Full text data of CAPZA2
CAPZA2
[Confidence: low (only semi-automatic identification from reviews)]
F-actin-capping protein subunit alpha-2 (CapZ alpha-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
F-actin-capping protein subunit alpha-2 (CapZ alpha-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P47755
ID CAZA2_HUMAN Reviewed; 286 AA.
AC P47755;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=F-actin-capping protein subunit alpha-2;
DE AltName: Full=CapZ alpha-2;
GN Name=CAPZA2;
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=Retina;
RX PubMed=7665558; DOI=10.1074/jbc.270.37.21472;
RA Barron-Casella E.A., Torres M.A., Scherer S.W., Heng H.H.Q.,
RA Tsui L.-C., Casella J.F.;
RT "Sequence analysis and chromosomal localization of human Cap Z.
RT Conserved residues within the actin-binding domain may link Cap Z to
RT gelsolin/severin and profilin protein families.";
RL J. Biol. Chem. 270:21472-21479(1995).
RN [2]
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-286.
RC TISSUE=Pancreas;
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 [6]
RP PROTEIN SEQUENCE OF 2-15.
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 [7]
RP PROTEIN SEQUENCE OF 2-15; 20-66; 122-129 AND 179-210, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Mammary carcinoma;
RA Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 20-86; 147-166 AND 179-226, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP INTERACTION WITH RCSD1/CAPZIP, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15850461; DOI=10.1042/BJ20050387;
RA Eyers C.E., McNeill H., Knebel A., Morrice N., Arthur S.J.C.,
RA Cuenda A., Cohen P.;
RT "The phosphorylation of CapZ-interacting protein (CapZIP) by stress-
RT activated protein kinases triggers its dissociation from CapZ.";
RL Biochem. J. 389:127-135(2005).
RN [10]
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 [11]
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 [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).
RN [13]
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).
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. Component of
CC the WASH complex, composed of F-actin-capping protein subunit
CC alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit
CC beta (CAPZB), WASH (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or
CC WASH6P), FAM21 (FAM21A, FAM21B or FAM21C), KIAA1033, KIAA0196 and
CC CCDC53. Interacts with RCSD1/CAPZIP.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U03269; AAA88848.1; -; mRNA.
DR EMBL; BT006735; AAP35381.1; -; mRNA.
DR EMBL; AC002543; AAC60382.1; -; Genomic_DNA.
DR EMBL; BC005338; AAH05338.1; -; mRNA.
DR EMBL; U03851; AAC00534.1; -; mRNA.
DR PIR; G01229; G01229.
DR RefSeq; NP_006127.1; NM_006136.2.
DR UniGene; Hs.446123; -.
DR ProteinModelPortal; P47755; -.
DR SMR; P47755; 8-276.
DR IntAct; P47755; 14.
DR STRING; 9606.ENSP00000354947; -.
DR PhosphoSite; P47755; -.
DR DMDM; 1345695; -.
DR DOSAC-COBS-2DPAGE; P47755; -.
DR OGP; P47755; -.
DR REPRODUCTION-2DPAGE; P47755; -.
DR PaxDb; P47755; -.
DR PeptideAtlas; P47755; -.
DR PRIDE; P47755; -.
DR DNASU; 830; -.
DR Ensembl; ENST00000361183; ENSP00000354947; ENSG00000198898.
DR GeneID; 830; -.
DR KEGG; hsa:830; -.
DR UCSC; uc003vil.3; human.
DR CTD; 830; -.
DR GeneCards; GC07P116451; -.
DR HGNC; HGNC:1490; CAPZA2.
DR HPA; HPA007470; -.
DR MIM; 601571; gene.
DR neXtProt; NX_P47755; -.
DR PharmGKB; PA26071; -.
DR eggNOG; NOG261759; -.
DR HOGENOM; HOG000036539; -.
DR HOVERGEN; HBG050810; -.
DR InParanoid; P47755; -.
DR KO; K10364; -.
DR OMA; WDKVLGY; -.
DR PhylomeDB; P47755; -.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR GeneWiki; CAPZA2; -.
DR GenomeRNAi; 830; -.
DR NextBio; 3418; -.
DR PRO; PR:P47755; -.
DR ArrayExpress; P47755; -.
DR Bgee; P47755; -.
DR CleanEx; HS_CAPZA2; -.
DR Genevestigator; P47755; -.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
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:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0071203; C:WASH complex; IEA:InterPro.
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:ProtInc.
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 Acetylation; Actin capping; Actin-binding; Complete proteome;
KW Direct protein sequencing; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 286 F-actin-capping protein subunit alpha-2.
