA030124; -.
DR neXtProt; NX_Q01518; -.
DR PharmGKB; PA399; -.
DR eggNOG; NOG254262; -.
DR HOGENOM; HOG000206192; -.
DR HOVERGEN; HBG003080; -.
DR InParanoid; Q01518; -.
DR KO; K17261; -.
DR OMA; GAVPYVQ; -.
DR OrthoDB; EOG7DNNTH; -.
DR PhylomeDB; Q01518; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; CAP1; human.
DR EvolutionaryTrace; Q01518; -.
DR GeneWiki; CAP1; -.
DR GenomeRNAi; 10487; -.
DR NextBio; 39792; -.
DR PRO; PR:Q01518; -.
DR ArrayExpress; Q01518; -.
DR Bgee; Q01518; -.
DR CleanEx; HS_CAP1; -.
DR Genevestigator; Q01518; -.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
DR GO; GO:0001667; P:ameboidal cell migration; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:ProtInc.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.160.20.70; -; 1.
DR InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR InterPro; IPR013992; Adenylate_cyclase-assoc_CAP_N.
DR InterPro; IPR017901; C-CAP_CF_C-like.
DR InterPro; IPR016098; CAP/MinC_C.
DR InterPro; IPR028415; CAP1.
DR InterPro; IPR028417; CAP_CS_C.
DR InterPro; IPR018106; CAP_CS_N.
DR InterPro; IPR006599; CARP_motif.
DR PANTHER; PTHR10652; PTHR10652; 1.
DR PANTHER; PTHR10652:SF1; PTHR10652:SF1; 1.
DR Pfam; PF08603; CAP_C; 1.
DR Pfam; PF01213; CAP_N; 1.
DR SMART; SM00673; CARP; 2.
DR SUPFAM; SSF101278; SSF101278; 1.
DR SUPFAM; SSF69340; SSF69340; 1.
DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR PROSITE; PS01088; CAP_1; 1.
DR PROSITE; PS01089; CAP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Cell membrane; Complete proteome; Direct protein sequencing; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 475 Adenylyl cyclase-associated protein 1.
FT /FTId=PRO_0000205696.
FT DOMAIN 319 453 C-CAP/cofactor C-like.
FT COMPBIAS 218 256 Ala/Pro/Ser-rich.
FT COMPBIAS 230 241 Poly-Pro.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 31 31 Phosphotyrosine (By similarity).
FT MOD_RES 34 34 Phosphoserine.
FT MOD_RES 81 81 N6-acetyllysine.
FT MOD_RES 290 290 Phosphoserine.
FT MOD_RES 295 295 Phosphoserine.
FT MOD_RES 301 301 Phosphoserine.
FT MOD_RES 307 307 Phosphothreonine.
FT MOD_RES 308 308 Phosphoserine.
FT MOD_RES 310 310 Phosphoserine.
FT VAR_SEQ 38 38 Missing (in isoform 2).
FT /FTId=VSP_036038.
FT VARIANT 229 229 C -> G (in dbSNP:rs11207440).
FT /FTId=VAR_028419.
FT VARIANT 236 236 C -> G (in dbSNP:rs6665926).
FT /FTId=VAR_028420.
FT VARIANT 245 245 I -> S (in dbSNP:rs6665933).
FT /FTId=VAR_028421.
FT VARIANT 247 247 C -> G (in dbSNP:rs6665936).
FT /FTId=VAR_028422.
FT VARIANT 249 249 Y -> D (in dbSNP:rs6665937).
FT /FTId=VAR_028423.
FT VARIANT 256 256 S -> A (in dbSNP:rs6665944).
FT /FTId=VAR_028424.
FT CONFLICT 374 374 N -> S (in Ref. 5; BAD96233).
