SRCRL_MOUSE
ID SRCRL_MOUSE Reviewed; 1371 AA.
AC Q8BV57; B2RUB0; C6ZFQ2; Q3TMW2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Soluble scavenger receptor cysteine-rich domain-containing protein SSC5D;
DE AltName: Full=Scavenger receptor cysteine-rich domain-containing protein LOC284297 homolog;
DE Flags: Precursor;
GN Name=Ssc5d; Synonyms=S5D-SRCRB;
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 [MRNA], FUNCTION, INTERACTION WITH LGALS1 AND LAMININ,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP GLYCOSYLATION.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=21217009; DOI=10.4049/jimmunol.1000840;
RA Miro-Julia C., Rosello S., Martinez V.G., Fink D.R., Escoda-Ferran C.,
RA Padilla O., Vazquez-Echeverria C., Espinal-Marin P., Pujades C.,
RA Garcia-Pardo A., Vila J., Serra-Pages C., Holmskov U., Yelamos J.,
RA Lozano F.;
RT "Molecular and functional characterization of mouse S5D-SRCRB: a new group
RT B member of the scavenger receptor cysteine-rich superfamily.";
RL J. Immunol. 186:2344-2354(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
CC {ECO:0000269|PubMed:21217009}.
CC -!- SUBUNIT: Interacts with LGALS1 and laminin.
CC {ECO:0000269|PubMed:21217009}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21217009}. Cytoplasm
CC {ECO:0000269|PubMed:21217009}.
CC -!- TISSUE SPECIFICITY: Detected throughout the gastrointestinal and
CC genitourinary tracts, in serosal salivary gland, the exocrine part of
CC pancreas and testis, as well as in a few tubular structures in kidney.
CC Not detected in lung and heart (at protein level). Strongly expressed
CC in testis, kidney and pancreas, with lower levels detected in bone
CC marrow, spleen, lung, liver, colon, stomach and skeletal muscle. Very
CC low levels or no expression detected in thymus, esophagus, jejunum,
CC ileum, duodenum, ovary, uterus, heart, trachea, brain, cerebellum and
CC bladder. {ECO:0000269|PubMed:21217009}.
CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc, detected in placodes, ectodermal
CC thickenings where organs or structures will develop. Expression levels
CC increase substantially between 9 and 14 dpc.
CC {ECO:0000269|PubMed:21217009}.
CC -!- PTM: Partially N- and O-glycosylated. {ECO:0000269|PubMed:21217009}.
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DR EMBL; EU850434; ACF54723.1; -; mRNA.
DR EMBL; AK079906; BAC37780.1; -; mRNA.
DR EMBL; AK165666; BAE38328.1; -; mRNA.
DR EMBL; CH466627; EDL31272.1; -; Genomic_DNA.
DR EMBL; BC141044; AAI41045.1; -; mRNA.
DR CCDS; CCDS20750.1; -.
DR RefSeq; NP_766596.1; NM_173008.2.
DR AlphaFoldDB; Q8BV57; -.
DR SMR; Q8BV57; -.
DR STRING; 10090.ENSMUSP00000052126; -.
DR GlyGen; Q8BV57; 4 sites.
DR PhosphoSitePlus; Q8BV57; -.
DR PaxDb; Q8BV57; -.
DR PeptideAtlas; Q8BV57; -.
DR PRIDE; Q8BV57; -.
DR ProteomicsDB; 257066; -.
DR Antibodypedia; 50987; 59 antibodies from 13 providers.
DR DNASU; 269855; -.
DR Ensembl; ENSMUST00000057612; ENSMUSP00000052126; ENSMUSG00000035279.
DR GeneID; 269855; -.
DR KEGG; mmu:269855; -.
DR UCSC; uc009eza.1; mouse.
DR CTD; 284297; -.
DR MGI; MGI:3606211; Ssc5d.
DR VEuPathDB; HostDB:ENSMUSG00000035279; -.
DR eggNOG; ENOG502SECN; Eukaryota.
DR GeneTree; ENSGT00940000162592; -.
DR HOGENOM; CLU_004182_0_0_1; -.
DR InParanoid; Q8BV57; -.
DR OMA; WTWDTPS; -.
DR OrthoDB; 158600at2759; -.
DR PhylomeDB; Q8BV57; -.
DR TreeFam; TF329295; -.
DR BioGRID-ORCS; 269855; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Ssc5d; mouse.
DR PRO; PR:Q8BV57; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BV57; protein.
DR Bgee; ENSMUSG00000035279; Expressed in retinal neural layer and 95 other tissues.