FT /FTId=PRO_0000208627.
FT MOD_RES 2 2 N-acetylalanine.
SQ SEQUENCE 286 AA; 32949 MW; B5E1B617A38E758B CRC64;
MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNLD
QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRICFKFDH LRKEATDPRP CEVENAVESW
RTSVETALRA YVKEHYPNGV CTVYGKKIDG QQTIIACIES HQFQAKNFWN GRWRSEWKFT
ITPSTTQVVG ILKIQVHYYE DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ
TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
//
ID CAZA2_HUMAN Reviewed; 286 AA.
AC P47755;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=F-actin-capping protein subunit alpha-2;
DE AltName: Full=CapZ alpha-2;
GN Name=CAPZA2;
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=Retina;
RX PubMed=7665558; DOI=10.1074/jbc.270.37.21472;
RA Barron-Casella E.A., Torres M.A., Scherer S.W., Heng H.H.Q.,
RA Tsui L.-C., Casella J.F.;
RT "Sequence analysis and chromosomal localization of human Cap Z.
RT Conserved residues within the actin-binding domain may link Cap Z to
RT gelsolin/severin and profilin protein families.";
RL J. Biol. Chem. 270:21472-21479(1995).
RN [2]
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-286.
RC TISSUE=Pancreas;
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 [6]
RP PROTEIN SEQUENCE OF 2-15.
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 [7]
RP PROTEIN SEQUENCE OF 2-15; 20-66; 122-129 AND 179-210, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Mammary carcinoma;
RA Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 20-86; 147-166 AND 179-226, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP INTERACTION WITH RCSD1/CAPZIP, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15850461; DOI=10.1042/BJ20050387;
RA Eyers C.E., McNeill H., Knebel A., Morrice N., Arthur S.J.C.,
RA Cuenda A., Cohen P.;
RT "The phosphorylation of CapZ-interacting protein (CapZIP) by stress-
RT activated protein kinases triggers its dissociation from CapZ.";
RL Biochem. J. 389:127-135(2005).
RN [10]
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 [11]
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 [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).
RN [13]
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).
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. Component of
CC the WASH complex, composed of F-actin-capping protein subunit
CC alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit
CC beta (CAPZB), WASH (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or
CC WASH6P), FAM21 (FAM21A, FAM21B or FAM21C), KIAA1033, KIAA0196 and
CC CCDC53. Interacts with RCSD1/CAPZIP.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U03269; AAA88848.1; -; mRNA.
DR EMBL; BT006735; AAP35381.1; -; mRNA.
DR EMBL; AC002543; AAC60382.1; -; Genomic_DNA.
DR EMBL; BC005338; AAH05338.1; -; mRNA.
DR EMBL; U03851; AAC00534.1; -; mRNA.
DR PIR; G01229; G01229.
DR RefSeq; NP_006127.1; NM_006136.2.
DR UniGene; Hs.446123; -.
DR ProteinModelPortal; P47755; -.
DR SMR; P47755; 8-276.
DR IntAct; P47755; 14.
DR STRING; 9606.ENSP00000354947; -.
DR PhosphoSite; P47755; -.
DR DMDM; 1345695; -.
DR DOSAC-COBS-2DPAGE; P47755; -.
DR OGP; P47755; -.
DR REPRODUCTION-2DPAGE; P47755; -.
DR PaxDb; P47755; -.
DR PeptideAtlas; P47755; -.
DR PRIDE; P47755; -.
DR DNASU; 830; -.
DR Ensembl; ENST00000361183; ENSP00000354947; ENSG00000198898.
DR GeneID; 830; -.
DR KEGG; hsa:830; -.
DR UCSC; uc003vil.3; human.
DR CTD; 830; -.
DR GeneCards; GC07P116451; -.
DR HGNC; HGNC:1490; CAPZA2.
DR HPA; HPA007470; -.
DR MIM; 601571; gene.
DR neXtProt; NX_P47755; -.
DR PharmGKB; PA26071; -.
DR eggNOG; NOG261759; -.
DR HOGENOM; HOG000036539; -.
DR HOVERGEN; HBG050810; -.
DR InParanoid; P47755; -.
DR KO; K10364; -.
DR OMA; WDKVLGY; -.
DR PhylomeDB; P47755; -.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR GeneWiki; CAPZA2; -.
DR GenomeRNAi; 830; -.
DR NextBio; 3418; -.
DR PRO; PR:P47755; -.
DR ArrayExpress; P47755; -.
DR Bgee; P47755; -.
DR CleanEx; HS_CAPZA2; -.
DR Genevestigator; P47755; -.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
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:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0071203; C:WASH complex; IEA:InterPro.