FT STRAND 321 325
FT STRAND 328 333
FT STRAND 340 342
FT STRAND 350 355
FT STRAND 360 374
FT STRAND 376 393
FT STRAND 395 403
FT STRAND 406 412
FT STRAND 414 419
FT STRAND 428 433
FT STRAND 435 443
FT TURN 444 446
FT STRAND 447 452
FT STRAND 456 461
FT STRAND 463 471
SQ SEQUENCE 475 AA; 51901 MW; 7789D1FAC0D1AB7B CRC64;
MADMQNLVER LERAVGRLEA VSHTSDMHRG YADSPSKAGA APYVQAFDSL LAGPVAEYLK
ISKEIGGDVQ KHAEMVHTGL KLERALLVTA SQCQQPAENK LSDLLAPISE QIKEVITFRE
KNRGSKLFNH LSAVSESIQA LGWVAMAPKP GPYVKEMNDA AMFYTNRVLK EYKDVDKKHV
DWVKAYLSIW TELQAYIKEF HTTGLAWSKT GPVAKELSGL PSGPSAGSCP PPPPPCPPPP
PVSTISCSYE SASRSSLFAQ INQGESITHA LKHVSDDMKT HKNPALKAQS GPVRSGPKPF
SAPKPQTSPS PKRATKKEPA VLELEGKKWR VENQENVSNL VIEDTELKQV AYIYKCVNTT
LQIKGKINSI TVDNCKKLGL VFDDVVGIVE IINSKDVKVQ VMGKVPTISI NKTDGCHAYL
SKNSLDCEIV SAKSSEMNVL IPTEGGDFNE FPVPEQFKTL WNGQKLVTTV TEIAG
//
ID CAP1_HUMAN Reviewed; 475 AA.
AC Q01518; Q53HR7; Q5T0S1; Q5T0S2; Q6I9U6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-OCT-2010, sequence version 5.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Adenylyl cyclase-associated protein 1;
DE Short=CAP 1;
GN Name=CAP1; Synonyms=CAP;
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 1), AND VARIANTS GLY-229; GLY-236;
RP SER-245; GLY-247; ASP-249 AND ALA-256.
RX PubMed=1406678;
RA Matviw H., Yu G., Young D.;
RT "Identification of a human cDNA encoding a protein that is
RT structurally and functionally related to the yeast adenylyl cyclase-
RT associated CAP proteins.";
RL Mol. Cell. Biol. 12:5033-5040(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLY-229; GLY-236;
RP SER-245; GLY-247; ASP-249 AND ALA-256.
RA Kawamukai M., O'Neill K., Rodgers L., Riggs M., Schaller H.C.,
RA Chalfie M., Field J., Wigler M.;
RT "Genes from metazoans encoding homologs of yeast adenylyl cyclase-
RT associated proteins.";
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP SPLICING.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP GLY-229; GLY-236; SER-245; GLY-247; ASP-249 AND ALA-256.
RC TISSUE=Kidney;
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 [8]
RP PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-308 AND
RP SER-310, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307; SER-308 AND
RP SER-310, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
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).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-290; SER-295;
RP SER-301; SER-308 AND SER-310, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 319-475.
RX PubMed=15311924; DOI=10.1021/bi049071r;
RA Dodatko T., Fedorov A.A., Grynberg M., Patskovsky Y., Rozwarski D.A.,
RA Jaroszewski L., Aronoff-Spencer E., Kondraskina E., Irving T.,
RA Godzik A., Almo S.C.;
RT "Crystal structure of the actin binding domain of the cyclase-
RT associated protein.";
RL Biochemistry 43:10628-10641(2004).
CC -!- FUNCTION: Directly regulates filament dynamics and has been
CC implicated in a number of complex developmental and morphological
CC processes, including mRNA localization and the establishment of
CC cell polarity.
CC -!- SUBUNIT: Homodimer. Binds actin monomers.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q01518-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q01518-2; Sequence=VSP_036038;
CC -!- SIMILARITY: Belongs to the CAP family.
CC -!- SIMILARITY: Contains 1 C-CAP/cofactor C-like domain.
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DR EMBL; M98474; AAA35648.1; -; mRNA.
DR EMBL; L12168; AAA35507.1; -; mRNA.
DR EMBL; BT007152; AAP35816.1; -; mRNA.
DR EMBL; CR457409; CAG33690.1; -; mRNA.
