SUSD2_MOUSE
ID SUSD2_MOUSE Reviewed; 820 AA.
AC Q9DBX3; Q8BY19; Q8BYN0; Q8BYZ3; Q8BYZ9; Q8BZQ4; Q8C179;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Sushi domain-containing protein 2;
DE Flags: Precursor;
GN Name=Susd2;
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Epididymis, Hypothalamus, Lung, Skin, Thymus, and Vagina;
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 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-159.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP STRUCTURE BY NMR OF 16-86, AND DISULFIDE BONDS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-041, a SMB-like domain from mouse cDNA.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [6]
RP FUNCTION.
RX PubMed=23131994; DOI=10.1158/1541-7786.mcr-12-0501-t;
RA Watson A.P., Evans R.L., Egland K.A.;
RT "Multiple functions of sushi domain containing 2 (SUSD2) in breast
RT tumorigenesis.";
RL Mol. Cancer Res. 11:74-85(2013).
CC -!- FUNCTION: May be a cytokine receptor for C10ORF99. May be a tumor
CC suppressor; together with C10ORF99 has a growth inhibitory effect on
CC colon cancer cells which includes G1 cell cycle arrest (By similarity).
CC May play a role in breast tumorigenesis (PubMed:23131994).
CC {ECO:0000250|UniProtKB:Q9UGT4, ECO:0000269|PubMed:23131994}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UGT4};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9DBX3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DBX3-2; Sequence=VSP_020426;
CC Name=3;
CC IsoId=Q9DBX3-3; Sequence=VSP_020425;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29714.1; Type=Frameshift; Evidence={ECO:0000305};
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; AK038944; BAC30177.1; -; mRNA.
DR EMBL; AK167155; BAE39296.1; -; mRNA.
DR EMBL; AK033823; BAC28486.1; -; mRNA.
DR EMBL; AK037127; BAC29714.1; ALT_FRAME; mRNA.
DR EMBL; AK028817; BAC26135.1; -; mRNA.
DR EMBL; AK004703; BAB23488.1; -; mRNA.
DR EMBL; AK037059; BAC29689.1; -; mRNA.
DR EMBL; AK042469; BAC31269.1; -; mRNA.
DR EMBL; BC026837; AAH26837.1; -; mRNA.
DR CCDS; CCDS23929.1; -. [Q9DBX3-1]
DR CCDS; CCDS48600.1; -. [Q9DBX3-2]
DR RefSeq; NP_001156385.1; NM_001162913.1. [Q9DBX3-2]
DR RefSeq; NP_082166.3; NM_027890.5. [Q9DBX3-1]
DR PDB; 2CQW; NMR; -; A=16-86.
DR PDBsum; 2CQW; -.
DR AlphaFoldDB; Q9DBX3; -.
DR SMR; Q9DBX3; -.
DR STRING; 10090.ENSMUSP00000093197; -.
DR GlyGen; Q9DBX3; 3 sites.
DR iPTMnet; Q9DBX3; -.
DR PhosphoSitePlus; Q9DBX3; -.
DR EPD; Q9DBX3; -.
DR jPOST; Q9DBX3; -.
DR MaxQB; Q9DBX3; -.
DR PaxDb; Q9DBX3; -.
DR PeptideAtlas; Q9DBX3; -.
DR PRIDE; Q9DBX3; -.
DR ProteomicsDB; 254499; -. [Q9DBX3-1]
DR ProteomicsDB; 254500; -. [Q9DBX3-2]
DR ProteomicsDB; 254501; -. [Q9DBX3-3]
DR Antibodypedia; 284; 335 antibodies from 22 providers.
DR DNASU; 71733; -.
DR Ensembl; ENSMUST00000077610; ENSMUSP00000076802; ENSMUSG00000006342. [Q9DBX3-2]
DR Ensembl; ENSMUST00000095541; ENSMUSP00000093197; ENSMUSG00000006342. [Q9DBX3-1]
DR GeneID; 71733; -.
DR KEGG; mmu:71733; -.
DR UCSC; uc007fqt.2; mouse. [Q9DBX3-1]
DR UCSC; uc011xgq.1; mouse. [Q9DBX3-2]
DR CTD; 56241; -.
DR MGI; MGI:1918983; Susd2.
DR VEuPathDB; HostDB:ENSMUSG00000006342; -.
DR eggNOG; KOG4291; Eukaryota.
DR GeneTree; ENSGT00730000110943; -.
DR HOGENOM; CLU_019295_0_0_1; -.
DR InParanoid; Q9DBX3; -.
