SRCRL_HUMAN
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 03-AUG-2022, entry version 116.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Pinheiro H.C.,
RA Oliveira C., Sreenu V.B., Evans E.J., Davis S.J., Moreira A., Carmo A.M.;
RT "Molecular cloning and analysis of SSc5D, a new member of the scavenger
RT 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., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Binds to extracellular matrix proteins. Binds to pathogen-
CC associated molecular patterns (PAMPs) present on the cell walls of
CC Gram-positive and Gram-negative bacteria and fungi, behaving as a
CC pattern recognition receptor (PRR). Induces bacterial and fungal
CC aggregation and subsequent inhibition of PAMP-induced cytokine release.
CC Does not possess intrinsic bactericidal activity. May play a role in
CC the innate defense and homeostasis of certain epithelial surfaces (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with LGALS1 and laminin. {ECO:0000250}.
CC -!- INTERACTION:
CC A1L4H1; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-10172867, EBI-465872;
CC A1L4H1; Q96L14: CEP170P1; NbExp=3; IntAct=EBI-10172867, EBI-743488;
CC A1L4H1; Q96EV8: DTNBP1; NbExp=3; IntAct=EBI-10172867, EBI-465804;
CC A1L4H1; Q9UPT5: EXOC7; NbExp=3; IntAct=EBI-10172867, EBI-720048;
CC A1L4H1; Q9UPT5-1: EXOC7; NbExp=3; IntAct=EBI-10172867, EBI-6251402;
CC A1L4H1; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-10172867, EBI-2514791;
CC A1L4H1; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-10172867, EBI-3044087;
CC A1L4H1; Q9P086: MED11; NbExp=3; IntAct=EBI-10172867, EBI-394704;
CC A1L4H1; Q13503: MED21; NbExp=6; IntAct=EBI-10172867, EBI-394678;
CC A1L4H1; Q9NX70: MED29; NbExp=3; IntAct=EBI-10172867, EBI-394656;
CC A1L4H1; Q7Z6G3-2: NECAB2; NbExp=6; IntAct=EBI-10172867, EBI-10172876;
CC A1L4H1; P37198: NUP62; NbExp=6; IntAct=EBI-10172867, EBI-347978;
CC A1L4H1; Q13526: PIN1; NbExp=3; IntAct=EBI-10172867, EBI-714158;
CC A1L4H1; O00560: SDCBP; NbExp=3; IntAct=EBI-10172867, EBI-727004;
CC A1L4H1; Q9Y6Y8: SEC23IP; NbExp=6; IntAct=EBI-10172867, EBI-1767971;
CC A1L4H1; Q96BD8: SKA1; NbExp=3; IntAct=EBI-10172867, EBI-741854;
CC A1L4H1; Q15560: TCEA2; NbExp=3; IntAct=EBI-10172867, EBI-710310;
CC A1L4H1; Q13077: TRAF1; NbExp=3; IntAct=EBI-10172867, EBI-359224;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm {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 T-
CC lymphocytes. Highly expressed in placenta and spleen, and also detected
CC at lower levels in colon, and more weakly in lung, heart and kidney.
CC {ECO:0000269|PubMed:19535143}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI30539.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI30541.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACJ02752.1; Type=Frameshift; 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 AlphaFoldDB; A1L4H1; -.
DR SMR; A1L4H1; -.
DR BioGRID; 129821; 28.
DR IntAct; A1L4H1; 20.
DR STRING; 9606.ENSP00000374274; -.
DR GlyGen; A1L4H1; 18 sites, 7 O-linked glycans (15 sites).
DR iPTMnet; A1L4H1; -.
DR PhosphoSitePlus; A1L4H1; -.
DR BioMuta; SSC5D; -.
DR jPOST; A1L4H1; -.
DR MassIVE; A1L4H1; -.
DR PaxDb; A1L4H1; -.
DR PeptideAtlas; A1L4H1; -.
DR PRIDE; A1L4H1; -.
DR ProteomicsDB; 150; -. [A1L4H1-1]
DR ProteomicsDB; 151; -. [A1L4H1-2]
DR Antibodypedia; 50987; 59 antibodies from 13 providers.
DR DNASU; 284297; -.
DR Ensembl; ENST00000389623.11; ENSP00000374274.4; ENSG00000179954.16. [A1L4H1-1]
DR Ensembl; ENST00000587166.5; ENSP00000467252.1; ENSG00000179954.16. [A1L4H1-2]
DR GeneID; 284297; -.
DR KEGG; hsa:284297; -.
DR MANE-Select; ENST00000389623.11; ENSP00000374274.4; NM_001144950.2; NP_001138422.1.
DR UCSC; uc002qlg.5; human. [A1L4H1-1]
DR CTD; 284297; -.
DR DisGeNET; 284297; -.
DR GeneCards; SSC5D; -.
DR HGNC; HGNC:26641; SSC5D.
DR HPA; ENSG00000179954; Tissue enhanced (endometrium).
DR MIM; 618194; gene.
DR neXtProt; NX_A1L4H1; -.
DR OpenTargets; ENSG00000179954; -.
DR VEuPathDB; HostDB:ENSG00000179954; -.
DR eggNOG; ENOG502SECN; Eukaryota.
DR GeneTree; ENSGT00940000162592; -.
DR HOGENOM; CLU_004182_1_0_1; -.
DR InParanoid; A1L4H1; -.
DR OMA; WTWDTPS; -.
DR OrthoDB; 158600at2759; -.
DR PhylomeDB; A1L4H1; -.
DR TreeFam; TF329295; -.
DR PathwayCommons; A1L4H1; -.
DR Reactome; R-HSA-3000471; Scavenging by Class B Receptors.
DR SignaLink; A1L4H1; -.
DR BioGRID-ORCS; 284297; 9 hits in 1065 CRISPR screens.
DR ChiTaRS; SSC5D; human.
DR GenomeRNAi; 284297; -.
DR Pharos; A1L4H1; Tbio.
DR PRO; PR:A1L4H1; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; A1L4H1; protein.
DR Bgee; ENSG00000179954; Expressed in tendon of biceps brachii and 163 other tissues.
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:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:0006952; P:defense response; IBA:GO_Central.
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:0032717; P:negative regulation of interleukin-8 production; 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; Cytoplasm; Developmental protein; Disulfide bond;
KW Glycoprotein; Immunity; Innate immunity; Receptor; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1573
FT /note="Soluble scavenger receptor cysteine-rich domain-
FT containing protein SSC5D"
FT /id="PRO_0000332985"
FT DOMAIN 20..120
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 198..298
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 304..404
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 467..568
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 772..872
FT /note="SRCR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 153..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1018
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1095
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1330
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1475
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 58..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 89..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 223..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 236..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 267..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 329..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 342..403
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 373..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 492..557
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 505..567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 537..547
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 797..861
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 810..871
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 841..851
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT VAR_SEQ 929..953
FT /note="GSKDGYKLPWTWDTPSGRGLAEGTP -> EPEAGAPRGDAPRSRTARVAAPP
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19535143"
FT /id="VSP_040792"
FT VAR_SEQ 954..1573
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19535143"
FT /id="VSP_040793"
FT CONFLICT 976
FT /note="L -> P (in Ref. 1; ACJ02751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1274
FT /note="M -> I (in Ref. 1; ACJ02751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1456
FT /note="P -> S (in Ref. 1; ACJ02751)"
FT /evidence="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