DR EMBL; AK222513; BAD96233.1; -; mRNA.
DR EMBL; AL512599; CAI11021.1; -; Genomic_DNA.
DR EMBL; AL512599; CAI11022.1; -; Genomic_DNA.
DR EMBL; BC013963; AAH13963.1; -; mRNA.
DR EMBL; BC095440; AAH95440.1; -; mRNA.
DR PIR; A48120; A48120.
DR RefSeq; NP_001099000.1; NM_001105530.1.
DR RefSeq; NP_006358.1; NM_006367.3.
DR RefSeq; XP_005270424.1; XM_005270367.1.
DR RefSeq; XP_005270425.1; XM_005270368.1.
DR RefSeq; XP_005270426.1; XM_005270369.1.
DR RefSeq; XP_005270427.1; XM_005270370.1.
DR RefSeq; XP_005270428.1; XM_005270371.1.
DR RefSeq; XP_005270429.1; XM_005270372.1.
DR RefSeq; XP_005270430.1; XM_005270373.1.
DR RefSeq; XP_005270431.1; XM_005270374.1.
DR RefSeq; XP_005270432.1; XM_005270375.1.
DR UniGene; Hs.370581; -.
DR PDB; 1K8F; X-ray; 2.80 A; A/B/C/D=319-475.
DR PDBsum; 1K8F; -.
DR ProteinModelPortal; Q01518; -.
DR SMR; Q01518; 44-215, 319-475.
DR IntAct; Q01518; 5.
DR MINT; MINT-3024327; -.
DR STRING; 9606.ENSP00000361878; -.
DR PhosphoSite; Q01518; -.
DR DMDM; 308153681; -.
DR OGP; Q01518; -.
DR REPRODUCTION-2DPAGE; IPI00639931; -.
DR PaxDb; Q01518; -.
DR PRIDE; Q01518; -.
DR Ensembl; ENST00000340450; ENSP00000344832; ENSG00000131236.
DR Ensembl; ENST00000372792; ENSP00000361878; ENSG00000131236.
DR Ensembl; ENST00000372797; ENSP00000361883; ENSG00000131236.
DR Ensembl; ENST00000372798; ENSP00000361884; ENSG00000131236.
DR Ensembl; ENST00000372802; ENSP00000361888; ENSG00000131236.
DR Ensembl; ENST00000372805; ENSP00000361891; ENSG00000131236.
DR GeneID; 10487; -.
DR KEGG; hsa:10487; -.
DR UCSC; uc001cez.4; human.
DR CTD; 10487; -.
DR GeneCards; GC01P040505; -.
DR HGNC; HGNC:20040; CAP1.
DR HPA; HPA030124; -.
DR neXtProt; NX_Q01518; -.
DR PharmGKB; PA399; -.
DR eggNOG; NOG254262; -.
DR HOGENOM; HOG000206192; -.
DR HOVERGEN; HBG003080; -.
DR InParanoid; Q01518; -.
DR KO; K17261; -.
DR OMA; GAVPYVQ; -.
DR OrthoDB; EOG7DNNTH; -.
DR PhylomeDB; Q01518; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; CAP1; human.
DR EvolutionaryTrace; Q01518; -.
DR GeneWiki; CAP1; -.
DR GenomeRNAi; 10487; -.
DR NextBio; 39792; -.
DR PRO; PR:Q01518; -.
DR ArrayExpress; Q01518; -.
DR Bgee; Q01518; -.
DR CleanEx; HS_CAP1; -.
DR Genevestigator; Q01518; -.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
DR GO; GO:0001667; P:ameboidal cell migration; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:ProtInc.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.160.20.70; -; 1.
DR InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR InterPro; IPR013992; Adenylate_cyclase-assoc_CAP_N.
DR InterPro; IPR017901; C-CAP_CF_C-like.
DR InterPro; IPR016098; CAP/MinC_C.
DR InterPro; IPR028415; CAP1.
DR InterPro; IPR028417; CAP_CS_C.
DR InterPro; IPR018106; CAP_CS_N.
