CPNE6_PONAB
ID CPNE6_PONAB Reviewed; 557 AA.
AC Q5R4W6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Copine-6 {ECO:0000305};
DE AltName: Full=Copine VI {ECO:0000250|UniProtKB:Q99829};
GN Name=CPNE6 {ECO:0000250|UniProtKB:O95741};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 (By similarity). Plays a role
CC in dendrite formation by melanocytes (By similarity).
CC {ECO:0000250|UniProtKB:O95741, 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}.
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DR EMBL; CR861125; CAH93200.1; -; mRNA.
DR RefSeq; NP_001127642.1; NM_001134170.1.
DR AlphaFoldDB; Q5R4W6; -.
DR SMR; Q5R4W6; -.
DR STRING; 9601.ENSPPYP00000006455; -.
DR PRIDE; Q5R4W6; -.
DR GeneID; 100174722; -.
DR KEGG; pon:100174722; -.
DR CTD; 9362; -.
DR eggNOG; KOG1327; Eukaryota.
DR InParanoid; Q5R4W6; -.
DR OrthoDB; 1067545at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:InterPro.
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 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 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_0000144847"
FT DOMAIN 2..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; 62028 MW; F75867E0BB1632E5 CRC64;
MSDPEMGWVP EPPTMTLGAS RVELRVSCHG LLDRDTLTKP HPCVLLKLYS DEQWVEVERT
EVLRSCSSPV FSRVLALEYF FEEKQPLQFH VFDAEDGATS PRNDTFLGST ECTLGQIVSQ
TKVTKPLLLK NGKTAGKSTI TIVAEEVSGT NDYVQLTFRA YKLDNKDPFS KSDPFMEIYK
TNEDQSDQLV WRTEVVKNNL NPSWEPFRLS LHSLCSCDVH RPLKFLVYDY DSSGKHDFIG
EFTSTFQEMQ EGTANPGQEM QWDCINPKYR DKKKNYKSSG TVVLAQCTVE KVHTFLDYIM
GGCQISFTVA IDFTASNGDP RSSQSLHCLS PRQPNHYLQA LRAVGGICQD YDSDKRFPAF
GFGARIPPNF EVSHDFAINF DPENPECEEI SGVIASYRRC LPQIQLYGPT NVAPIINRVA
EPAQREQSTG QATKYSVLLV LTDGVVSDMA ETRTAIVRAS RLPMSIIIVG VGNADFSDMR
LLDGDDGPLR CPRGVPAARD IVQFVPFRDF KDAAPSALAK RVLAEVPRQV VEYYASQGIS
PGAPRPCTLA TTPSPSP
