ID   SRCRL_HUMAN             Reviewed;        1573 AA.
AC   A1L4H1; B5MDQ5; C7S7T9; C7S7U0; K7EP70;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 3.
DT   13-FEB-2019, entry version 97.
DE   RecName: Full=Soluble scavenger receptor cysteine-rich domain-containing protein SSC5D;
DE   AltName: Full=Soluble scavenger protein with 5 SRCR domains;
DE            Short=SSc5D;
DE   Flags: Precursor;
GN   Name=SSC5D;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX   PubMed=19535143; DOI=10.1016/j.molimm.2009.05.006;
RA   Goncalves C.M., Castro M.A., Henriques T., Oliveira M.I.,
RA   Pinheiro H.C., Oliveira C., Sreenu V.B., Evans E.J., Davis S.J.,
RA   Moreira A., Carmo A.M.;
RT   "Molecular cloning and analysis of SSc5D, a new member of the
RT   scavenger receptor cysteine-rich superfamily.";
RL   Mol. Immunol. 46:2585-2596(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1475-1573 (ISOFORM 1).
RC   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Binds to extracellular matrix proteins. Binds to
CC       pathogen-associated molecular patterns (PAMPs) present on the cell
CC       walls of Gram-positive and Gram-negative bacteria and fungi,
CC       behaving as a pattern recognition receptor (PRR). Induces
CC       bacterial and fungal aggregation and subsequent inhibition of
CC       PAMP-induced cytokine release. Does not possess intrinsic
CC       bactericidal activity. May play a role in the innate defense and
CC       homeostasis of certain epithelial surfaces (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with LGALS1 and laminin. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q96L14:CEP170P1; NbExp=5; IntAct=EBI-10172867, EBI-743488;
CC       Q96EV8:DTNBP1; NbExp=3; IntAct=EBI-10172867, EBI-465804;
CC       Q9UPT5:EXOC7; NbExp=3; IntAct=EBI-10172867, EBI-720048;
CC       Q13503:MED21; NbExp=5; IntAct=EBI-10172867, EBI-394678;
CC       Q7Z6G3-2:NECAB2; NbExp=5; IntAct=EBI-10172867, EBI-10172876;
CC       P37198:NUP62; NbExp=5; IntAct=EBI-10172867, EBI-347978;
CC       Q9Y6Y8:SEC23IP; NbExp=5; IntAct=EBI-10172867, EBI-1767971;
CC       Q13077:TRAF1; NbExp=3; IntAct=EBI-10172867, EBI-359224;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A1L4H1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A1L4H1-2; Sequence=VSP_040792, VSP_040793;
CC   -!- TISSUE SPECIFICITY: Highly expressed in monocytes/macrophages and
CC       T-lymphocytes. Highly expressed in placenta and spleen, and also
CC       detected at lower levels in colon, and more weakly in lung, heart
CC       and kidney. {ECO:0000269|PubMed:19535143}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI30539.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAI30541.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=ACJ02752.1; Type=Frameshift; Positions=934; Evidence={ECO:0000305};
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DR   EMBL; EU699476; ACJ02751.1; -; mRNA.
DR   EMBL; EU699477; ACJ02752.1; ALT_FRAME; mRNA.
DR   EMBL; AC008735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC130538; AAI30539.1; ALT_INIT; mRNA.
DR   EMBL; BC130540; AAI30541.1; ALT_INIT; mRNA.
DR   CCDS; CCDS46196.1; -. [A1L4H1-1]
DR   CCDS; CCDS59424.1; -. [A1L4H1-2]
DR   RefSeq; NP_001138422.1; NM_001144950.1. [A1L4H1-1]
DR   RefSeq; NP_001182196.1; NM_001195267.1. [A1L4H1-2]
DR   UniGene; Hs.554182; -.
DR   ProteinModelPortal; A1L4H1; -.
DR   BioGrid; 129821; 13.
DR   IntAct; A1L4H1; 17.
DR   iPTMnet; A1L4H1; -.
DR   PhosphoSitePlus; A1L4H1; -.
DR   BioMuta; SSC5D; -.
DR   jPOST; A1L4H1; -.
DR   PaxDb; A1L4H1; -.
DR   PRIDE; A1L4H1; -.
DR   ProteomicsDB; 150; -.
