SPSB3_MOUSE
ID SPSB3_MOUSE Reviewed; 354 AA.
AC Q571F5; Q3U0T8; Q6GQX9; Q8C6A9; Q8R4S9; Q9D7E0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=SPRY domain-containing SOCS box protein 3;
DE Short=SSB-3;
GN Name=Spsb3; Synonyms=Kiaa4204, Ssb3, Tce1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Friedel E.J., Nicholson S.E., Nicola N.A., Kile B.T., Hilton D.J.;
RT "SOCS box proteins.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, Spleen, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: May be a substrate recognition component of a SCF-like ECS
CC (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase
CC complex which mediates the ubiquitination and subsequent proteasomal
CC degradation of target proteins. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with MET. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q571F5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q571F5-2; Sequence=VSP_023378;
CC Name=3;
CC IsoId=Q571F5-3; Sequence=VSP_023379;
CC Name=4;
CC IsoId=Q571F5-4; Sequence=VSP_023380;
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC BC complex, an adapter module in different E3 ubiquitin ligase
CC complexes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPSB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH72556.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD90159.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF403038; AAL57357.2; -; mRNA.
DR EMBL; AK220234; BAD90159.1; ALT_INIT; mRNA.
DR EMBL; AK009325; BAB26218.1; -; mRNA.
DR EMBL; AK076170; BAC36231.1; -; mRNA.
DR EMBL; AK156579; BAE33763.1; -; mRNA.
DR EMBL; BC072556; AAH72556.1; ALT_FRAME; mRNA.
DR CCDS; CCDS28501.1; -. [Q571F5-1]
DR CCDS; CCDS50022.1; -. [Q571F5-1]
DR RefSeq; NP_001157222.1; NM_001163750.1.
DR RefSeq; NP_001157223.1; NM_001163751.1.
DR RefSeq; NP_081417.2; NM_027141.2. [Q571F5-2]
DR AlphaFoldDB; Q571F5; -.
DR SMR; Q571F5; -.
DR STRING; 10090.ENSMUSP00000024976; -.
DR iPTMnet; Q571F5; -.
DR PhosphoSitePlus; Q571F5; -.
DR PaxDb; Q571F5; -.
DR PRIDE; Q571F5; -.
DR ProteomicsDB; 254536; -. [Q571F5-1]
DR ProteomicsDB; 254537; -. [Q571F5-2]
DR ProteomicsDB; 254538; -. [Q571F5-3]
DR ProteomicsDB; 254539; -. [Q571F5-4]
DR Antibodypedia; 23246; 34 antibodies from 16 providers.
DR Ensembl; ENSMUST00000024976; ENSMUSP00000024976; ENSMUSG00000024160. [Q571F5-2]
DR Ensembl; ENSMUST00000068508; ENSMUSP00000068567; ENSMUSG00000024160. [Q571F5-4]
DR Ensembl; ENSMUST00000117890; ENSMUSP00000112380; ENSMUSG00000024160. [Q571F5-1]
DR Ensembl; ENSMUST00000120943; ENSMUSP00000112492; ENSMUSG00000024160. [Q571F5-1]
DR GeneID; 79043; -.
DR KEGG; mmu:79043; -.
DR UCSC; uc008ayr.2; mouse. [Q571F5-2]
DR UCSC; uc008ayv.1; mouse. [Q571F5-1]
DR CTD; 90864; -.
DR MGI; MGI:1891471; Spsb3.
DR VEuPathDB; HostDB:ENSMUSG00000024160; -.
DR eggNOG; KOG3953; Eukaryota.
DR GeneTree; ENSGT01030000234629; -.
DR HOGENOM; CLU_042284_0_0_1; -.
DR InParanoid; Q571F5; -.
DR OMA; VRDCRCG; -.
DR OrthoDB; 614988at2759; -.
DR TreeFam; TF312822; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 79043; 3 hits in 60 CRISPR screens.
DR ChiTaRS; Spsb3; mouse.
DR PRO; PR:Q571F5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q571F5; protein.
DR Bgee; ENSMUSG00000024160; Expressed in ear vesicle and 243 other tissues.
DR ExpressionAtlas; Q571F5; baseline and differential.
DR Genevisible; Q571F5; MM.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd12876; SPRY_SOCS3; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035754; SPRY_SPSB3.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..354
FT /note="SPRY domain-containing SOCS box protein 3"
FT /id="PRO_0000278779"
FT DOMAIN 85..274
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 264..315
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT REGION 32..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1
FT /note="M -> MGWDTSKVMGVWVVFHTIALGLIEVLRYSSQVLSTM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_023378"
FT VAR_SEQ 198
FT /note="T -> TGRCYLGHGWGWQYSRPPRITPLLLA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023379"
FT VAR_SEQ 242..354
FT /note="VAATRLQNRRFYPMVCSTAAKSSMKVIRSCASSTSLQYLCCYRLRQLRPNSG
FT DTLEGLPLPPGLKQVLHNKLGWVLSMNCNHWKSPVPPPGTATPGAESLETRPCQRKRCR
FT RS -> GASWLPTHMALRLSLPPRSGCYSASKQKVLPDGLLHGCQEQHESHPLLRQLHI
FT PAVPVLLPLAPTAAKFRGHPRGPALATWPQASAA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023380"
FT CONFLICT 245
FT /note="T -> I (in Ref. 1; AAL57357 and 3; BAB26218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 39321 MW; F0AB9473401B6754 CRC64;
MARRTRSSRA WHFVLSAARR DTDARAVALA GSSNWGYDSD GQHSDSDSDP EYSSLPPSIP
SAVPVTGESF CDCEGQNEAT FCNSLHTAHR GKDCRCGEED EDFDWVWDDL NKSSATLLSC
DNRKVSFHME YSCGTAAIRG TKELGDGQHF WEIKMTSPVY GTDMMVGIGT SDVDLDKYHH
TFCSLLGRDE DSWGLSYTGL LHHKGDKTSF SSRFGQGSII GVHLDTWHGT LTFFKNRKCI
GVAATRLQNR RFYPMVCSTA AKSSMKVIRS CASSTSLQYL CCYRLRQLRP NSGDTLEGLP
LPPGLKQVLH NKLGWVLSMN CNHWKSPVPP PGTATPGAES LETRPCQRKR CRRS
