Full text data of CAPZA1
CAPZA1
[Confidence: high (present in two of the MS resources)]
F-actin-capping protein subunit alpha-1 (CapZ alpha-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
F-actin-capping protein subunit alpha-1 (CapZ alpha-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00005969
IPI00005969 F-actin capping protein alpha-1 subunit F-actin capping protein alpha-1 subunit membrane n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 1 cytoskeleton associated n/a found at its expected molecular weight found at molecular weight
IPI00005969 F-actin capping protein alpha-1 subunit F-actin capping protein alpha-1 subunit membrane n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 1 cytoskeleton associated n/a found at its expected molecular weight found at molecular weight
UniProt
P52907
ID CAZA1_HUMAN Reviewed; 286 AA.
AC P52907; Q53FQ6; Q6FHD5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=F-actin-capping protein subunit alpha-1;
DE AltName: Full=CapZ alpha-1;
GN Name=CAPZA1;
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].
RC TISSUE=Placenta;
RX PubMed=9331217;
RX DOI=10.1002/(SICI)1097-0169(1997)38:2<120::AID-CM2>3.0.CO;2-B;
RA Hart M.C., Korshunova Y.O., Cooper J.A.;
RT "Vertebrates have conserved capping protein alpha isoforms with
RT specific expression patterns.";
RL Cell Motil. Cytoskeleton 38:120-132(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastric mucosa;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [7]
RP PROTEIN SEQUENCE OF 2-12 AND 178-192, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [8]
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 [9]
RP IDENTIFICATION IN THE WASH COMPLEX.
RX PubMed=19922875; DOI=10.1016/j.devcel.2009.09.010;
RA Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.;
RT "The Arp2/3 activator WASH controls the fission of endosomes through a
RT large multiprotein complex.";
RL Dev. Cell 17:712-723(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-97, AND MASS
RP 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 [11]
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 [12]
RP STRUCTURE BY NMR OF 265-276 IN COMPLEX WITH S100B AND CALCIUM.
RX PubMed=12470955; DOI=10.1016/S0022-2836(02)01152-X;
RA Inman K.G., Yang R., Rustandi R.R., Miller K.E., Baldisseri D.M.,
RA Weber D.J.;
RT "Solution NMR structure of S100B bound to the high-affinity target
RT peptide TRTK-12.";
RL J. Mol. Biol. 324:1003-1014(2002).
RN [13]
RP STRUCTURE BY NMR OF 265-276 IN COMPLEX WITH S100B AND CALCIUM.
RX PubMed=12480931; DOI=10.1074/jbc.M210622200;
RA McClintock K.A., Shaw G.S.;
RT "A novel S100 target conformation is revealed by the solution
RT structure of the Ca2+-S100B-TRTK-12 complex.";
RL J. Biol. Chem. 278:6251-6257(2003).
CC -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent
CC manner to the fast growing ends of actin filaments (barbed end)
CC thereby blocking the exchange of subunits at these ends. Unlike
CC other capping proteins (such as gelsolin and severin), these
CC proteins do not sever actin filaments.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts
CC with S100A (By similarity). Component of the WASH complex,
CC composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2
CC or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH
CC (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), FAM21 (FAM21A,
CC FAM21B or FAM21C), KIAA1033, KIAA0196 and CCDC53. Interacts with
CC S100B.
CC -!- INTERACTION:
CC Q96B97:SH3KBP1; NbExp=2; IntAct=EBI-355586, EBI-346595;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family.
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DR EMBL; U56637; AAC00533.1; -; mRNA.
DR EMBL; CR407657; CAG28585.1; -; mRNA.
DR EMBL; CR541819; CAG46618.1; -; mRNA.
DR EMBL; BT019364; AAV38171.1; -; mRNA.
DR EMBL; AK223226; BAD96946.1; -; mRNA.
DR EMBL; AL603832; CAI14054.1; -; Genomic_DNA.
DR EMBL; AL929470; CAI14054.1; JOINED; Genomic_DNA.
