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
