CD5L_HUMAN
ID CD5L_HUMAN Reviewed; 347 AA.
AC O43866; A8K7M5; Q6UX63;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=CD5 antigen-like;
DE AltName: Full=Apoptosis inhibitor expressed by macrophages {ECO:0000303|PubMed:23236605};
DE Short=hAIM {ECO:0000303|PubMed:23236605};
DE AltName: Full=CT-2 {ECO:0000303|Ref.2};
DE AltName: Full=IgM-associated peptide {ECO:0000303|PubMed:8034987};
DE AltName: Full=SP-alpha {ECO:0000303|PubMed:9045627};
DE Flags: Precursor;
GN Name=CD5L; Synonyms=API6;
GN ORFNames=UNQ203/PRO229 {ECO:0000303|PubMed:12975309};
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], PROTEIN SEQUENCE OF N-TERMINUS, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Spleen;
RX PubMed=9045627; DOI=10.1074/jbc.272.10.6151;
RA Gebe J.A., Kiener P.A., Ring H.Z., Li X., Francke U., Aruffo A.;
RT "Molecular cloning, mapping to human chromosome 1 q21-q23, and cell binding
RT characteristics of Spalpha, a new member of the scavenger receptor
RT cysteine-rich (SRCR) family of proteins.";
RL J. Biol. Chem. 272:6151-6158(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Miyazaki T., Yusa S.;
RT "Human CT-2 cDNA.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Spleen;
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 [8]
RP PROTEIN SEQUENCE OF 20-31, AND INTERACTION WITH IGM.
RX PubMed=8034987; DOI=10.1016/0022-1759(94)90284-4;
RA Tissot J.-D., Schifferli J.A., Hochstrasser D.F., Pasquali C., Spertini F.,
RA Clement F., Frutiger S., Paquet N., Hughes G.J., Schneider P.;
RT "Two-dimensional polyacrylamide gel electrophoresis analysis of
RT cryoglobulins and identification of an IgM-associated peptide.";
RL J. Immunol. Methods 173:63-75(1994).
RN [9]
RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11981870;
RX DOI=10.1002/1522-2683(200204)23:7/8<1203::aid-elps1203>3.0.co;2-1;
RA Tissot J.D., Sanchez J.-C., Vuadens F., Scherl A., Schifferli J.A.,
RA Hochstrasser D.F., Schneider P., Duchosal M.A.;
RT "IgM are associated to Spalpha (CD5 antigen-like).";
RL Electrophoresis 23:1203-1206(2002).
RN [10]
RP PROTEIN SEQUENCE OF 20-34.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [11]
RP FUNCTION.
RX PubMed=16030018; DOI=10.1074/jbc.m505042200;
RA Sarrias M.R., Rosello S., Sanchez-Barbero F., Sierra J.M., Vila J.,
RA Yelamos J., Vives J., Casals C., Lozano F.;
RT "A role for human Sp alpha as a pattern recognition receptor.";
RL J. Biol. Chem. 280:35391-35398(2005).
RN [12]
RP MUTAGENESIS OF SER-123 AND 129-SER--SER-132.
RX PubMed=23236605; DOI=10.1016/j.febslet.2012.08.017;
RA Mori M., Kimura H., Iwamura Y., Arai S., Miyazaki T.;
RT "Modification of N-glycosylation modulates the secretion and lipolytic
RT function of apoptosis inhibitor of macrophage (AIM).";
RL FEBS Lett. 586:3569-3574(2012).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24223991; DOI=10.1371/journal.pone.0079670;
RA Sanjurjo L., Amezaga N., Vilaplana C., Caceres N., Marzo E., Valeri M.,
RA Cardona P.J., Sarrias M.R.;
RT "The scavenger protein apoptosis inhibitor of macrophages (AIM) potentiates
RT the antimicrobial response against Mycobacterium tuberculosis by enhancing
RT autophagy.";
RL PLoS ONE 8:E79670-E79670(2013).
RN [14]
RP FUNCTION.
RX PubMed=24583716; DOI=10.1038/cmi.2014.12;
RA Martinez V.G., Escoda-Ferran C., Tadeu Simoes I., Arai S., Orta Mascaro M.,
RA Carreras E., Martinez-Florensa M., Yelamos J., Miyazaki T., Lozano F.;
RT "The macrophage soluble receptor AIM/Api6/CD5L displays a broad pathogen
RT recognition spectrum and is involved in early response to microbial
RT aggression.";
RL Cell. Mol. Immunol. 11:343-354(2014).
RN [15]
RP FUNCTION.
RX PubMed=24295828; DOI=10.1189/jlb.1212660;
RA Amezaga N., Sanjurjo L., Julve J., Aran G., Perez-Cabezas B.,
RA Bastos-Amador P., Armengol C., Vilella R., Escola-Gil J.C., Blanco-Vaca F.,
RA Borras F.E., Valledor A.F., Sarrias M.R.;
RT "Human scavenger protein AIM increases foam cell formation and CD36-
RT mediated oxLDL uptake.";
RL J. Leukoc. Biol. 95:509-520(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH IGM.
