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RAB14_PIG
ID   RAB14_PIG               Reviewed;         215 AA.
AC   Q52NJ6;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Ras-related protein Rab-14;
GN   Name=RAB14;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Liu G.Y., Xiong Z.Y.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in membrane trafficking between the Golgi complex
CC       and endosomes during early embryonic development. Regulates the Golgi
CC       to endosome transport of FGFR-containing vesicles during early
CC       development, a key process for developing basement membrane and
CC       epiblast and primitive endoderm lineages during early postimplantation
CC       development. May act by modulating the kinesin KIF16B-cargo association
CC       to endosomes. Regulates, together with its guanine nucleotide exchange
CC       factor DENND6A, the specific endocytic transport of ADAM10, N-
CC       cadherin/CDH2 shedding and cell-cell adhesion (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with KIF16B. Interacts with ZFYVE20 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Recycling endosome
CC       {ECO:0000250|UniProtKB:P61106}. Early endosome membrane
CC       {ECO:0000250|UniProtKB:P61106}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:P61106}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250|UniProtKB:P61106}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Cytoplasmic vesicle, phagosome
CC       {ECO:0000250|UniProtKB:P61106}. Note=Recruited to recycling endosomes
CC       by DENND6A. Recruited to phagosomes containing S.aureus or
CC       M.tuberculosis. {ECO:0000250|UniProtKB:P61106}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AY996809; AAY17505.1; -; mRNA.
DR   RefSeq; NP_001026953.1; NM_001031783.1.
DR   AlphaFoldDB; Q52NJ6; -.
DR   SMR; Q52NJ6; -.
DR   STRING; 9823.ENSSSCP00000005910; -.
DR   PaxDb; Q52NJ6; -.
DR   PeptideAtlas; Q52NJ6; -.
DR   PRIDE; Q52NJ6; -.
DR   GeneID; 595112; -.
DR   KEGG; ssc:595112; -.
DR   CTD; 51552; -.
DR   eggNOG; KOG0097; Eukaryota.
DR   InParanoid; Q52NJ6; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; IEA:InterPro.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:InterPro.
DR   GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006895; P:Golgi to endosome transport; ISS:UniProtKB.
DR   GO; GO:0090382; P:phagosome maturation; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
DR   GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR   CDD; cd04122; Rab14; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR030702; Rab14.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasmic vesicle; Endosome; Golgi apparatus; GTP-binding;
KW   Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P61106"
FT   CHAIN           2..215
FT                   /note="Ras-related protein Rab-14"
FT                   /id="PRO_0000253739"
FT   REGION          188..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           40..48
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         18..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..70
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         124..127
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         154..156
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P61106"
FT   MOD_RES         215
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           213
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           215
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   215 AA;  23927 MW;  B435AAC6F562B007 CRC64;
     MATTPYNYSY IFKYIIIGDM GVGKSCLLHQ FTEKKFMADC PHTIGVEFGT RIIEVSGQKI
     KLQIWDTAGQ ERFRAVTRSY YRGAAGALMV YDITRRSTYN HLSSWLTDAR NLTNPNTVII
     LIGNKADLEA QRDVTYEEAK QFAEENGLLF LEASAKTGEN VEDAFLEAAK KIYQNIQDGS
     LDLNAAESGV QHKPSAPQGG RLTSEPQPQR EGCGC
 
 
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