SOBP_RAT
ID SOBP_RAT Reviewed; 864 AA.
AC A7XYI6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Sine oculis-binding protein homolog;
DE AltName: Full=Jackson circler protein 1;
GN Name=Sobp {ECO:0000250|UniProtKB:Q0P5V2};
GN Synonyms=Jxc1 {ECO:0000312|EMBL:ABF56058.1};
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:0000312|EMBL:ABF56058.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:ABF56058.1};
RA Noben-Trauth K.;
RT "Mutations in Jxc1 are associated with deafness, vestibular deficits and
RT cochlea malformation in the Jackson circler (jc) mutant mouse.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Implicated in development of the cochlea.
CC {ECO:0000250|UniProtKB:Q0P5V2}.
CC -!- SUBUNIT: Interacts (via SIM domains) with SUMO1 and SUMO2.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SOBP family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ503410; ABF56058.1; -; mRNA.
DR RefSeq; NP_001098110.1; NM_001104640.1.
DR RefSeq; XP_006256636.1; XM_006256574.3.
DR AlphaFoldDB; A7XYI6; -.
DR STRING; 10116.ENSRNOP00000000348; -.
DR iPTMnet; A7XYI6; -.
DR PhosphoSitePlus; A7XYI6; -.
DR PaxDb; A7XYI6; -.
DR PRIDE; A7XYI6; -.
DR Ensembl; ENSRNOT00000000348; ENSRNOP00000000348; ENSRNOG00000000316.
DR GeneID; 309860; -.
DR KEGG; rno:309860; -.
DR UCSC; RGD:1560479; rat.
DR CTD; 55084; -.
DR RGD; 1560479; Sobp.
DR eggNOG; ENOG502QZ8A; Eukaryota.
DR GeneTree; ENSGT00940000154164; -.
DR HOGENOM; CLU_012732_0_0_1; -.
DR InParanoid; A7XYI6; -.
DR OMA; MAPCVIS; -.
DR OrthoDB; 184811at2759; -.
DR PhylomeDB; A7XYI6; -.
DR PRO; PR:A7XYI6; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000316; Expressed in skeletal muscle tissue and 12 other tissues.
DR Genevisible; A7XYI6; RN.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032184; F:SUMO polymer binding; ISO:RGD.
DR GO; GO:0048513; P:animal organ development; IBA:GO_Central.
DR GO; GO:0090102; P:cochlea development; ISO:RGD.
DR GO; GO:0050890; P:cognition; ISO:RGD.
DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR InterPro; IPR026092; RAI2/SOBP.
DR PANTHER; PTHR23186; PTHR23186; 1.
DR Pfam; PF15279; SOBP; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..864
FT /note="Sine oculis-binding protein homolog"
FT /id="PRO_0000312234"
FT ZN_FING 142..180
FT /note="FCS-type 1"
FT /evidence="ECO:0000255"
FT ZN_FING 216..256
FT /note="FCS-type 2"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 618..622
FT /note="SUMO interaction motif 1 (SIM); mediates the binding
FT to polysumoylated substrates"
FT /evidence="ECO:0000250"
FT MOTIF 648..652
FT /note="SUMO interaction motif 2 (SIM); mediates the binding
FT to polysumoylated substrates"
FT /evidence="ECO:0000250"
FT COMPBIAS 320..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..749
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0P5V2"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0P5V2"
FT CROSSLNK 672
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:A7XYQ1"
SQ SEQUENCE 864 AA; 91771 MW; C96860E8B24E40EF CRC64;
MAEMEKEGRP PENKRSRKPA HPVKREINEE MKNFAENTMN ELLGWYGYDK VELKDGEDIE
FRSYTTDGES RQHISVLKEN SLPKPKLPED SVISSYNIST GYSGLATGNG LSDSPAGSKD
HGNVPIIVPL IPPPFIKPPA EDEVSNVQIM CAWCQKVGIK RYSLSMGSEV KSFCSEKCFA
ACRRAYFKRN KARDEDGHAE SFPQQHYAKE TPRLAFKNNC ELLVCDWCKH IRHTKEYLDF
GDGERRLQFC SAKCLNQYKM DIFYKETQAN LPAGLCGTLH PHMESKAEGT GVQLLTPDSW
NIPLTDARRK APSPVAAAGQ SQGPGPSSST TVSPSDTANC SVTKIPTPVP KSLPISETPS
IPPVSVQPPA SIGPPLGVPP RSPPMVMTNR GPVPLPIFME QQIIQQIRPP FIRGPPHHAS
NPNSPLSNPM LPGIGPPPGG PRNLGPTSSP MHRPMLSPHI HPPSTPTMPG NPPGLLPPPP
PGAPLPSLPF PPVSMMPNGP MPVPQMMNFG LPSLAPLVPP PTLLVPYPVI VPLPVPIPIP
IPIPHVNDSK PPNGFSSNGE SFVPSAPGDS SAAGGKAGGR SLSPRDSKQG SSKSADSPPG
SSGQALSLAP SERGRGEVVD LTRRAASPAG AGGQPGFAGV LHGPQDGVID LTVGHRARLH
NVIHRALHAH VKAEREPGAA ERRTCGGCRD GHCSPPAAGD PGPGAPAGPE AAAACNVIVN
GTRSAPAEAK GAEPPPEQPP PPAPPKKLLS PEEPAVNELE SVKENNCASN CHLDGEVTKK
LMGEEALAGG DKSDPNLNNP ADEDHAYALR MLPKTGCVIQ PVPKPAEKAA MTPCVISSPM
LSAGPEDLEP PLKRRCLRIR NQNK