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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
 
 
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