SUSD6_HUMAN
ID SUSD6_HUMAN Reviewed; 303 AA.
AC Q92537;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Sushi domain-containing protein 6 {ECO:0000312|HGNC:HGNC:19956};
DE AltName: Full=Drug-activated gene overexpressed protein {ECO:0000303|PubMed:24652652};
DE Flags: Precursor;
GN Name=SUSD6 {ECO:0000312|HGNC:HGNC:19956};
GN Synonyms=DRAGO {ECO:0000303|PubMed:24652652},
GN KIAA0247 {ECO:0000312|HGNC:HGNC:19956};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 FUNCTION, AND INDUCTION.
RX PubMed=20236627; DOI=10.1016/j.cellimm.2010.02.017;
RA Schwanzer-Pfeiffer D., Rossmanith E., Schildberger A., Falkenhagen D.;
RT "Characterization of SVEP1, KIAA, and SRPX2 in an in vitro cell culture
RT model of endotoxemia.";
RL Cell. Immunol. 263:65-70(2010).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=24652652; DOI=10.1093/jnci/dju053;
RA Polato F., Rusconi P., Zangrossi S., Morelli F., Boeri M., Musi A.,
RA Marchini S., Castiglioni V., Scanziani E., Torri V., Broggini M.;
RT "DRAGO (KIAA0247), a new DNA damage-responsive, p53-inducible gene that
RT cooperates with p53 as oncosuppressor. [Corrected].";
RL J. Natl. Cancer Inst. 106:1-10(2014).
CC -!- FUNCTION: May play a role in growth-suppressive activity and cell death
CC (PubMed:24652652). May be involved in the production of chemokine
CC molecules in umbilical vein endothelial cells (HUVECs) cultured in THP1
CC monocyte LPS-induced medium (PubMed:20236627). Plays a role in
CC preventing tumor onset (By similarity). {ECO:0000250|UniProtKB:Q8BGE4,
CC ECO:0000269|PubMed:20236627, ECO:0000269|PubMed:24652652}.
CC -!- INTERACTION:
CC Q92537; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-2866213, EBI-10173507;
CC Q92537; Q96GG9: DCUN1D1; NbExp=3; IntAct=EBI-2866213, EBI-740086;
CC Q92537; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-2866213, EBI-12118888;
CC Q92537; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-2866213, EBI-11749135;
CC Q92537; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-2866213, EBI-10171774;
CC Q92537; Q8N3F0: MTURN; NbExp=3; IntAct=EBI-2866213, EBI-11980301;
CC Q92537; Q96BN8: OTULIN; NbExp=3; IntAct=EBI-2866213, EBI-750730;
CC Q92537; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-2866213, EBI-741829;
CC Q92537; Q9BZV1: UBXN6; NbExp=3; IntAct=EBI-2866213, EBI-1993899;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by chemotherapeutic DNA-damaging agents and by
CC p53/TP53 and/or by p73/TP73 in response to cytotoxic insults
CC (PubMed:24652652). Up-regulated by lipopolysaccharide (LPS) in
CC monocytic THP1 cells (PubMed:20236627). Up-regulated in umbilical vein
CC endothelial cells (HUVECs) cultured in THP1 monocyte LPS-induced
CC medium. {ECO:0000269|PubMed:20236627, ECO:0000269|PubMed:24652652}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13378.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D87434; BAA13378.2; ALT_INIT; mRNA.
DR EMBL; BC064697; AAH64697.1; -; mRNA.
DR CCDS; CCDS9796.1; -.
DR RefSeq; NP_055549.1; NM_014734.3.
DR RefSeq; XP_011535714.1; XM_011537412.1.
DR RefSeq; XP_016877327.1; XM_017021838.1.
DR RefSeq; XP_016877328.1; XM_017021839.1.
DR AlphaFoldDB; Q92537; -.
DR BioGRID; 115112; 20.
DR IntAct; Q92537; 15.
DR MINT; Q92537; -.
DR STRING; 9606.ENSP00000344424; -.
DR iPTMnet; Q92537; -.
DR PhosphoSitePlus; Q92537; -.
DR BioMuta; SUSD6; -.
DR DMDM; 2495723; -.
DR EPD; Q92537; -.
DR jPOST; Q92537; -.
DR MassIVE; Q92537; -.
DR PaxDb; Q92537; -.
DR PeptideAtlas; Q92537; -.
DR PRIDE; Q92537; -.
DR ProteomicsDB; 75295; -.
DR Antibodypedia; 25061; 77 antibodies from 19 providers.
DR DNASU; 9766; -.
DR Ensembl; ENST00000342745.5; ENSP00000344424.4; ENSG00000100647.8.
DR GeneID; 9766; -.
DR KEGG; hsa:9766; -.
DR MANE-Select; ENST00000342745.5; ENSP00000344424.4; NM_014734.4; NP_055549.1.
DR UCSC; uc001xlk.4; human.
DR CTD; 9766; -.
DR DisGeNET; 9766; -.
DR GeneCards; SUSD6; -.
DR HGNC; HGNC:19956; SUSD6.
DR HPA; ENSG00000100647; Low tissue specificity.
DR neXtProt; NX_Q92537; -.
DR OpenTargets; ENSG00000100647; -.
DR PharmGKB; PA128394557; -.
DR VEuPathDB; HostDB:ENSG00000100647; -.
DR eggNOG; ENOG502QYTF; Eukaryota.
DR GeneTree; ENSGT00940000157120; -.
DR HOGENOM; CLU_044351_0_1_1; -.
DR InParanoid; Q92537; -.
DR OMA; NGGYVCH; -.
DR OrthoDB; 1224817at2759; -.
DR PhylomeDB; Q92537; -.
DR TreeFam; TF332459; -.
DR PathwayCommons; Q92537; -.
DR SignaLink; Q92537; -.
DR BioGRID-ORCS; 9766; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; SUSD6; human.
DR GenomeRNAi; 9766; -.
DR Pharos; Q92537; Tbio.
DR PRO; PR:Q92537; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q92537; protein.
DR Bgee; ENSG00000100647; Expressed in epithelium of nasopharynx and 198 other tissues.
DR Genevisible; Q92537; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008219; P:cell death; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR CDD; cd00033; CCP; 1.
DR InterPro; IPR042866; SUSD6.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR46839; PTHR46839; 1.
DR Pfam; PF00084; Sushi; 1.
DR SMART; SM00032; CCP; 1.
DR SUPFAM; SSF57535; SSF57535; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Membrane; Reference proteome; Signal; Sushi; Transmembrane;
KW Transmembrane helix; Tumor suppressor.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..303
FT /note="Sushi domain-containing protein 6"
FT /id="PRO_0000013985"
FT TOPO_DOM 40..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..104
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 199..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 42..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 74..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 303 AA; 32090 MW; D5EBDB2F2A8781E1 CRC64;
MCHGRIAPKS TSVFAVASVG HGVFLPLVIL CTLLGDGLAS VCPLPPEPEN GGYICHPRPC
RDPLTAGSVI EYLCAEGYML KGDYKYLTCK NGEWKPAMEI SCRLNEDKDT HTSLGVPTLS
IVASTASSVA LILLLVVLFV LLQPKLKSFH HSRRDQGVSG DQVSIMVDGV QVALPSYEEA
VYGSSGHCVP PADPRVQIVL SEGSGPSGRS VPREQQLPDQ GACSSAGGED EAPGQSGLCE
AWGSRASETV MVHQATTSSW VAGSGNRQLA HKETADSENS DIQSLLSLTS EEYTDDIPLL
KEA