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:ProtInc.
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 Acetylation; Actin capping; Actin-binding; Complete proteome;
KW Direct protein sequencing; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 286 F-actin-capping protein subunit alpha-2.
FT /FTId=PRO_0000208627.
FT MOD_RES 2 2 N-acetylalanine.
SQ SEQUENCE 286 AA; 32949 MW; B5E1B617A38E758B CRC64;
MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNLD
QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRICFKFDH LRKEATDPRP CEVENAVESW
RTSVETALRA YVKEHYPNGV CTVYGKKIDG QQTIIACIES HQFQAKNFWN GRWRSEWKFT
ITPSTTQVVG ILKIQVHYYE DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ
TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
//
MIM
601571
*RECORD*
*FIELD* NO
601571
*FIELD* TI
*601571 CAPPING PROTEIN, ALPHA-2; CAPZA2
;;CAP PROTEIN, ACTIN, ALPHA-2 SUBUNIT; CAPPA2
read more*FIELD* TX
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
(CAPZA1; 601580) and alpha-2 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. From a human retinal cDNA library, Barron-Casella et al.
(1995) isolated cDNAs that are homologs for the alpha-2 and beta
subunits of chicken CapZ. The derived human alpha subunit shares 95%
amino acid identity with the chicken-alpha subunit; the beta subunit is
99% identical to chicken subunit residues 1-243. The remaining portion
of the human beta subunit (amino acids 244-272) diverges significantly
with only 8 out of 29 C-terminal amino acids conserved between the 2
species. The human alpha-2 gene (symbolized CAPZA2) was mapped to
chromosome 7q31.2-q31.3 by PCR screening of the NIGMS human/rodent
somatic cell hybrid mapping panel 2 and with refinement by PCR analysis
of a human chromosome 7-specific YAC library. One set of overlapping
clones contained both the MET gene (164860) and the CAPZA2 gene. The 2
genes were separated by a maximum distance of 330 kb, with MET
centromeric and WNT2 (147870) and CFTR (602421) distal to CAPZA2.
Hart et al. (1997) cloned the mouse homolog of the CAPZA2 gene. By
interspecific backcross analysis, they mapped the mouse Capza2 gene to
chromosome 6, in a region that shows conservation of synteny with human
7q31.2-q31.3.
*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. 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
Rebekah S. Rasooly - updated: 5/21/1998
*FIELD* CD
Victor A. McKusick: 12/13/1996
*FIELD* ED
joanna: 06/10/2004
mgross: 6/10/2004
dkim: 6/30/1998
psherman: 5/21/1998
carol: 3/28/1998
jenny: 12/20/1996
mark: 12/16/1996
*RECORD*
*FIELD* NO
601571
*FIELD* TI
*601571 CAPPING PROTEIN, ALPHA-2; CAPZA2
;;CAP PROTEIN, ACTIN, ALPHA-2 SUBUNIT; CAPPA2
read more*FIELD* TX
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
(CAPZA1; 601580) and alpha-2 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. From a human retinal cDNA library, Barron-Casella et al.
(1995) isolated cDNAs that are homologs for the alpha-2 and beta
subunits of chicken CapZ. The derived human alpha subunit shares 95%
amino acid identity with the chicken-alpha subunit; the beta subunit is
99% identical to chicken subunit residues 1-243. The remaining portion
of the human beta subunit (amino acids 244-272) diverges significantly
with only 8 out of 29 C-terminal amino acids conserved between the 2
species. The human alpha-2 gene (symbolized CAPZA2) was mapped to
chromosome 7q31.2-q31.3 by PCR screening of the NIGMS human/rodent
somatic cell hybrid mapping panel 2 and with refinement by PCR analysis
of a human chromosome 7-specific YAC library. One set of overlapping
clones contained both the MET gene (164860) and the CAPZA2 gene. The 2
genes were separated by a maximum distance of 330 kb, with MET
centromeric and WNT2 (147870) and CFTR (602421) distal to CAPZA2.
Hart et al. (1997) cloned the mouse homolog of the CAPZA2 gene. By
interspecific backcross analysis, they mapped the mouse Capza2 gene to
chromosome 6, in a region that shows conservation of synteny with human
7q31.2-q31.3.
*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. 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
Rebekah S. Rasooly - updated: 5/21/1998
*FIELD* CD
Victor A. McKusick: 12/13/1996
*FIELD* ED
joanna: 06/10/2004
mgross: 6/10/2004
dkim: 6/30/1998
psherman: 5/21/1998
carol: 3/28/1998
jenny: 12/20/1996
mark: 12/16/1996