RX PubMed=24804991; DOI=10.1371/journal.pone.0097037;
RA Kai T., Yamazaki T., Arai S., Miyazaki T.;
RT "Stabilization and augmentation of circulating AIM in mice by synthesized
RT IgM-Fc.";
RL PLoS ONE 9:E97037-E97037(2014).
RN [18]
RP FUNCTION.
RX PubMed=25713983; DOI=10.1080/15548627.2015.1017183;
RA Sanjurjo L., Amezaga N., Aran G., Naranjo-Gomez M., Arias L., Armengol C.,
RA Borras F.E., Sarrias M.R.;
RT "The human CD5L/AIM-CD36 axis: A novel autophagy inducer in macrophages
RT that modulates inflammatory responses.";
RL Autophagy 11:487-502(2015).
CC -!- FUNCTION: Secreted protein that acts as a key regulator of lipid
CC synthesis: mainly expressed by macrophages in lymphoid and inflamed
CC tissues and regulates mechanisms in inflammatory responses, such as
CC infection or atherosclerosis. Able to inhibit lipid droplet size in
CC adipocytes. Following incorporation into mature adipocytes via CD36-
CC mediated endocytosis, associates with cytosolic FASN, inhibiting fatty
CC acid synthase activity and leading to lipolysis, the degradation of
CC triacylglycerols into glycerol and free fatty acids (FFA). CD5L-induced
CC lipolysis occurs with progression of obesity: participates in obesity-
CC associated inflammation following recruitment of inflammatory
CC macrophages into adipose tissues, a cause of insulin resistance and
CC obesity-related metabolic disease. Regulation of intracellular lipids
CC mediated by CD5L has a direct effect on transcription regulation
CC mediated by nuclear receptors ROR-gamma (RORC). Acts as a key regulator
CC of metabolic switch in T-helper Th17 cells. Regulates the expression of
CC pro-inflammatory genes in Th17 cells by altering the lipid content and
CC limiting synthesis of cholesterol ligand of RORC, the master
CC transcription factor of Th17-cell differentiation. CD5L is mainly
CC present in non-pathogenic Th17 cells, where it decreases the content of
CC polyunsaturated fatty acyls (PUFA), affecting two metabolic proteins
CC MSMO1 and CYP51A1, which synthesize ligands of RORC, limiting RORC
CC activity and expression of pro-inflammatory genes. Participates in
CC obesity-associated autoimmunity via its association with IgM,
CC interfering with the binding of IgM to Fcalpha/mu receptor and
CC enhancing the development of long-lived plasma cells that produce high-
CC affinity IgG autoantibodies (By similarity). Also acts as an inhibitor
CC of apoptosis in macrophages: promotes macrophage survival from the
CC apoptotic effects of oxidized lipids in case of atherosclerosis
CC (PubMed:24295828). Involved in early response to microbial infection
CC against various pathogens by acting as a pattern recognition receptor
CC and by promoting autophagy (PubMed:16030018, PubMed:24223991,
CC PubMed:24583716, PubMed:25713983). {ECO:0000250|UniProtKB:Q9QWK4,
CC ECO:0000269|PubMed:16030018, ECO:0000269|PubMed:24223991,
CC ECO:0000269|PubMed:24295828, ECO:0000269|PubMed:24583716,
CC ECO:0000269|PubMed:25713983}.
CC -!- SUBUNIT: Interacts with FASN; the interaction is direct (By
CC similarity). Interacts with IgM; protecting CD5L from renal excretion
CC and leading to increased CD5L levels in circulating blood
CC (PubMed:8034987, PubMed:24804991). {ECO:0000250|UniProtKB:Q9QWK4,
CC ECO:0000269|PubMed:24804991, ECO:0000269|PubMed:8034987}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24223991,
CC ECO:0000269|PubMed:24804991}. Cytoplasm {ECO:0000250|UniProtKB:Q9QWK4}.
CC Note=Secreted by macrophages and circulates in the blood
CC (PubMed:24223991, PubMed:24804991). Transported in the cytoplasm via
CC CD36-mediated endocytosis (By similarity).
CC {ECO:0000250|UniProtKB:Q9QWK4, ECO:0000269|PubMed:24223991,
CC ECO:0000269|PubMed:24804991}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, lymph node, thymus, bone
CC marrow, and fetal liver, but not in non-lymphoid tissues.
CC {ECO:0000269|PubMed:9045627}.
CC -!- PTM: Not N-glycosylated (PubMed:23236605). Probably not O-glycosylated
CC (PubMed:23236605). {ECO:0000269|PubMed:23236605}.
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DR EMBL; U82812; AAB91989.1; -; mRNA.
DR EMBL; AF011429; AAD01446.1; -; mRNA.
DR EMBL; AY358494; AAQ88858.1; -; mRNA.
DR EMBL; AK292040; BAF84729.1; -; mRNA.
DR EMBL; AL139409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52859.1; -; Genomic_DNA.
