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