DR InterPro; IPR006599; CARP_motif.
DR PANTHER; PTHR10652; PTHR10652; 1.
DR PANTHER; PTHR10652:SF1; PTHR10652:SF1; 1.
DR Pfam; PF08603; CAP_C; 1.
DR Pfam; PF01213; CAP_N; 1.
DR SMART; SM00673; CARP; 2.
DR SUPFAM; SSF101278; SSF101278; 1.
DR SUPFAM; SSF69340; SSF69340; 1.
DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR PROSITE; PS01088; CAP_1; 1.
DR PROSITE; PS01089; CAP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Cell membrane; Complete proteome; Direct protein sequencing; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 475 Adenylyl cyclase-associated protein 1.
FT /FTId=PRO_0000205696.
FT DOMAIN 319 453 C-CAP/cofactor C-like.
FT COMPBIAS 218 256 Ala/Pro/Ser-rich.
FT COMPBIAS 230 241 Poly-Pro.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 31 31 Phosphotyrosine (By similarity).
FT MOD_RES 34 34 Phosphoserine.
FT MOD_RES 81 81 N6-acetyllysine.
FT MOD_RES 290 290 Phosphoserine.
FT MOD_RES 295 295 Phosphoserine.
FT MOD_RES 301 301 Phosphoserine.
FT MOD_RES 307 307 Phosphothreonine.
FT MOD_RES 308 308 Phosphoserine.
FT MOD_RES 310 310 Phosphoserine.
FT VAR_SEQ 38 38 Missing (in isoform 2).
FT /FTId=VSP_036038.
FT VARIANT 229 229 C -> G (in dbSNP:rs11207440).
FT /FTId=VAR_028419.
FT VARIANT 236 236 C -> G (in dbSNP:rs6665926).
FT /FTId=VAR_028420.
FT VARIANT 245 245 I -> S (in dbSNP:rs6665933).
FT /FTId=VAR_028421.
FT VARIANT 247 247 C -> G (in dbSNP:rs6665936).
FT /FTId=VAR_028422.
FT VARIANT 249 249 Y -> D (in dbSNP:rs6665937).
FT /FTId=VAR_028423.
FT VARIANT 256 256 S -> A (in dbSNP:rs6665944).
FT /FTId=VAR_028424.
FT CONFLICT 374 374 N -> S (in Ref. 5; BAD96233).
FT STRAND 321 325
FT STRAND 328 333
FT STRAND 340 342
FT STRAND 350 355
FT STRAND 360 374
FT STRAND 376 393
FT STRAND 395 403
FT STRAND 406 412
FT STRAND 414 419
FT STRAND 428 433
FT STRAND 435 443
FT TURN 444 446
FT STRAND 447 452
FT STRAND 456 461
FT STRAND 463 471
SQ SEQUENCE 475 AA; 51901 MW; 7789D1FAC0D1AB7B CRC64;
MADMQNLVER LERAVGRLEA VSHTSDMHRG YADSPSKAGA APYVQAFDSL LAGPVAEYLK
ISKEIGGDVQ KHAEMVHTGL KLERALLVTA SQCQQPAENK LSDLLAPISE QIKEVITFRE
KNRGSKLFNH LSAVSESIQA LGWVAMAPKP GPYVKEMNDA AMFYTNRVLK EYKDVDKKHV
DWVKAYLSIW TELQAYIKEF HTTGLAWSKT GPVAKELSGL PSGPSAGSCP PPPPPCPPPP
PVSTISCSYE SASRSSLFAQ INQGESITHA LKHVSDDMKT HKNPALKAQS GPVRSGPKPF
SAPKPQTSPS PKRATKKEPA VLELEGKKWR VENQENVSNL VIEDTELKQV AYIYKCVNTT
LQIKGKINSI TVDNCKKLGL VFDDVVGIVE IINSKDVKVQ VMGKVPTISI NKTDGCHAYL
SKNSLDCEIV SAKSSEMNVL IPTEGGDFNE FPVPEQFKTL WNGQKLVTTV TEIAG
//