CPNE6_BOVIN
ID CPNE6_BOVIN Reviewed; 557 AA.
AC Q2KHY1;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Copine-6 {ECO:0000305};
DE AltName: Full=Copine VI {ECO:0000250|UniProtKB:Q99829};
GN Name=CPNE6 {ECO:0000250|UniProtKB:O95741};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-dependent phospholipid-binding protein that plays a
CC role in calcium-mediated intracellular processes. Binds phospholipid
CC membranes in a calcium-dependent manner. Plays a role in dendrite
CC formation by melanocytes. {ECO:0000250|UniProtKB:O95741,
CC ECO:0000250|UniProtKB:Q9Z140}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts (via second C2 domain) with OS9 (via C-terminus);
CC this interaction occurs in a calcium-dependent manner in vitro. May
CC interact with NECAB1. {ECO:0000250|UniProtKB:O95741,
CC ECO:0000250|UniProtKB:Q9Z140}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z140}. Cell
CC membrane {ECO:0000250|UniProtKB:Q9Z140}. Endosome
CC {ECO:0000250|UniProtKB:Q9Z140}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:Q9Z140}. Perikaryon
CC {ECO:0000250|UniProtKB:Q9Z140}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9Z140}. Note=Mainly cytoplasmic in absence of
CC calcium. Associated predominantly with membranes in presence of
CC calcium. Translocates to the cell membrane in a calcium-dependent
CC manner. Colocalized with transferrin in intracellular clathrin-coated
CC membrane vesicles in a calcium-dependent manner.
CC {ECO:0000250|UniProtKB:Q9Z140}.
CC -!- DOMAIN: The C2 domain 1 binds phospholipids in a calcium-independent
CC manner and is not necessary for calcium-mediated translocation and
CC association to the plasma membrane. The C2 domain 2 binds phospholipids
CC in a calcium-dependent manner and is necessary for calcium-mediated
CC translocation and association to the plasma membrane. The linker region
CC contributes to the calcium-dependent translocation and association to
CC the plasma membrane. The VWFA domain is necessary for association with
CC intracellular clathrin-coated vesicles in a calcium-dependent manner.
CC {ECO:0000250|UniProtKB:Q9Z140}.
CC -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC112841; AAI12842.1; -; mRNA.
DR RefSeq; NP_001039455.1; NM_001045990.2.
DR RefSeq; XP_005211342.1; XM_005211285.3.
DR RefSeq; XP_010807201.1; XM_010808899.2.
DR AlphaFoldDB; Q2KHY1; -.
DR SMR; Q2KHY1; -.
DR STRING; 9913.ENSBTAP00000002436; -.
DR PaxDb; Q2KHY1; -.
DR PeptideAtlas; Q2KHY1; -.
DR PRIDE; Q2KHY1; -.
DR Ensembl; ENSBTAT00000002436; ENSBTAP00000002436; ENSBTAG00000001870.
DR GeneID; 508059; -.
DR KEGG; bta:508059; -.
DR CTD; 9362; -.
DR VEuPathDB; HostDB:ENSBTAG00000001870; -.
DR VGNC; VGNC:27662; CPNE6.
DR eggNOG; KOG1327; Eukaryota.
DR GeneTree; ENSGT00940000161567; -.
DR HOGENOM; CLU_020452_4_0_1; -.
DR InParanoid; Q2KHY1; -.
DR OMA; PLRCPQG; -.
DR OrthoDB; 1067545at2759; -.
DR TreeFam; TF316419; -.
DR Reactome; R-BTA-1483206; Glycerophospholipid biosynthesis.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000001870; Expressed in Ammon's horn and 28 other tissues.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
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:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
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.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW Differentiation; Endosome; Membrane; Metal-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..557
FT /note="Copine-6"
FT /id="PRO_0000249765"
FT DOMAIN 1..127
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 134..263
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 306..526
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 244..303
FT /note="Linker region"
FT /evidence="ECO:0000250|UniProtKB:Q9Z140"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ SEQUENCE 557 AA; 61865 MW; AF3015C2C3A78F79 CRC64;
MSDPEMAWVP EPPAMTLGAS RVELRVSCHG LLDRDTLTKP HPCVLLKLHS DEQWVEVERT
EVLRSCSSPV FSRVLALEYF FEEKQPLQFH VFDAEDGSTS PRNDTFLGST ECTLGQIVSQ
TKVTKPLLLK NGKNAGKSTI TIVAEEVSGT NDYVQLTFRA HKLDNKDLFS KSDPFMEIYK
TNGDQSDQLV WRTEVVKNNL NPSWEPFRLS LHSLCSCDVH RPLKFLVYDY DSSGKHDFIG
EFTSTFQEMQ EGTANPGQEM QWDCINPKYR DKKKHYKSSG TVVLAQCTVE KVHTFLDYIM
GGCQISFTVA IDFTASNGDP RSSQSLHCLS PRQPNHYLQA LRAVGGICQD YDSDKRFPAF
GFGARIPPNF EVSHDFAINF DPENPECEEI SGVIASYRRC LPQIQLYGPT NVAPIINRVA
GPAQREQSTG QATKYSVLLV LTDGVVSDMA ETRTAIVRAS RLPMSIIIVG VGNADFSDMR
LLDGDDGTLR CPRGVPAARD IVQFVPFRDF KDASPSALAK CVLAEVPRQV VEYYASQGIS
PGAPRPCTPA MTPSPSP
