SUSD4_MOUSE
ID SUSD4_MOUSE Reviewed; 490 AA.
AC Q8BH32; Q8VC43;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Sushi domain-containing protein 4;
DE Flags: Precursor;
GN Name=Susd4;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Liver;
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 TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=20348246; DOI=10.2353/ajpath.2010.091036;
RA Tu Z., Cohen M., Bu H., Lin F.;
RT "Tissue distribution and functional analysis of Sushi domain-containing
RT protein 4.";
RL Am. J. Pathol. 176:2378-2384(2010).
CC -!- FUNCTION: Acts as complement inhibitor by disrupting the formation of
CC the classical C3 convertase. Isoform 3 inhibits the classical
CC complement pathway, while membrane-bound isoform 1 inhibits deposition
CC of C3b via both the classical and alternative complement pathways.
CC {ECO:0000250|UniProtKB:Q5VX71, ECO:0000269|PubMed:20348246}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BH32-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BH32-2; Sequence=VSP_020844;
CC -!- TISSUE SPECIFICITY: High expression in brain and eye, with weaker
CC expression in spinal cord and testis. Detected in white matter of brain
CC and in the outer segments of photoreceptors.
CC {ECO:0000269|PubMed:20348246}.
CC -!- MISCELLANEOUS: In contrast some authors report that SUSD4 acts as an
CC activator of the alternative complement pathway, while having no effect
CC on the classical pathway (in vitro) (PubMed:20348246). These
CC contradictory results with human may lie in the differences in protein
CC expression, in this study SUSD4 is expressed in bacteria and not in
CC eukaryotic cells. {ECO:0000269|PubMed:20348246, ECO:0000305}.
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DR EMBL; AK035779; BAC29184.1; -; mRNA.
DR EMBL; AK088629; BAC40464.1; -; mRNA.
DR EMBL; BC021842; AAH21842.2; -; mRNA.
DR CCDS; CCDS15590.1; -. [Q8BH32-1]
DR RefSeq; NP_659045.2; NM_144796.4. [Q8BH32-1]
DR RefSeq; XP_006497124.1; XM_006497061.3.
DR RefSeq; XP_006497126.1; XM_006497063.1. [Q8BH32-2]
DR RefSeq; XP_006497127.1; XM_006497064.3.
DR AlphaFoldDB; Q8BH32; -.
DR SMR; Q8BH32; -.
DR STRING; 10090.ENSMUSP00000082873; -.
DR GlyConnect; 2430; 1 N-Linked glycan (1 site). [Q8BH32-2]
DR GlyGen; Q8BH32; 3 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; Q8BH32; -.
DR PaxDb; Q8BH32; -.
DR PRIDE; Q8BH32; -.
DR ProteomicsDB; 254782; -. [Q8BH32-1]
DR ProteomicsDB; 254783; -. [Q8BH32-2]
DR Antibodypedia; 34634; 80 antibodies from 16 providers.
DR Ensembl; ENSMUST00000085724; ENSMUSP00000082873; ENSMUSG00000038576. [Q8BH32-1]
DR Ensembl; ENSMUST00000153348; ENSMUSP00000119488; ENSMUSG00000038576. [Q8BH32-1]
DR GeneID; 96935; -.
DR KEGG; mmu:96935; -.
DR UCSC; uc007dyk.1; mouse. [Q8BH32-1]
DR CTD; 55061; -.
DR MGI; MGI:2138351; Susd4.
DR VEuPathDB; HostDB:ENSMUSG00000038576; -.
DR eggNOG; ENOG502QU1F; Eukaryota.
DR GeneTree; ENSGT00940000160410; -.
DR HOGENOM; CLU_044351_1_0_1; -.
DR InParanoid; Q8BH32; -.
DR OMA; IIACHEG; -.
DR OrthoDB; 560016at2759; -.
DR PhylomeDB; Q8BH32; -.
DR TreeFam; TF332459; -.
DR BioGRID-ORCS; 96935; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Susd4; mouse.
DR PRO; PR:Q8BH32; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BH32; protein.
DR Bgee; ENSMUSG00000038576; Expressed in ventromedial nucleus of hypothalamus and 179 other tissues.
DR ExpressionAtlas; Q8BH32; baseline and differential.
DR Genevisible; Q8BH32; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045957; P:negative regulation of complement activation, alternative pathway; ISO:MGI.
DR GO; GO:0045959; P:negative regulation of complement activation, classical pathway; ISO:MGI.
DR GO; GO:0030449; P:regulation of complement activation; ISO:MGI.
DR CDD; cd00033; CCP; 4.
DR InterPro; IPR042985; SUSD4.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR47007; PTHR47007; 1.
DR Pfam; PF00084; Sushi; 4.
DR SMART; SM00032; CCP; 4.
DR SUPFAM; SSF57535; SSF57535; 4.
DR PROSITE; PS50923; SUSHI; 4.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Sushi; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..490
FT /note="Sushi domain-containing protein 4"
FT /id="PRO_0000251976"
FT TOPO_DOM 42..319
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 55..119
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 120..179
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 178..239
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 241..304
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 85..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 122..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 147..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 180..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 210..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 243..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 274..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT VAR_SEQ 241
FT /note="E -> EAQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020844"
SQ SEQUENCE 490 AA; 53797 MW; 54FF891F2B620AD8 CRC64;
MYHGMNPSNG DGFLEQQLQQ QQPQSPQRLL AVILWFQLAL CFGPAQLTGG FDDLNVCADP
GVPENGFRTP SGGVFFESSV TRFHCQDGFR LKGSTKRLCM KHFNGTLGWV PSDKPVCIQE
DCRIPQIEDA EIRNKTYRHG EKLVIDCHEG FKIRYPDLYN LVSLCRDDGT WDNLPICQGC
LRPLASSNGY VNISEFQTSF PVGTVIAYRC FPGFKLEGSE NLECLHNLIW SSSPPRCLAL
EVCPLPPMVS HGDFICHPRP CERYNHGTVV EFYCDPGYSL TSDYKYITCQ YGEWFPSYQV
YCIKSEQTWP STHETLLTTW KIVAFTATSV LLVLLLVILA RMFQTKFKAH FPPRGPPRSS
SSDPDFVVVD GVPVMLPTYD EAVNGSSSAL GPGYPASVGQ GCPLPVDDQS PPAYPGSGDT
DTGPGESETC DSTSGSSEML QSLYSPPMCQ GGSRPAPDTP DTISSTAGEV ASTSPGIDIA
DEIPLMEEDP