DR OMA; PFTISMD; -.
DR OrthoDB; 668024at2759; -.
DR PhylomeDB; Q9DBX3; -.
DR TreeFam; TF321438; -.
DR BioGRID-ORCS; 71733; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Susd2; mouse.
DR EvolutionaryTrace; Q9DBX3; -.
DR PRO; PR:Q9DBX3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9DBX3; protein.
DR Bgee; ENSMUSG00000006342; Expressed in epithelium of lens and 161 other tissues.
DR Genevisible; Q9DBX3; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; ISO:MGI.
DR GO; GO:0051782; P:negative regulation of cell division; ISO:MGI.
DR CDD; cd00033; CCP; 1.
DR InterPro; IPR005533; AMOP_dom.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF03782; AMOP; 1.
DR Pfam; PF01033; Somatomedin_B; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM00723; AMOP; 1.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF57535; SSF57535; 1.
DR SUPFAM; SSF90188; SSF90188; 1.
DR PROSITE; PS50856; AMOP; 1.
DR PROSITE; PS00524; SMB_1; 1.
DR PROSITE; PS50958; SMB_2; 1.
DR PROSITE; PS50923; SUSHI; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Signal; Sushi;
KW Transmembrane; Transmembrane helix; Tumor suppressor.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..820
FT /note="Sushi domain-containing protein 2"
FT /id="PRO_0000249440"
FT TOPO_DOM 23..782
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 783..803
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 804..820
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..64
FT /note="SMB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 282..430
FT /note="AMOP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00347"
FT DOMAIN 442..636
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 720..777
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..42
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|Ref.5"
FT DISULFID 29..33
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 33..60
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|Ref.5"
FT DISULFID 40..53
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|Ref.5"
FT DISULFID 40..42
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 46..52
FT /evidence="ECO:0000269|Ref.5"
FT DISULFID 53..60
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 722..762
FT /evidence="ECO:0000250"
FT DISULFID 748..775
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..402
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020425"
FT VAR_SEQ 24..143
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020426"
FT CONFLICT 239
FT /note="Q -> R (in Ref. 1; BAC28486)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="A -> G (in Ref. 1; BAC26135)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="S -> C (in Ref. 1; BAC26135)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="P -> T (in Ref. 1; BAC29689)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="L -> Q (in Ref. 1; BAC31269)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="I -> F (in Ref. 1; BAC26135)"
FT /evidence="ECO:0000305"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:2CQW"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:2CQW"
SQ SEQUENCE 820 AA; 90641 MW; 72B0847EE9C7A687 CRC64;
MKLALLPWIL MLLSTIPGPG FTAGAQGSCS LRCGAQDGLC SCHPTCSGLG TCCEDFLDYC
LEILPSSGSM MGGKDFVVQH LKWTDPTDGV ICRFKESIQT LGYVDDFYQV HCISPLLYES
GYIPFTISMD NGRSFPHAGT WLAAHPYKVS ESEKSQLVNE THWQYYGTSD TRGNLNLTWD
TSALPTPAVT IELWGYEETG KPYSGNWTSK WSYLYPLATN IPNTGFFTFT PKPASPQYQR
WKVGALRISS SRNYPGEKDV RALWTNDHAL AWHLGDDFRA DSVAWARAQC LAWEALEDQL
PNFLTELPDC PCTLAQARAD SGRFFTDYGC DIEHGSVCTY HPGAVHCVRS VQASPRYGSG
QQCCYTAAGT QLLTSDSTSG STPDRGHDWG APPYRTPPRV PGMSHWLYDV ISFYYCCLWA
PECPRYMKRR PSSDCRNYRP PRLASAFGDP HFVTFDGTSF SFSGNGEYVL LETTLSDLRV
QGRAQPGRMP NGTQARGTGL TAVAVQEDNS DVIEVRLAGG SRVLEVLLNQ KVLSFTEQNW
MDLKGMFLSV AAQDKVSIML SSGAGLEVGV QGPFLSVSIL LPEKFLTHTR GLLGTLNNNP
RDDFTLRNGQ VLPLNASAQQ VFQFGADWAV SNTSSLFTYD SWLLVYQFVY GPKHNPNFKP
LFPDETTLSP SQTEDVARLC EGDRFCILDV MSTGSSSVGN ATRIAHQLHQ HRLKSLQPVV
SCGWLPPPAN GHKEGLRYLE GSVVRFSCNN GYSLVGPESS TCQADGKWSM PTPECQPGRS
YTVLLSIIFG GLAIVALISI IYMMLHRRRK SNMTMWSSQP
