RTKN_RAT
ID RTKN_RAT Reviewed; 548 AA.
AC Q6V7V2; Q6V7V1;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Rhotekin;
GN Name=Rtkn {ECO:0000312|RGD:727874};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAQ55227.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAQ55227.1};
RA Zhou G., Huang X., Yu L.;
RT "Cloning of rat rhotekin's two splicing isoform.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Mediates Rho signaling to activate NF-kappa-B and may confer
CC increased resistance to apoptosis to cells in gastric tumorigenesis.
CC May play a novel role in the organization of septin structures (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts via its C-terminal region with the TAX1BP3 PDZ
CC domain. This interaction facilitates Rho-mediated activation of the c-
CC Fos serum response element (SRE). Interacts with SEPT9. Specifically
CC binds to GTP-bound RHOA, RHOB and RHOC and inhibits their GTPase
CC activity (By similarity). {ECO:0000250|UniProtKB:Q9BST9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|Ref.1};
CC IsoId=Q6V7V2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|Ref.1};
CC IsoId=Q6V7V2-2; Sequence=VSP_052007;
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DR EMBL; AY348867; AAQ55227.1; -; mRNA.
DR EMBL; AY348868; AAQ55228.1; -; mRNA.
DR RefSeq; NP_908935.1; NM_184046.1. [Q6V7V2-1]
DR RefSeq; XP_008761258.1; XM_008763036.2. [Q6V7V2-1]
DR RefSeq; XP_008761277.1; XM_008763055.2. [Q6V7V2-1]
DR RefSeq; XP_017448493.1; XM_017593004.1. [Q6V7V2-1]
DR RefSeq; XP_017458304.1; XM_017602815.1. [Q6V7V2-1]
DR RefSeq; XP_017458305.1; XM_017602816.1. [Q6V7V2-1]
DR AlphaFoldDB; Q6V7V2; -.
DR SMR; Q6V7V2; -.
DR BioGRID; 255562; 1.
DR IntAct; Q6V7V2; 1.
DR MINT; Q6V7V2; -.
DR STRING; 10116.ENSRNOP00000032233; -.
DR iPTMnet; Q6V7V2; -.
DR PhosphoSitePlus; Q6V7V2; -.
DR PaxDb; Q6V7V2; -.
DR PRIDE; Q6V7V2; -.
DR Ensembl; ENSRNOT00000031964; ENSRNOP00000032233; ENSRNOG00000009022. [Q6V7V2-1]
DR GeneID; 297383; -.
DR KEGG; rno:297383; -.
DR UCSC; RGD:727874; rat. [Q6V7V2-1]
DR CTD; 6242; -.
DR RGD; 727874; Rtkn.
DR eggNOG; ENOG502QRWR; Eukaryota.
DR GeneTree; ENSGT00940000158491; -.
DR HOGENOM; CLU_025066_2_0_1; -.
DR InParanoid; Q6V7V2; -.
DR OMA; KGLPRTW; -.
DR OrthoDB; 497196at2759; -.
DR PhylomeDB; Q6V7V2; -.
DR Reactome; R-RNO-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR PRO; PR:Q6V7V2; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000009022; Expressed in cerebellum and 16 other tissues.
DR ExpressionAtlas; Q6V7V2; baseline.
DR Genevisible; Q6V7V2; RN.
DR GO; GO:0005826; C:actomyosin contractile ring; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005095; F:GTPase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0031106; P:septin ring organization; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR InterPro; IPR012966; AHD.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR030471; RTKN.
DR PANTHER; PTHR21538:SF19; PTHR21538:SF19; 1.
DR Pfam; PF08174; Anillin; 1.
DR SMART; SM00742; Hr1; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS51860; REM_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Coiled coil; GTP-binding; Methylation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..548
FT /note="Rhotekin"
FT /id="PRO_0000233942"
FT DOMAIN 10..85
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 296..403
FT /note="PH"
FT /evidence="ECO:0000255"
FT REGION 83..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BST9"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BST9"
FT MOD_RES 217
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8C6B2"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BST9"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BST9"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BST9"
FT VAR_SEQ 139..372
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_052007"
SQ SEQUENCE 548 AA; 61154 MW; A10A358EC6108B4E CRC64;
MQDRLRILED LNMLYIRQMA LSLEDTELQR KLDHEIRMRE GACKLLAACS QREQALEATK
SLLVCNSRIL SYMGELQRRK EAQVLGKTGR RPSDSVQPPE RSPCRGRVCI SDLRIPLMWK
DTEYFKNKGD LHRWAVFLLL QLGEQIQDTE MVLVDRTLTD ISFQNNAIFA EAGPDFELRL
ELYGACVEEE GALAGAPKRL ATKLSSSLGR SSGKRVRASL DSAGGSGNSP ILLPTPAVGG
PRYHLLAHTT LTLAAVQDGF RTHDLTLTSH EENPAWLPLY GSMCCRLVAQ PLCMTQPTAS
GTLRVQQAGE LQSGTLVHGV LKGTNLFCYW RSEDADSGQE PLFTILINKE TRVRAGELEQ
APEWPFTLSI SNRYGDDEVT NTLQVQSRDA LQSWMEALWQ LFLDMSQWKH CCDEVMKIET
PAPRKPPQAL AKQGSLYHEM AIEPLEDIAA VTDILAQREG TRLEPPPPWL AMFTDQPALR
SSCSPASVPT WTQPLPWGRP RTFSLDAVPA DHSLGPSRSV APLPPQRSPQ SRGFYSKSQL
STWLQSPV