DR EMBL; AL929470; CAI16528.1; -; Genomic_DNA.
DR EMBL; AL603832; CAI16528.1; JOINED; Genomic_DNA.
DR EMBL; BC000144; AAH00144.1; -; mRNA.
DR PIR; G02639; G02639.
DR RefSeq; NP_006126.1; NM_006135.2.
DR UniGene; Hs.744974; -.
DR PDB; 1MQ1; NMR; -; C/D=265-276.
DR PDB; 1MWN; NMR; -; X/Y=265-276.
DR PDBsum; 1MQ1; -.
DR PDBsum; 1MWN; -.
DR ProteinModelPortal; P52907; -.
DR SMR; P52907; 7-277.
DR IntAct; P52907; 15.
DR MINT; MINT-5001076; -.
DR STRING; 9606.ENSP00000263168; -.
DR PhosphoSite; P52907; -.
DR DMDM; 1705650; -.
DR OGP; P52907; -.
DR REPRODUCTION-2DPAGE; IPI00005969; -.
DR REPRODUCTION-2DPAGE; P52907; -.
DR SWISS-2DPAGE; P52907; -.
DR PaxDb; P52907; -.
DR PeptideAtlas; P52907; -.
DR PRIDE; P52907; -.
DR DNASU; 829; -.
DR Ensembl; ENST00000263168; ENSP00000263168; ENSG00000116489.
DR GeneID; 829; -.
DR KEGG; hsa:829; -.
DR UCSC; uc001ecj.1; human.
DR CTD; 829; -.
DR GeneCards; GC01P113161; -.
DR HGNC; HGNC:1488; CAPZA1.
DR HPA; CAB045963; -.
DR MIM; 601580; gene.
DR neXtProt; NX_P52907; -.
DR PharmGKB; PA26069; -.
DR eggNOG; NOG261759; -.
DR HOGENOM; HOG000036539; -.
DR HOVERGEN; HBG050810; -.
DR InParanoid; P52907; -.
DR KO; K10364; -.
DR OMA; ACDSALR; -.
DR OrthoDB; EOG71ZP25; -.
DR PhylomeDB; P52907; -.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; CAPZA1; human.
DR EvolutionaryTrace; P52907; -.
DR GenomeRNAi; 829; -.
DR NextBio; 3414; -.
DR PRO; PR:P52907; -.
DR Bgee; P52907; -.
DR CleanEx; HS_CAPZA1; -.
DR Genevestigator; P52907; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0008290; C:F-actin capping protein complex; TAS:ProtInc.
DR GO; GO:0071203; C:WASH complex; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0006928; P:cellular component movement; TAS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
DR InterPro; IPR002189; CapZ_alpha.
DR InterPro; IPR017865; F-actin_cap_asu_CS.
DR PANTHER; PTHR10653; PTHR10653; 1.
DR Pfam; PF01267; F-actin_cap_A; 1.
DR PRINTS; PR00191; FACTINCAPA.
DR PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
DR PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin capping; Actin-binding;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 286 F-actin-capping protein subunit alpha-1.
FT /FTId=PRO_0000208624.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 19 19 N6-acetyllysine.
FT MOD_RES 97 97 N6-acetyllysine.
FT CONFLICT 192 192 L -> P (in Ref. 4; BAD96946).
FT HELIX 271 275
SQ SEQUENCE 286 AA; 32923 MW; 0F47ADAB6A3689DD CRC64;
MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD
QFTPVKIEGY EDQVLITEHG DLGNSRFLDP RNKISFKFDH LRKEASDPQP EEADGGLKSW
RESCDSALRA YVKDHYSNGF CTVYAKTIDG QQTIIACIES HQFQPKNFWN GRWRSEWKFT
ITPPTAQVVG VLKIQVHYYE DGNVQLVSHK DVQDSLTVSN EAQTAKEFIK IIENAENEYQ
TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
//
ID CAZA1_HUMAN Reviewed; 286 AA.
