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CPNA1_CAEEL
ID   CPNA1_CAEEL             Reviewed;        1107 AA.
AC   H2KYS8; H2KYS9; H2KYT0; Q7JPE2;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Copine family protein 1;
DE   AltName: Full=Atypical copine family protein 1 {ECO:0000305|PubMed:23283987};
GN   Name=cpna-1 {ECO:0000303|PubMed:23283987, ECO:0000312|WormBase:F31D5.3b};
GN   ORFNames=F31D5.3 {ECO:0000312|WormBase:F31D5.3b};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH UNC-89; UNC-96; PAT-6; LIM-9 AND SCPL-1,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23283987; DOI=10.1091/mbc.e12-06-0478;
RA   Warner A., Xiong G., Qadota H., Rogalski T., Vogl A.W., Moerman D.G.,
RA   Benian G.M.;
RT   "CPNA-1, a copine domain protein, is located at integrin adhesion sites and
RT   is required for myofilament stability in Caenorhabditis elegans.";
RL   Mol. Biol. Cell 24:601-616(2013).
CC   -!- FUNCTION: Involved in the assembly of dense bodies and M lines during
CC       body wall muscle development. Acts by recruiting downstream of
CC       integrin-associated protein pat-6/actopaxin several dense bodies and M
CC       line components including unc-89, lim-9, scpl-1 and unc-96 to integrin-
CC       mediated attachment sites. {ECO:0000269|PubMed:23283987}.
CC   -!- SUBUNIT: May interact (via VWFA domain) with unc-89 (via Ig-like C2-
CC       type 1-3) and unc-96 (via C-terminus); cpna-1 binding sites for unc-89
CC       and unc-96 are different. May interact with pat-6. May interact with
CC       lim-9 (via LIM domains) and with scpl-1 (via FCP1 homology domain).
CC       {ECO:0000269|PubMed:23283987}.
CC   -!- SUBCELLULAR LOCATION: Basal cell membrane
CC       {ECO:0000269|PubMed:23283987}; Single-pass type I membrane protein
CC       {ECO:0000305}. Cytoplasm, myofibril, sarcomere, M line
CC       {ECO:0000269|PubMed:23283987}. Note=Colocalizes with unc-89, unc-112,
CC       pat-3 and pat-6 at the M-line and with alpha-actinin, unc-112, pat-3
CC       and pat-6 in dense bodies. In body wall muscle cells, colocalizes with
CC       beta-integrin pat-3 at integrin adhesion sites.
CC       {ECO:0000269|PubMed:23283987}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=b {ECO:0000312|WormBase:F31D5.3b};
CC         IsoId=H2KYS8-1; Sequence=Displayed;
CC       Name=a {ECO:0000312|WormBase:F31D5.3a};
CC         IsoId=H2KYS8-2; Sequence=VSP_058737;
CC       Name=c {ECO:0000312|WormBase:F31D5.3c};
CC         IsoId=H2KYS8-3; Sequence=VSP_058734, VSP_058735;
CC   -!- TISSUE SPECIFICITY: Expressed in body wall muscles (at protein level).
CC       {ECO:0000269|PubMed:23283987}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos and in adults.
CC       {ECO:0000269|PubMed:23283987}.
CC   -!- DISRUPTION PHENOTYPE: Embryos stop elongation at the 2-fold stage and
CC       have defects in the organization of the myofibril lattice. pat-3, deb-
CC       1, pat-4 and pat-6 are slightly mislocalized in the post 1.5-fold
CC       stage. At the 1.5-fold stage, unc-89 and myo-3 localization is normal.
CC       However, at the 1.75- and 2-fold stages, unc-89 and myo-3 are
CC       mislocalized into large foci within muscle cells.
CC       {ECO:0000269|PubMed:23283987}.
CC   -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
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DR   EMBL; BX284602; CCD64642.1; -; Genomic_DNA.
DR   EMBL; BX284602; CCD64643.1; -; Genomic_DNA.
DR   EMBL; BX284602; CCD64644.1; -; Genomic_DNA.
DR   RefSeq; NP_494736.1; NM_062335.5. [H2KYS8-1]
DR   RefSeq; NP_494737.1; NM_062336.4. [H2KYS8-2]
DR   RefSeq; NP_871985.1; NM_182185.4. [H2KYS8-3]
DR   AlphaFoldDB; H2KYS8; -.
DR   SMR; H2KYS8; -.
DR   IntAct; H2KYS8; 2.
DR   STRING; 6239.F31D5.3b; -.
DR   EPD; H2KYS8; -.
DR   PaxDb; H2KYS8; -.
DR   PeptideAtlas; H2KYS8; -.
DR   EnsemblMetazoa; F31D5.3a.1; F31D5.3a.1; WBGene00006495. [H2KYS8-2]
DR   EnsemblMetazoa; F31D5.3b.1; F31D5.3b.1; WBGene00006495. [H2KYS8-1]
DR   EnsemblMetazoa; F31D5.3c.1; F31D5.3c.1; WBGene00006495. [H2KYS8-3]
DR   GeneID; 173753; -.