DR   ProteomicsDB; 151; -. [A1L4H1-2]
DR   Ensembl; ENST00000389623; ENSP00000374274; ENSG00000179954. [A1L4H1-1]
DR   Ensembl; ENST00000587166; ENSP00000467252; ENSG00000179954. [A1L4H1-2]
DR   GeneID; 284297; -.
DR   KEGG; hsa:284297; -.
DR   UCSC; uc002qlg.5; human. [A1L4H1-1]
DR   CTD; 284297; -.
DR   EuPathDB; HostDB:ENSG00000179954.14; -.
DR   GeneCards; SSC5D; -.
DR   H-InvDB; HIX0015472; -.
DR   HGNC; HGNC:26641; SSC5D.
DR   HPA; HPA042008; -.
DR   MIM; 618194; gene.
DR   neXtProt; NX_A1L4H1; -.
DR   OpenTargets; ENSG00000179954; -.
DR   eggNOG; ENOG410IHBC; Eukaryota.
DR   eggNOG; ENOG410XQVR; LUCA.
DR   GeneTree; ENSGT00940000162592; -.
DR   HOGENOM; HOG000154412; -.
DR   HOVERGEN; HBG108511; -.
DR   InParanoid; A1L4H1; -.
DR   OMA; PVRVMAC; -.
DR   OrthoDB; 158600at2759; -.
DR   PhylomeDB; A1L4H1; -.
DR   TreeFam; TF329295; -.
DR   Reactome; R-HSA-3000471; Scavenging by Class B Receptors.
DR   GenomeRNAi; 284297; -.
DR   PRO; PR:A1L4H1; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000179954; Expressed in 188 organ(s), highest expression level in tendon.
DR   ExpressionAtlas; A1L4H1; baseline and differential.
DR   Genevisible; A1L4H1; HS.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005622; C:intracellular; ISS:UniProtKB.
DR   GO; GO:0050840; F:extracellular matrix binding; ISS:UniProtKB.
DR   GO; GO:0001968; F:fibronectin binding; ISS:UniProtKB.
DR   GO; GO:0043236; F:laminin binding; ISS:UniProtKB.
DR   GO; GO:0005044; F:scavenger receptor activity; ISS:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR   GO; GO:0042494; P:detection of bacterial lipoprotein; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:2000483; P:negative regulation of interleukin-8 secretion; ISS:UniProtKB.
DR   Gene3D; 3.10.250.10; -; 5.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   Pfam; PF00530; SRCR; 5.
DR   PRINTS; PR00258; SPERACTRCPTR.
DR   SMART; SM00202; SR; 5.
DR   SUPFAM; SSF56487; SSF56487; 5.
DR   PROSITE; PS00420; SRCR_1; 5.
DR   PROSITE; PS50287; SRCR_2; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Cytoplasm;
KW   Developmental protein; Disulfide bond; Glycoprotein; Immunity;
KW   Innate immunity; Receptor; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   CHAIN        17   1573       Soluble scavenger receptor cysteine-rich
FT                                domain-containing protein SSC5D.
FT                                /FTId=PRO_0000332985.
FT   DOMAIN       20    120       SRCR 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00196}.
FT   DOMAIN      198    298       SRCR 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00196}.
FT   DOMAIN      304    404       SRCR 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00196}.
FT   DOMAIN      467    568       SRCR 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00196}.
FT   DOMAIN      772    872       SRCR 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00196}.
FT   COMPBIAS    616    729       Thr-rich.
FT   COMPBIAS    970   1488       Pro-rich.
FT   COMPBIAS   1089   1382       Thr-rich.
FT   COMPBIAS   1558   1561       Poly-Thr.
FT   COMPBIAS   1563   1566       Poly-Glu.
FT   CARBOHYD    168    168       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    376    376       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    420    420       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     45    109       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID     58    119       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID     89     99       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID    223    287       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID    236    297       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID    267    277       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID    329    393       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID    342    403       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID    373    383       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID    492    557       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID    505    567       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID    537    547       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID    797    861       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID    810    871       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   DISULFID    841    851       {ECO:0000255|PROSITE-ProRule:PRU00196}.
FT   VAR_SEQ     929    953       GSKDGYKLPWTWDTPSGRGLAEGTP -> EPEAGAPRGDAP
FT                                RSRTARVAAPP (in isoform 2).
FT                                {ECO:0000303|PubMed:19535143}.
FT                                /FTId=VSP_040792.
FT   VAR_SEQ     954   1573       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:19535143}.
FT                                /FTId=VSP_040793.