AC P52907; Q53FQ6; Q6FHD5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=F-actin-capping protein subunit alpha-1;
DE AltName: Full=CapZ alpha-1;
GN Name=CAPZA1;
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].
RC TISSUE=Placenta;
RX PubMed=9331217;
RX DOI=10.1002/(SICI)1097-0169(1997)38:2<120::AID-CM2>3.0.CO;2-B;
RA Hart M.C., Korshunova Y.O., Cooper J.A.;
RT "Vertebrates have conserved capping protein alpha isoforms with
RT specific expression patterns.";
RL Cell Motil. Cytoskeleton 38:120-132(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastric mucosa;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [7]
RP PROTEIN SEQUENCE OF 2-12 AND 178-192, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [8]
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 [9]
RP IDENTIFICATION IN THE WASH COMPLEX.
RX PubMed=19922875; DOI=10.1016/j.devcel.2009.09.010;
RA Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.;
RT "The Arp2/3 activator WASH controls the fission of endosomes through a
RT large multiprotein complex.";
RL Dev. Cell 17:712-723(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-97, AND MASS
RP 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 [11]
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 [12]
RP STRUCTURE BY NMR OF 265-276 IN COMPLEX WITH S100B AND CALCIUM.
RX PubMed=12470955; DOI=10.1016/S0022-2836(02)01152-X;
RA Inman K.G., Yang R., Rustandi R.R., Miller K.E., Baldisseri D.M.,
RA Weber D.J.;
RT "Solution NMR structure of S100B bound to the high-affinity target
RT peptide TRTK-12.";
RL J. Mol. Biol. 324:1003-1014(2002).
RN [13]
RP STRUCTURE BY NMR OF 265-276 IN COMPLEX WITH S100B AND CALCIUM.
RX PubMed=12480931; DOI=10.1074/jbc.M210622200;
RA McClintock K.A., Shaw G.S.;
RT "A novel S100 target conformation is revealed by the solution
RT structure of the Ca2+-S100B-TRTK-12 complex.";
RL J. Biol. Chem. 278:6251-6257(2003).
CC -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent
CC manner to the fast growing ends of actin filaments (barbed end)
CC thereby blocking the exchange of subunits at these ends. Unlike
CC other capping proteins (such as gelsolin and severin), these
CC proteins do not sever actin filaments.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts
CC with S100A (By similarity). Component of the WASH complex,
CC composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2
CC or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH
CC (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), FAM21 (FAM21A,
CC FAM21B or FAM21C), KIAA1033, KIAA0196 and CCDC53. Interacts with
CC S100B.
CC -!- INTERACTION:
CC Q96B97:SH3KBP1; NbExp=2; IntAct=EBI-355586, EBI-346595;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family.
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DR EMBL; U56637; AAC00533.1; -; mRNA.
DR EMBL; CR407657; CAG28585.1; -; mRNA.
DR EMBL; CR541819; CAG46618.1; -; mRNA.
DR EMBL; BT019364; AAV38171.1; -; mRNA.
DR EMBL; AK223226; BAD96946.1; -; mRNA.
DR EMBL; AL603832; CAI14054.1; -; Genomic_DNA.
DR EMBL; AL929470; CAI14054.1; JOINED; Genomic_DNA.
DR EMBL; AL929470; CAI16528.1; -; Genomic_DNA.
DR EMBL; AL603832; CAI16528.1; JOINED; Genomic_DNA.
DR EMBL; BC000144; AAH00144.1; -; mRNA.
DR PIR; G02639; G02639.
DR RefSeq; NP_006126.1; NM_006135.2.
DR UniGene; Hs.744974; -.
DR PDB; 1MQ1; NMR; -; C/D=265-276.
DR PDB; 1MWN; NMR; -; X/Y=265-276.
DR PDBsum; 1MQ1; -.
DR PDBsum; 1MWN; -.
DR ProteinModelPortal; P52907; -.
DR SMR; P52907; 7-277.
DR IntAct; P52907; 15.
