ID   UBX11_RAT               Reviewed;         485 AA.
AC   Q8R512;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=UBX domain-containing protein 11;
DE   AltName: Full=Socius;
DE   AltName: Full=UBX domain-containing protein 5;
GN   Name=Ubxn11; Synonyms=Soc, Ubxd5;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RND1; RND2 AND RND3, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RC   STRAIN=Wistar; TISSUE=Testis;
RX   PubMed=11940653; DOI=10.1128/mcb.22.9.2952-2964.2002;
RA   Katoh H., Harada A., Mori K., Negishi M.;
RT   "Socius is a novel Rnd GTPase-interacting protein involved in disassembly
RT   of actin stress fibers.";
RL   Mol. Cell. Biol. 22:2952-2964(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH GNA12 AND GNA13, AND FUNCTION.
RX   PubMed=16202387; DOI=10.1016/j.bbrc.2005.09.097;
RA   Tateiwa K., Katoh H., Negishi M.;
RT   "Socius, a novel binding partner of Galpha12/13, promotes the Galpha12-
RT   induced RhoA activation.";
RL   Biochem. Biophys. Res. Commun. 337:615-620(2005).
CC   -!- FUNCTION: May be involved in the reorganization of actin cytoskeleton
CC       mediated by RND1, RND2 AND RND3. Promotes RHOA activation mediated by
CC       GNA12 and GNA13. {ECO:0000269|PubMed:11940653,
CC       ECO:0000269|PubMed:16202387}.
CC   -!- SUBUNIT: Interacts with GNA12, GNA13, RND1, RND2 AND RND3.
CC       {ECO:0000269|PubMed:11940653, ECO:0000269|PubMed:16202387}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:11940653}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in testis. Also expressed in
CC       lung, brain and thymus. {ECO:0000269|PubMed:11940653}.
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DR   EMBL; AB072920; BAB88905.1; -; mRNA.
DR   EMBL; BC078730; AAH78730.1; -; mRNA.
DR   RefSeq; NP_620208.1; NM_138853.2.
DR   AlphaFoldDB; Q8R512; -.
DR   SMR; Q8R512; -.
DR   IntAct; Q8R512; 4.
DR   STRING; 10116.ENSRNOP00000021342; -.
DR   PhosphoSitePlus; Q8R512; -.
DR   PaxDb; Q8R512; -.
DR   GeneID; 192207; -.
DR   KEGG; rno:192207; -.
DR   UCSC; RGD:620769; rat.
DR   CTD; 91544; -.
DR   RGD; 620769; Ubxn11.
DR   VEuPathDB; HostDB:ENSRNOG00000015476; -.
DR   eggNOG; KOG2086; Eukaryota.
DR   HOGENOM; CLU_044433_0_1_1; -.
DR   InParanoid; Q8R512; -.
DR   OMA; NQVHEME; -.
DR   OrthoDB; 690078at2759; -.
DR   PhylomeDB; Q8R512; -.
DR   TreeFam; TF329799; -.
DR   Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR   Reactome; R-RNO-9696270; RND2 GTPase cycle.
DR   Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR   PRO; PR:Q8R512; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000015476; Expressed in testis and 18 other tissues.
DR   Genevisible; Q8R512; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.420.210; -; 1.
DR   InterPro; IPR036241; NSFL1C_SEP_dom_sf.
DR   InterPro; IPR012989; SEP_domain.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR001012; UBX_dom.
DR   Pfam; PF08059; SEP; 1.
DR   Pfam; PF00789; UBX; 1.
DR   SUPFAM; SSF102848; SSF102848; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS51399; SEP; 1.
DR   PROSITE; PS50033; UBX; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT   CHAIN           1..485
FT                   /note="UBX domain-containing protein 11"
FT                   /id="PRO_0000284923"
FT   DOMAIN          224..288
FT                   /note="SEP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00732"
FT   DOMAIN          386..463
FT                   /note="UBX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          67..143
FT                   /evidence="ECO:0000255"
FT   MOD_RES         479
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D572"
FT   MOD_RES         483
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D572"
SQ   SEQUENCE   485 AA;  54721 MW;  FA6B8C22629BFB45 CRC64;
     MSSPLASLSK TRKVPLESEP VNPGRRGIRI YGDEDEVDMV NDGQDSEEKI SLPSCYGGIG
     RQGLMIHDSE LLTSMARKLQ ELEQQLKARN EEMLSKEQKI LALEDLVQTL QQHQSSTTRE
     EELETQCIQL QRQVGEMERF LNDYGLQWVG EPMDQENSEG KIISESDERD WMKAKKFWKP
     GDSIVPPEVD FDRLLSSLQD LSELVVEGEA QVTPVPGGAQ FRTLEPIPLK LYRNGIMMFD
     GPFRPFYDPY TQRCLRDILD GFFPSELQRL YPDGVPFKVS DLRNQVYPED GLGPFPGEGR
     VVGRQKIRKV TDRVEETSGS RMTAEKFLNR LPKCVIRQGE VIDIRGPIRD TLQNCCPMPV
     RIQEIIVETP ALASERQRTQ ESPNMPVPPL SMLRIKSENG EQAFLLMMRP EDTIGDVRNL
     LAQARDMDSA AFEILSTFPP TVYRDDTVTL QAAGLVPNAT LLLRTRRVLP ANPSFGTDSG
     PGSLP