DR EMBL; BC033586; AAH33586.1; -; mRNA.
DR CCDS; CCDS1171.1; -.
DR RefSeq; NP_001334627.1; NM_001347698.1.
DR RefSeq; NP_005885.1; NM_005894.2.
DR AlphaFoldDB; O43866; -.
DR SMR; O43866; -.
DR IntAct; O43866; 7.
DR STRING; 9606.ENSP00000357156; -.
DR GlyGen; O43866; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43866; -.
DR PhosphoSitePlus; O43866; -.
DR BioMuta; CD5L; -.
DR CPTAC; non-CPTAC-1092; -.
DR jPOST; O43866; -.
DR MassIVE; O43866; -.
DR PaxDb; O43866; -.
DR PeptideAtlas; O43866; -.
DR PRIDE; O43866; -.
DR ProteomicsDB; 49213; -.
DR Antibodypedia; 20452; 511 antibodies from 37 providers.
DR DNASU; 922; -.
DR Ensembl; ENST00000368174.5; ENSP00000357156.4; ENSG00000073754.6.
DR GeneID; 922; -.
DR KEGG; hsa:922; -.
DR MANE-Select; ENST00000368174.5; ENSP00000357156.4; NM_005894.3; NP_005885.1.
DR UCSC; uc001frk.5; human.
DR CTD; 922; -.
DR DisGeNET; 922; -.
DR GeneCards; CD5L; -.
DR HGNC; HGNC:1690; CD5L.
DR HPA; ENSG00000073754; Tissue enriched (lymphoid).
DR MIM; 602592; gene.
DR neXtProt; NX_O43866; -.
DR OpenTargets; ENSG00000073754; -.
DR PharmGKB; PA26229; -.
DR VEuPathDB; HostDB:ENSG00000073754; -.
DR eggNOG; ENOG502SHID; Eukaryota.
DR GeneTree; ENSGT00940000161974; -.
DR HOGENOM; CLU_002555_11_0_1; -.
DR InParanoid; O43866; -.
DR OMA; LHKGVWG; -.
DR OrthoDB; 158600at2759; -.
DR PhylomeDB; O43866; -.
DR TreeFam; TF329295; -.
DR PathwayCommons; O43866; -.
DR SignaLink; O43866; -.
DR BioGRID-ORCS; 922; 8 hits in 1063 CRISPR screens.
DR ChiTaRS; CD5L; human.
DR GeneWiki; CD5L; -.
DR GenomeRNAi; 922; -.
DR Pharos; O43866; Tbio.
DR PRO; PR:O43866; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43866; protein.
DR Bgee; ENSG00000073754; Expressed in spleen and 84 other tissues.
DR Genevisible; O43866; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:1903661; P:positive regulation of complement-dependent cytotoxicity; IEA:Ensembl.
DR GO; GO:0030449; P:regulation of complement activation; IEA:Ensembl.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR Gene3D; 3.10.250.10; -; 3.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR Pfam; PF00530; SRCR; 3.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 3.
DR SUPFAM; SSF56487; SSF56487; 3.
DR PROSITE; PS00420; SRCR_1; 2.
DR PROSITE; PS50287; SRCR_2; 3.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunity; Inflammatory response; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:15340161,
FT ECO:0000269|PubMed:8034987, ECO:0000269|PubMed:9045627"
FT CHAIN 20..347
FT /note="CD5 antigen-like"
FT /id="PRO_0000033225"
FT DOMAIN 24..125
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 138..239
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 244..346
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 33..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 49..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 62..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 96..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 163..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 176..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 208..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 253..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 269..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 282..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 315..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT VARIANT 117
FT /note="D -> E (in dbSNP:rs11537583)"
FT /id="VAR_033728"
FT MUTAGEN 123
FT /note="S->A: No effect; when associated with 129-A--A-132."
FT /evidence="ECO:0000269|PubMed:23236605"
FT MUTAGEN 129..132
FT /note="SSFS->AAFA: No effect; when associated with A-123."
FT /evidence="ECO:0000269|PubMed:23236605"
FT CONFLICT 347
FT /note="G -> V (in Ref. 3; AAQ88858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 38088 MW; 40A8BE08F9495D83 CRC64;
MALLFSLILA ICTRPGFLAS PSGVRLVGGL HRCEGRVEVE QKGQWGTVCD DGWDIKDVAV
LCRELGCGAA SGTPSGILYE PPAEKEQKVL IQSVSCTGTE DTLAQCEQEE VYDCSHDEDA
GASCENPESS FSPVPEGVRL ADGPGHCKGR VEVKHQNQWY TVCQTGWSLR AAKVVCRQLG
CGRAVLTQKR CNKHAYGRKP IWLSQMSCSG REATLQDCPS GPWGKNTCNH DEDTWVECED
PFDLRLVGGD NLCSGRLEVL HKGVWGSVCD DNWGEKEDQV VCKQLGCGKS LSPSFRDRKC
YGPGVGRIWL DNVRCSGEEQ SLEQCQHRFW GFHDCTHQED VAVICSG
