CPNE5_MOUSE
ID CPNE5_MOUSE Reviewed; 593 AA.
AC Q8JZW4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Copine-5 {ECO:0000305};
DE AltName: Full=Copine V {ECO:0000250|UniProtKB:Q99829, ECO:0000312|MGI:MGI:2385908};
GN Name=Cpne5 {ECO:0000312|MGI:MGI:2385908};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18614158; DOI=10.1016/j.brainres.2008.05.051;
RA Ding X., Jin Y., Wu Y., Wu Y., Wu H., Xiong L., Song X., Liu S., Fan W.,
RA Fan M.;
RT "Localization and cellular distribution of CPNE5 in embryonic mouse
RT brain.";
RL Brain Res. 1224:20-28(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-140, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Probable calcium-dependent phospholipid-binding protein that
CC may play a role in calcium-mediated intracellular processes. Plays a
CC role in dendrite formation by melanocytes.
CC {ECO:0000250|UniProtKB:Q99829, ECO:0000250|UniProtKB:Q9HCH3}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:18614158}. Cell
CC projection {ECO:0000269|PubMed:18614158}.
CC -!- TISSUE SPECIFICITY: Expressed in the cerebra and cerebellum of newborn
CC brain. Expressed in the eye, lung and muscles but weakly expressed in
CC the adult brain (at protein level) (PubMed:18614158).
CC {ECO:0000269|PubMed:18614158}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the ventricular zone and
CC subventricular zone areas, in the tectum, frontal cortex, ganglionic
CC eminence, dorsal thalamus, hippocampus and tegmentum of the embryonic
CC brain from 12.5 to 14.5 dpc. Expressed in neural progenitor cells (at
CC protein level). Expressed in the embryonic brain from 10.5 to 17.5 dpc.
CC Expressed in the telencephalon, mesencephalon and rhombencephalon areas
CC from 11.5 to 12.5 dpc. Expressed in the developing central nervous
CC system (CNS), such as the frontal cortex, hypothalamus and ventricular
CC zones along the IV ventricle and aquaeductus mesencephali at 13.5 dpc
CC (PubMed:18614158). {ECO:0000269|PubMed:18614158}.
CC -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
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DR EMBL; AK044042; BAC31750.1; -; mRNA.
DR EMBL; BC036971; AAH36971.1; -; mRNA.
DR CCDS; CCDS28592.1; -.
DR RefSeq; NP_694806.1; NM_153166.2.
DR AlphaFoldDB; Q8JZW4; -.
DR SMR; Q8JZW4; -.
DR BioGRID; 232154; 1.
DR STRING; 10090.ENSMUSP00000024805; -.
DR iPTMnet; Q8JZW4; -.
DR PhosphoSitePlus; Q8JZW4; -.
DR jPOST; Q8JZW4; -.
DR MaxQB; Q8JZW4; -.
DR PaxDb; Q8JZW4; -.
DR PeptideAtlas; Q8JZW4; -.
DR PRIDE; Q8JZW4; -.
DR ProteomicsDB; 283815; -.
DR Antibodypedia; 29719; 106 antibodies from 20 providers.
DR DNASU; 240058; -.
DR Ensembl; ENSMUST00000024805; ENSMUSP00000024805; ENSMUSG00000024008.
DR GeneID; 240058; -.
DR KEGG; mmu:240058; -.
DR UCSC; uc008bsj.2; mouse.
DR CTD; 57699; -.
DR MGI; MGI:2385908; Cpne5.
DR VEuPathDB; HostDB:ENSMUSG00000024008; -.
DR eggNOG; KOG1327; Eukaryota.
DR GeneTree; ENSGT00940000156194; -.
DR HOGENOM; CLU_020452_3_2_1; -.
DR InParanoid; Q8JZW4; -.
DR OMA; FIGDYTT; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; Q8JZW4; -.
DR TreeFam; TF316419; -.
DR BioGRID-ORCS; 240058; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Cpne5; mouse.
DR PRO; PR:Q8JZW4; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8JZW4; protein.
DR Bgee; ENSMUSG00000024008; Expressed in caudate-putamen and 170 other tissues.
DR ExpressionAtlas; Q8JZW4; baseline and differential.
DR Genevisible; Q8JZW4; MM.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR CDD; cd04047; C2B_Copine; 1.
DR CDD; cd01459; vWA_copine_like; 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.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell projection; Differentiation; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..593
FT /note="Copine-5"
FT /id="PRO_0000144844"
FT DOMAIN 2..134
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 161..284
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 328..554
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 562..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..584
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH3"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 593 AA; 65592 MW; 0B0BF66A852EACC2 CRC64;
MEQPEDMASL SEFDSLAGSI PATKVEITVS CRNLLDKDMF SKSDPLCVMY TQGMENKQWR
EFGRTEVIDN TLNPDFVRKF IVDYFFEEKQ NLRFDLYDVD SKSPDLSKHD FLGQAFCTLG
EIVGSSGSRL EKPLTIGTFS LNSRTGKPMP AVSNGGVPGK KCGTIILSAE ELSNCRDVAT
MQFCANKLDK KDFFGKSDPF LVFYRSNEDG TFTICHKTEV MKNTLNPVWQ TFSIPVRALC
NGDYDRTIKV EVYDWDRDGS HDFIGEFTTS YRELARGQSQ FNIYEVINPK KKMKKKKYVN
SGTVTLLSFA VESESTFLDY IKGGTQINFT VAIDFTASNG NPSQSTSLHY MSPYQLNAYA
LALTAVGEII QHYDSDKMFP ALGFGAKLPP DGRVSHEFPL NGNQENPSCC GIDGILEAYH
SSLRTVQLYG PTNFAPVVTH VARNAAAVQD GSQYSVLLII TDGVISDMAQ TKEAIVNAAK
LPMSIIIVGV GQAEFDAMVE LDGDDVRISS RGKLAERDIV QFVPFRDYVD RTGNHVLSMA
RLARDVLAEI PDQLVSYMKA QGIRPRPPPA APAQSPPQSP AHSPPGSPVH THI
