ID   RAC1_STIJA              Reviewed;         192 AA.
AC   A0A286QZ36;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2017, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Ras-related protein Rac1 {ECO:0000305};
DE   AltName: Full=AjRac1 {ECO:0000303|PubMed:28844967};
DE   Flags: Precursor;
GN   Name=RAC1 {ECO:0000312|EMBL:ASU91374.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000312|EMBL:ASU91374.1};
RN   [1] {ECO:0000312|EMBL:ASU91374.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
RX   PubMed=28844967; DOI=10.1016/j.fsi.2017.08.027;
RA   Li K., Liu L., Shang S., Wang Y., Zhan Y., Song J., Zhang X., Chang Y.;
RT   "cDNA cloning, expression and immune function analysis of a novel Rac1 gene
RT   (AjRac1) in the sea cucumber Apostichopus japonicus.";
RL   Fish Shellfish Immunol. 69:218-226(2017).
CC   -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC       active GTP-bound and inactive GDP-bound states.
CC       {ECO:0000250|UniProtKB:P63000}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63000};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P63000}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P63000}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in respiratory tubes and
CC       coelomocytes. Moderate expression in intestinal tissue and body wall.
CC       Low expression in tube feet and longitudinal muscle.
CC       {ECO:0000269|PubMed:28844967}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in the blastula stage with
CC       reduced expression through the rest of development.
CC       {ECO:0000269|PubMed:28844967}.
CC   -!- INDUCTION: By infection with the Gram-negative bacterium V. splendidus.
CC       Following infection, expression is significantly increased at 4 hours
CC       (approximately 15-fold above control), then decreases to control levels
CC       at 8 hours. Expression increases 2-fold above control 12 hours post
CC       infection and remains constant till 48 hours post expression. By 72
CC       hours, expression returns to control levels.
CC       {ECO:0000269|PubMed:28844967}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000305}.
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DR   EMBL; MF196911; ASU91374.1; -; mRNA.
DR   AlphaFoldDB; A0A286QZ36; -.
DR   SMR; A0A286QZ36; -.
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:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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   InterPro; IPR003578; Small_GTPase_Rho.
DR   PANTHER; PTHR24072; PTHR24072; 1.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation.
FT   CHAIN           1..192
FT                   /note="Ras-related protein Rac1"
FT                   /id="PRO_0000444673"
FT   PROPEP          190..192
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P61586"
FT                   /id="PRO_0000444674"
FT   MOTIF           32..40
FT                   /note="Effector region"
FT                   /evidence="ECO:0000305"
FT   BINDING         13..18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P63000"
FT   BINDING         30..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P63000"
FT   BINDING         116..118
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P63000"
FT   BINDING         159..160
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P63000"
FT   MOD_RES         189
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:P63000"
FT   LIPID           189
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P63000"
SQ   SEQUENCE   192 AA;  21476 MW;  B61F67C8FA164585 CRC64;
     MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGRP VNLGLWDTAG
     QEDYDRLRPL SYPQTDVFLI CFSLVSPASY ENVRTKWYPE VSHHCPSTPI ILVGTKLDLR
     DDKETMNKLS ERSLRPIAYP QGLQMQKEIH AVKYLECSAL TQKGLKTVFD EAIRAVLCPP
     AKNKSKRSCQ LL