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YPTC4_CHLRE
ID   YPTC4_CHLRE             Reviewed;         213 AA.
AC   Q39570;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=GTP-binding protein YPTC4;
GN   Name=YPTC4;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cw15;
RX   PubMed=7789809; DOI=10.1016/0378-1119(95)00052-8;
RA   Dietmaier W., Fabry S., Huber H., Schmitt R.;
RT   "Analysis of a family of ypt genes and their products from Chlamydomonas
RT   reinhardtii.";
RL   Gene 158:41-50(1995).
CC   -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; U13167; AAA82726.1; -; Genomic_DNA.
DR   PIR; JC4106; JC4106.
DR   AlphaFoldDB; Q39570; -.
DR   SMR; Q39570; -.
DR   STRING; 3055.EDP02222; -.
DR   eggNOG; KOG0098; Eukaryota.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
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   3: Inferred from homology;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW   Prenylation; Protein transport; Transport.
FT   CHAIN           1..213
FT                   /note="GTP-binding protein YPTC4"
FT                   /id="PRO_0000121294"
FT   REGION          194..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           35..43
FT                   /note="Effector region"
FT                   /evidence="ECO:0000305"
FT   BINDING         13..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61019"
FT   BINDING         61..65
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         119..122
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61019"
FT   BINDING         149..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61019"
FT   LIPID           212
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           213
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  23598 MW;  CB9B3AAAE4E8BA76 CRC64;
     MSYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMINI DGKQIKLQIW
     DTAGQESFRS ITRSYYRGAA GALLVYDITR RETFNHLASW LEDARQHANP NMTIMLIGNK
     CDLTHRRAVT TEEGEQFAKE HGLIFLETSA RTAHNVEEAF INTAKEIYKK IQDGVFDVSN
     ESYGIKVGYG GGNAGPQTVK PGEGGAAKSS SCC
 
 
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