DR MINT; MINT-5001076; -.
DR STRING; 9606.ENSP00000263168; -.
DR PhosphoSite; P52907; -.
DR DMDM; 1705650; -.
DR OGP; P52907; -.
DR REPRODUCTION-2DPAGE; IPI00005969; -.
DR REPRODUCTION-2DPAGE; P52907; -.
DR SWISS-2DPAGE; P52907; -.
DR PaxDb; P52907; -.
DR PeptideAtlas; P52907; -.
DR PRIDE; P52907; -.
DR DNASU; 829; -.
DR Ensembl; ENST00000263168; ENSP00000263168; ENSG00000116489.
DR GeneID; 829; -.
DR KEGG; hsa:829; -.
DR UCSC; uc001ecj.1; human.
DR CTD; 829; -.
DR GeneCards; GC01P113161; -.
DR HGNC; HGNC:1488; CAPZA1.
DR HPA; CAB045963; -.
DR MIM; 601580; gene.
DR neXtProt; NX_P52907; -.
DR PharmGKB; PA26069; -.
DR eggNOG; NOG261759; -.
DR HOGENOM; HOG000036539; -.
DR HOVERGEN; HBG050810; -.
DR InParanoid; P52907; -.
DR KO; K10364; -.
DR OMA; ACDSALR; -.
DR OrthoDB; EOG71ZP25; -.
DR PhylomeDB; P52907; -.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; CAPZA1; human.
DR EvolutionaryTrace; P52907; -.
DR GenomeRNAi; 829; -.
DR NextBio; 3414; -.
DR PRO; PR:P52907; -.
DR Bgee; P52907; -.
DR CleanEx; HS_CAPZA1; -.
DR Genevestigator; P52907; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0008290; C:F-actin capping protein complex; TAS:ProtInc.
DR GO; GO:0071203; C:WASH complex; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0006928; P:cellular component movement; TAS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
DR InterPro; IPR002189; CapZ_alpha.
DR InterPro; IPR017865; F-actin_cap_asu_CS.
DR PANTHER; PTHR10653; PTHR10653; 1.
DR Pfam; PF01267; F-actin_cap_A; 1.
DR PRINTS; PR00191; FACTINCAPA.
DR PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
DR PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin capping; Actin-binding;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 286 F-actin-capping protein subunit alpha-1.
FT /FTId=PRO_0000208624.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 19 19 N6-acetyllysine.
FT MOD_RES 97 97 N6-acetyllysine.
FT CONFLICT 192 192 L -> P (in Ref. 4; BAD96946).
FT HELIX 271 275
SQ SEQUENCE 286 AA; 32923 MW; 0F47ADAB6A3689DD CRC64;
MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD
QFTPVKIEGY EDQVLITEHG DLGNSRFLDP RNKISFKFDH LRKEASDPQP EEADGGLKSW
RESCDSALRA YVKDHYSNGF CTVYAKTIDG QQTIIACIES HQFQPKNFWN GRWRSEWKFT
ITPPTAQVVG VLKIQVHYYE DGNVQLVSHK DVQDSLTVSN EAQTAKEFIK IIENAENEYQ
TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
//
MIM
601580
*RECORD*
*FIELD* NO
601580
*FIELD* TI
*601580 CAPPING PROTEIN, ALPHA-1; CAPZA1
;;CAP PROTEIN, ACTIN, ALPHA-1 SUBUNIT; CAPPA1
read more*FIELD* TX
Barron-Casella et al. (1995) stated that CapZ was identified in chicken
as a nonsevering, barbed-end actin-binding protein composed of alpha and
beta subunits. In the chicken, 2 cDNAs were isolated for the alpha
subunit. The alpha-1 and alpha-2 (CAPZA2; 601571) isoforms, which share
85% identity, are the products of 2 separate genes; 1 gene appears to be
responsible for beta-subunit expression (see CAPZB; 601572). By capping
the barbed end of actin filaments, CapZ regulates the growth of the
actin filament at the barbed end.
