CPNA_DICDI
ID CPNA_DICDI Reviewed; 600 AA.
AC Q7YXU4; Q54CC8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Copine-A;
GN Name=cpnA; ORFNames=DDB_G0293008;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=16343335; DOI=10.1186/1471-2121-6-46;
RA Damer C.K., Bayeva M., Hahn E.S., Rivera J., Socec C.I.;
RT "Copine A, a calcium-dependent membrane-binding protein, transiently
RT localizes to the plasma membrane and intracellular vacuoles in
RT Dictyostelium.";
RL BMC Cell Biol. 6:46-46(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17259548; DOI=10.1128/ec.00322-06;
RA Damer C.K., Bayeva M., Kim P.S., Ho L.K., Eberhardt E.S., Socec C.I.,
RA Lee J.S., Bruce E.A., Goldman-Yassen A.E., Naliboff L.C.;
RT "Copine A is required for cytokinesis, contractile vacuole function, and
RT development in Dictyostelium.";
RL Eukaryot. Cell 6:430-442(2007).
CC -!- FUNCTION: Required for cytokinesis, contractile vacuole function and
CC development. {ECO:0000269|PubMed:17259548}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16343335}. Membrane
CC {ECO:0000269|PubMed:16343335}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16343335}. Note=In starved cells it binds
CC transiently and in a calcium-dependent manner to the plasma membrane
CC and intracellular vacuoles. In some cells, the transient membrane
CC localization is observed to occur multiple times in an oscillatory
CC manner over several minutes. Also found to be associated to the plasma
CC membrane, contractile vacuoles, organelles of the endolysosomal pathway
CC and phagosomes.
CC -!- DEVELOPMENTAL STAGE: Expressed at relatively high levels in vegetative
CC cells. The expression goes down at the 2th hour of development and
CC increase slightly up to the 8th hour, it then goes down until the 12th
CC hour where it increase gain to reach a maximal value at the 16th hour.
CC {ECO:0000269|PubMed:17259548}.
CC -!- DISRUPTION PHENOTYPE: Cells exhibit normal growth rates and a slight
CC cytokinesis defect. When placed in starvation conditions these cells
CC appear to aggregate into mounds and form fingers with normal timing;
CC however, they are delayed or arrested in the finger stage. When placed
CC in water the cells forme unusually large contractile vacuoles,
CC indicating a defect in contractile vacuole function.
CC {ECO:0000269|PubMed:17259548}.
CC -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
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DR EMBL; AY332759; AAP92687.1; -; mRNA.
DR EMBL; AAFI02000199; EAL60856.1; -; Genomic_DNA.
DR RefSeq; XP_629291.1; XM_629289.1.
DR AlphaFoldDB; Q7YXU4; -.
DR SMR; Q7YXU4; -.
DR STRING; 44689.DDB0215368; -.
DR PaxDb; Q7YXU4; -.
DR EnsemblProtists; EAL60856; EAL60856; DDB_G0293008.
DR GeneID; 8629014; -.
DR KEGG; ddi:DDB_G0293008; -.
DR dictyBase; DDB_G0293008; cpnA.
DR eggNOG; KOG1327; Eukaryota.
DR HOGENOM; CLU_020452_3_2_1; -.
DR InParanoid; Q7YXU4; -.
DR OMA; EMAAQCV; -.
DR PhylomeDB; Q7YXU4; -.
DR Reactome; R-DDI-1483206; Glycerophospholipid biosynthesis.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-9013406; RHOQ GTPase cycle.
DR PRO; PR:Q7YXU4; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0031164; C:contractile vacuolar membrane; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0031901; C:early endosome membrane; IDA:dictyBase.
DR GO; GO:0031902; C:late endosome membrane; IDA:dictyBase.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:dictyBase.
DR GO; GO:0070177; P:contractile vacuole discharge; IMP:dictyBase.
DR GO; GO:0033298; P:contractile vacuole organization; IMP:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0006971; P:hypotonic response; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0045920; P:negative regulation of exocytosis; IMP:dictyBase.
DR GO; GO:0046956; P:positive phototaxis; IMP:dictyBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:dictyBase.
DR GO; GO:0031157; P:regulation of aggregate size involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0044656; P:regulation of post-lysosomal vacuole size; IMP:dictyBase.
DR GO; GO:0060359; P:response to ammonium ion; IMP:dictyBase.
DR GO; GO:0051592; P:response to calcium ion; IMP:dictyBase.
DR GO; GO:0031149; P:sorocarp stalk cell differentiation; IMP:dictyBase.
DR GO; GO:0043052; P:thermotaxis; IMP:dictyBase.
DR CDD; cd04047; C2B_Copine; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037768; C2B_Copine.
DR InterPro; IPR045052; Copine.
DR InterPro; IPR010734; Copine_C.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10857; PTHR10857; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF07002; Copine; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50004; C2; 2.
PE 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Membrane; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..600
FT /note="Copine-A"
FT /id="PRO_0000330654"
FT DOMAIN 1..111
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 116..246
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 286..503
FT /note="VWFA"
FT REGION 535..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ SEQUENCE 600 AA; 65878 MW; 04B6F0404C6A5057 CRC64;
MNLKPPTSKV ELRIKCHKIL DKDTLSKSDP RASVYEKDRA GQFRLIGKTE TIQNQLNPEF
KTPIVIDYRF EEIQVLKFEI HDVDKNDEDF IGDASCTLTS ILSKPGQTVC LQLLTKSGKH
AGSMTVIAEE IKNTLQTIKF NLIGKKFDKK DLFGAGCDPY LIISRKVPST NTFVKIYESQ
VQKGTLNPVF SGIEMKLEEL CGGDMQREIK FEFYDWDRIG KHDYIGEFHT NAQELLQPNQ
AFNVINSHKQ EKKSGYKNSG TVSVSDAVIE REYNFLEYIM GGCQMNLIVG IDCTASNGDS
NDPNSLHYKN AQGLNQYANA ICSVGNVIVP YTTTPLIPVY GFGGIMPGQS EVSHCFPMTL
NASNTLCCGV NGVLDCYYDN ISKIQLHGPT YFAPLINMAA RYASQGQSQS NQKYTILMII
TDGEILDADN TIDAIVKSSG LPLSIIIVGV GNANFTNMNI LDGDDAALQS GGVRAERDIV
QFVAMRDYLN RPNELAAEVL REIPTQFLSF MKKYKFRPNP PPPPPPVIIG APPQYDNPTT
TTTATSPSTG IDLNKGSNVG LNLTKTESSP SPSGGAGIDL NKGSVVDITK GVSNVSLEKN
