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Database: UniProt
Entry: Q2KHY1
LinkDB: Q2KHY1
Original site: Q2KHY1 
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   27-MAR-2024, entry version 96.
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}.
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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; 9913-ENSBTAP00000002436; -.
DR   PeptideAtlas; Q2KHY1; -.
DR   Ensembl; ENSBTAT00000002436.5; ENSBTAP00000002436.4; ENSBTAG00000001870.5.
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; YKTNRDQ; -.
DR   OrthoDB; 672483at2759; -.
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 cell types or tissues.
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; 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; cd04048; C2A_Copine; 1.
DR   CDD; cd04047; C2B_Copine; 1.
DR   CDD; cd01459; vWA_copine_like; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 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; COPINE; 1.
DR   PANTHER; PTHR10857:SF5; COPINE-6; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF07002; Copine; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF53300; vWA-like; 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
//
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