SUSD4_DANRE
ID SUSD4_DANRE Reviewed; 484 AA.
AC E7FEC4;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Sushi domain-containing protein 4;
DE Flags: Precursor;
GN Name=susd4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP DISRUPTION PHENOTYPE.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC defects in development, abnormal locomotion and increased mortality. At
CC 3 days postfertilization morphants have abnormally (delayed) developed
CC eyes. {ECO:0000269|PubMed:20348246}.
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DR EMBL; BX088653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001306062.1; NM_001319133.1.
DR AlphaFoldDB; E7FEC4; -.
DR SMR; E7FEC4; -.
DR STRING; 7955.ENSDARP00000032279; -.
DR PaxDb; E7FEC4; -.
DR Ensembl; ENSDART00000034432; ENSDARP00000032279; ENSDARG00000026335.
DR GeneID; 560304; -.
DR KEGG; dre:560304; -.
DR CTD; 55061; -.
DR ZFIN; ZDB-GENE-110511-1; susd4.
DR eggNOG; ENOG502QU1F; Eukaryota.
DR GeneTree; ENSGT00940000160410; -.
DR HOGENOM; CLU_044351_1_0_1; -.
DR InParanoid; E7FEC4; -.
DR OMA; IIACHEG; -.
DR OrthoDB; 560016at2759; -.
DR PhylomeDB; E7FEC4; -.
DR TreeFam; TF332459; -.
DR PRO; PR:E7FEC4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000026335; Expressed in intestine and 14 other tissues.
DR ExpressionAtlas; E7FEC4; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043009; P:chordate embryonic development; IMP:ZFIN.
DR GO; GO:0045957; P:negative regulation of complement activation, alternative pathway; IBA:GO_Central.
DR GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IBA:GO_Central.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Repeat; Signal;
KW Sushi; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..484
FT /note="Sushi domain-containing protein 4"
FT /id="PRO_0000431993"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 46..110
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 111..168
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 169..230
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 232..295
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 374..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 76..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 113..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 138..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 171..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 201..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 234..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 265..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 484 AA; 53453 MW; B0DF9FB55BBBAD05 CRC64;
MFHHADKGGK KSAFGHPVCG QIILSIILLR PPLLVTAFPV NTVEEQICKD PGFPEHGIRT
PSIGKFFENS VARFSCADGF SLKGPAKIIC TRFYNGSLGW KPSLKPVCLS EDCLPPFIED
ADVTNRTYRP GDSLIISCHE GFQIRYPDTE TMESVCQADG TWDNQPTCQG CLRPLIPPHS
YMNISETKFS VPVGTVVHYQ CFPGYKLEGP ELLECMYNLI WSDTPPRCLD VEACSLPPMI
EHGDYTCHPH PCDRYIHGTV VEYYCYPGYS LANDYKYITC QYGQWFPQMQ LYCVKDETTW
PGFQDSLLTT WKVVACTATS VLLALLLVIT AKMFHYKCKS QQSPSDEPDE SRDPNILVVD
GVAVPLPSYE EAISGNYCQP PNDLPPDGLE SAQHSEEQNP PSYPGHTGSQ NSVPLDTGDV
ENCDSLSDTS ECLQGLQPSS SHPGGLNMSE KTNAITSMEE TASTSPSIDI ADEIPLVEDG
EEDC