FT   CONFLICT    976    976       L -> P (in Ref. 1; ACJ02751).
FT                                {ECO:0000305}.
FT   CONFLICT   1274   1274       M -> I (in Ref. 1; ACJ02751).
FT                                {ECO:0000305}.
FT   CONFLICT   1456   1456       P -> S (in Ref. 1; ACJ02751).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1573 AA;  165743 MW;  9151F14B58BD1A0D CRC64;
     MRVLACLLAA LVGIQAVERL RLADGPHGCA GRLEVWHGGR WGTVCDDGWD LRDAAVACRQ
     LGCGGALAAP GGAFFGEGAG PVWLSELACR GNEGQLGLCH HRGWKAHICS HEEDAGVVCA
     GQRVANSRDD STSPLDGAPW PGLLLELSPS TEEPLVTHAP RPAGNPQNAS RKKSPRPKQA
     KSTRAPLLTT GAPRQERLRL VSGPHRCAGR LEVWHGGRWG TVCDDGWDLR DAAVACRELG
     CGGALAAPGG ARFGPGAGPV WMDDVGCGGG EQALRDCPRS PWGRSNCDHS EDAGLVCTGP
     APRLRLADGP HGCAGRLEVW HGGRWGSVCD DAWDLRDAAV ACRELGCGGA LAAPGGAFFG
     EGSGPIILDD LRCRGNETAL RFCPARPWGQ HDCHHREDAG AVCDGMPLGY VPPTAPTDSN
     NSTPREAASR PPSTMTSQAP GTAGVSPPPA SPTVLWEPGP EAGSPQLRLV AGPSKCSGRL
     EVWHDQRWGT VCDDSWDMRD SAVVCRELGC GGPQQPDPAA GRFGWGAGPI WLDDVGCVGT
     EASLSDCPAA PWGKHNCAHN EDVGVTCTGP PGLDSISDPF SWSWIPGLGR DRDAWLPGEL
     ATKPSASVTA SVLEKTTTKA PGKMPKSTKK WVTKNAKRPT TQPPVMPTTK HSRAQSPPDL
     TSQTTAALTT EASRRPTSEF TRRPTTEAPQ RWTSHTTATL TPQAPRERTT KTMAMLTTQG
     PQEMTSESTI KSIPQASLEP SAEIPEGSPE SPKDPAPSPS VSTTGESGLF RVRLADGPNR
     CAGRLEVWHA GRWGTVCDDN WDLRDATVAC WELGCGKVRP RVGKTHYGPG TGPIWLDDMG
     CKGSEASLSD CPSGAWGKHN CDHEEDVGLT CTGYTDYDDY PPWTWDPTSR EDLAKGTTTA
     GVPGHTLPWR TTRRPGSSSP AIRRLPDTGS KDGYKLPWTW DTPSGRGLAE GTPTAGKLGP
     TLGAGTTRSP GSPPTLRVHG DTGSPRKPWP ERRPPRPAAT RTAPPTPSPG PSASPGPPGP
     ALTSDSSREL TPHSALTSEA TSDAPDTSPP TPDPASRTNP DLILTSPDFA LSTPDSSVVP
     ALTPEPSPTP LPTLPKELTS DPSTPSEVTS LSPTSEQVPE SDTTPDLDTT PYSSTVSEYS
     RSPDPSPSPH PTTTPDPTMA PDPITTLNPT VTPHFPTTPH PTTTPHPTTI THSTMIPDPT
     TTPQPFTTIT HSTMIPDPTT TPQPFTTMQP TTTPHSTTPH PTTTPHPTTI THSTMIPDPT
     TTPQPFTTMQ PTTMPHPTTT PHPTTTPHPT TTPHPTTTPH PTMTPDPTTT PYPTTTPDPT
     TTPHPTTPDP SSTPVITTVS LPTSLGTELS SPTLAPTVKP SLHPQLTFTA PAPHTSTSQI
     PTLEPSPALE SSPSRSSTAT SMDPLSTEDF KPPRSQSPNL TPPPTHTPHS ASDLTVSPDP
     LLSPTAHPLD HPPLDPLTLG PTPGQSPGPH GPCVAPTPPV RVMACEPPAL VELVAAVRDV
     GGQLQRLTQV VEQERQERQA LLLGLTQLVE AARGLGQLGE AVKRLAEMAW TTSMPAPTTT
     TPEEEERPLR GDV
//