DR   KEGG; cel:CELE_F31D5.3; -.
DR   UCSC; F31D5.3a; c. elegans.
DR   CTD; 173753; -.
DR   WormBase; F31D5.3a; CE19827; WBGene00006495; cpna-1. [H2KYS8-2]
DR   WormBase; F31D5.3b; CE19828; WBGene00006495; cpna-1. [H2KYS8-1]
DR   WormBase; F31D5.3c; CE31797; WBGene00006495; cpna-1. [H2KYS8-3]
DR   eggNOG; KOG1327; Eukaryota.
DR   InParanoid; H2KYS8; -.
DR   OMA; MMRIFDE; -.
DR   OrthoDB; 1067545at2759; -.
DR   PRO; PR:H2KYS8; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00006495; Expressed in larva and 3 other tissues.
DR   GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031430; C:M band; IDA:WormBase.
DR   GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
DR   GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:UniProtKB.
DR   GO; GO:0060298; P:positive regulation of sarcomere organization; IMP:UniProtKB.
DR   InterPro; IPR010734; Copine_C.
DR   InterPro; IPR031115; Copine_CPNA-1.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR45751:SF11; PTHR45751:SF11; 1.
DR   Pfam; PF07002; Copine; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Coiled coil; Cytoplasm; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1107
FT                   /note="Copine family protein 1"
FT                   /id="PRO_0000438738"
FT   TOPO_DOM        1..22
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        23..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..1107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          863..1023
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          478..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          67..124
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        478..492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..698
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         450..484
FT                   /note="RDSQLTDYDISDFHAHDEPHYHTVLTPQQLQQNQQ -> GASTVAVVVGSGS
FT                   GVGDVVGDVVDDVAFVEYVTVL (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058734"
FT   VAR_SEQ         485..1107
FT                   /note="Missing (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058735"
FT   VAR_SEQ         767..783
FT                   /note="QIETSIPDSSLLKPVGR -> Q (in isoform a)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058737"
SQ   SEQUENCE   1107 AA;  124605 MW;  E872038FA2A8ADD7 CRC64;
     MVFDARLGYD PDEWEECPEP EHFLVFSGFT RYMLTFAAIA FVYYFFKLLD DKNKKESGEK
     EEPQTSVESV LAKAGDKLHD VKEQVQQHIP ESAEELMREA DQYLKEQAHS VQNNVHQFAE
     QAANKFPSLE VDLNLGHPID ATREKFDTVL SSVNNHLHET KNMDLSPTSR DSTQFEQIPS
     IAPEESAFGH DFEHVPPHLK TAAEQYYAQQ HQPPPVPQHK IVQPVPISPT DQQLLHEFDI
     YDAPAHQRMN QISEQLGQLG QKTPAQLQQL QHAQLAHQQL QQQGVFQPIQ QPSPLQIQTH
     PQQPYFDFSQ LSPASQARYN QQQFVDISQL SPGAGALIAE QQASGAFQPV TKKLGREKRL
     SEQDERALQD WEKEKALLEA DRLKKLLDHE VGGDSTDLDS SQKAYDHFAP ASHISYESHS
     GAAQIQPMTP TAPKRADVPA PQVTSITNVR DSQLTDYDIS DFHAHDEPHY HTVLTPQQLQ
     QNQQQHQQPS AIDRRRTTAD SDDYVKVSEP IYDYPPKGHE APVAEPKRIS PTEAAQLQEL
     YQEYDLGLDL PGVAPIQGVA KPPVQQRTPL QIQQQVVQNV QNQPNMMARQ NSVPESPRTV
     INVPISRKTD VPIQVQQQQN QFSYNVPIQV KDDPRNLATA DLFVQDAQEY VAHQQNQQDK
     GSFVMEEEML SLHEPETGSN KKKLTPKNPS FEATSRQVRT NDVFERIEHD EHDDMTYAPE
     IQSVEIPPDQ MSETSENMID YFDKVAAESE QQIQHLQEQQ NTLKKQQIET SIPDSSLLKP
     VGRAPQILPA FGNRISSNSS LGSAGRSGSG VSSSDVYPYR HLRKQSSLLS VLGVTSMQEM
     LLAITSLDSL SEAMRKAGLE TTNLIFGIDY TASNKYQGEE SFGGRSLHTI HPHVTNPYQQ
     VISILGRTLA PFAGQGRLGV YGFGDAKTGD WSVFNLKGEG GDCRSLDEVL NVYNTVTPTV
     ALSGPTNFAP LIYQAMEICQ KSRDYHILVI IADGQVTNER ATRRAIVQAC QHPLSIIVVG
     VGDGPWDMMR IFDESLPKRP WDNFHFVEFH EIVKKSTNME DGDVKLAVQS LLEIPDQYRC
     ICELGLLDRS IPPRGSEIRR EMMHNPL
 
 
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