DR Genevisible; Q8BV57; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:UniProtKB.
DR GO; GO:0001968; F:fibronectin binding; IDA:UniProtKB.
DR GO; GO:0043236; F:laminin binding; IDA:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IDA:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0042494; P:detection of bacterial lipoprotein; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IDA:UniProtKB.
DR GO; GO:0032677; P:regulation of interleukin-8 production; IDA:MGI.
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 Cytoplasm; Developmental protein; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Receptor; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1371
FT /note="Soluble scavenger receptor cysteine-rich domain-
FT containing protein SSC5D"
FT /id="PRO_0000332986"
FT DOMAIN 20..120
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 199..299
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 305..405
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 464..565
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 758..858
FT /note="SRCR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 143..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..459
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1044
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1131
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 224..288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 237..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 268..278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 330..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 343..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 374..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 489..554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 502..564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 534..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 783..847
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 796..857
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 827..837
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT CONFLICT 633
FT /note="R -> K (in Ref. 2; BAE38328, 3; EDL31272 and 4;
FT AAI41045)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1371 AA; 144637 MW; 42D0E12A10207D5D CRC64;
MRGLACLLAM LVGIQAIERL RLADGPHGCA GRLEVWHSGR WGTVCDDGWD LRDAEVACRV
LGCGGALAAP GGAFFGEGTG PVWLSELNCR GNEGQLGICP HRGWKAHICS HEEDAGVVCV
GQRAANSRED SMSLLDGDPW LALSGELSPS SEEPPITHAP QPAASSQNGP RKKNPRPPKQ
TKSTRAPVLT NGAPHQERLR LVSGPHGCAG RLEVWHGGRW GTVCDDGWDL RDAAVACREL
GCGGALAAPG GARFGPGEGP VWMDDVGCGG GEEALRDCPR SPWGRSNCDH TEDAGLVCTG
PAPRIRLADG PHGCAGRLEV WHGGRWGSVC DDAWDLRDAA VACKELGCGG ALAAPGGAFF
GEGTGPIILD DLRCRGNETA LRFCPARPWG QHDCHHREDA GAVCDGMPLG AVQPTVPAVD
SNSTAHRLLS TSVGQMPGPA GPWPPSASPT APPEPGPEAG SPQLRLVAGP SRCSGRLEVW
HDGRWGTVCD DSWDMRDSAV VCRELGCGRP RQPDPAAGRF GWGAGPIWLD DVGCMGTEAS
LSECPAASWG KHNCAHNEDV GVTCTGTPGL DTISDPFSWS WLPGLGRDQD AWLPGELTTK
PSASLTSSVP QKPTKVPGKA PKSTKKWVTK NARRPTTQPP GMPTTKHSRA PGTPTSLHPT
ARTSELPKRL TTEAPHRQTS HTTVRLTPRV PWEWTSEPVV SQSTQGPQEV TSEATTTENP
QTSLEPSGEN TEGSLESSQD PATTPTAGVP VPSGPFRVRL ADGPNRCAGR LEVWHAGLWG
TVCDDSWDIR DATVACWELG CGKVRPRVGK THYGPGTGPI WLDDMGCKGS EMSLSDCPSG
AWGKHNCDHE EDVVLTCTGY TGDDDYPSWT WDPTSGEDLT KGTTVAARPG HTLSWATTTN
TEVPSPATQN LPDTDDQGGY ESSWTWDTPS GRGLFKGTPT TTKPGSTVTT STSKSPGHPF
PAPRARAGSP RKPTPERRPL PTSATTSSPA SSSSPEPSGS RQTSGSWPQL IPDSKQEGTS
SSPKPSLLTP GLPSPATFAL STPNTSLLPT RSPELSGSPT PTSPEGLTSA SSMLSEVSRL
SPTSELTPGP DTTPAPEIIP ESSDSSDLPM NTRTPTQPFT ASHPTSIPQL NTTSYPTIAP
QPTTNPQQPR SPHPATSPQP PTNTHPSSTP ATPTESLPSS RKTELSSPTK PRLNSELTFE
EAPSTDASQT QNLELFLASE SGPSSPSPAS NLDPLPTDAF KPPRSQTLHS ASDHLTQGPT
PNHNPDPFGP CVSPLPPVRV MACEPPALVE LVGAVREVGD QLQRLTWVLE QDRQERQVLA
LGLAQLVEAA QGLGQLSETV KRLAEVAWPP STPVPMTTTT EEEERPLRGD V