Cooper (1999) noted that the STS stSG3463 (GenBank GENBANK G43425),
which has been mapped to chromosome 1, shares sequence identity with the
corresponding region of a CAPZA1 cDNA.
Hart et al. (1997) cloned 3 mouse homologs of CAPZA1, 2 of which are
pseudogenes. They mapped the functional mouse Capza1 gene to chromosome
3 by interspecific backcross analysis.
*FIELD* RF
1. Barron-Casella, E. A.; Torres, M. A.; Scherer, S. W.; Heng, H.
H. Q.; Tsui, L.-C.; Casella, J. F.: Sequence analysis and chromosomal
localization of human Cap Z: conserved residues within the actin-binding
domain may link Cap Z to gelsolin/severin and profilin protein families. J.
Biol. Chem. 270: 21472-21479, 1995.
2. Cooper, J. A.: Personal Communication. St. Louis, Mo. 3/8/1999.
3. Hart, M. C.; Korshunova, Y. O.; Cooper, J. A.: Mapping of the
mouse actin capping protein alpha subunit genes and pseudogenes. Genomics 39:
264-270, 1997.
*FIELD* CN
Patti M. Sherman - updated: 9/8/2000
Rebekah S. Rasooly - updated: 5/21/1998
*FIELD* CD
Victor A. McKusick: 12/16/1996
*FIELD* ED
joanna: 06/10/2004
mgross: 6/10/2004
mcapotos: 9/12/2000
psherman: 9/8/2000
dkim: 6/30/1998
psherman: 5/21/1998
mark: 12/16/1996
*RECORD*
*FIELD* NO
601580
*FIELD* TI
*601580 CAPPING PROTEIN, ALPHA-1; CAPZA1
;;CAP PROTEIN, ACTIN, ALPHA-1 SUBUNIT; CAPPA1
read more*FIELD* TX
Barron-Casella et al. (1995) stated that CapZ was identified in chicken
as a nonsevering, barbed-end actin-binding protein composed of alpha and
beta subunits. In the chicken, 2 cDNAs were isolated for the alpha
subunit. The alpha-1 and alpha-2 (CAPZA2; 601571) isoforms, which share
85% identity, are the products of 2 separate genes; 1 gene appears to be
responsible for beta-subunit expression (see CAPZB; 601572). By capping
the barbed end of actin filaments, CapZ regulates the growth of the
actin filament at the barbed end.
Cooper (1999) noted that the STS stSG3463 (GenBank GENBANK G43425),
which has been mapped to chromosome 1, shares sequence identity with the
corresponding region of a CAPZA1 cDNA.
Hart et al. (1997) cloned 3 mouse homologs of CAPZA1, 2 of which are
pseudogenes. They mapped the functional mouse Capza1 gene to chromosome
3 by interspecific backcross analysis.
*FIELD* RF
1. Barron-Casella, E. A.; Torres, M. A.; Scherer, S. W.; Heng, H.
H. Q.; Tsui, L.-C.; Casella, J. F.: Sequence analysis and chromosomal
localization of human Cap Z: conserved residues within the actin-binding
domain may link Cap Z to gelsolin/severin and profilin protein families. J.
Biol. Chem. 270: 21472-21479, 1995.
2. Cooper, J. A.: Personal Communication. St. Louis, Mo. 3/8/1999.
3. Hart, M. C.; Korshunova, Y. O.; Cooper, J. A.: Mapping of the
mouse actin capping protein alpha subunit genes and pseudogenes. Genomics 39:
264-270, 1997.
*FIELD* CN
Patti M. Sherman - updated: 9/8/2000
Rebekah S. Rasooly - updated: 5/21/1998
*FIELD* CD
Victor A. McKusick: 12/16/1996
*FIELD* ED
joanna: 06/10/2004
mgross: 6/10/2004
mcapotos: 9/12/2000
psherman: 9/8/2000
dkim: 6/30/1998
psherman: 5/21/1998
mark: 12/16/1996