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 13-FEB-2019, entry version 146. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT binding characteristics of Spalpha, a new member of the scavenger RT receptor 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., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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., RA Spertini F., Clement F., Frutiger S., Paquet N., Hughes G.J., RA 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 RT verified 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., RA Valeri M., Cardona P.J., Sarrias M.R.; RT "The scavenger protein apoptosis inhibitor of macrophages (AIM) RT potentiates the antimicrobial response against Mycobacterium RT tuberculosis by enhancing 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., RA Orta Mascaro M., Carreras E., Martinez-Florensa M., Yelamos J., RA Miyazaki T., Lozano F.; RT "The macrophage soluble receptor AIM/Api6/CD5L displays a broad RT pathogen recognition spectrum and is involved in early response to RT microbial 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., RA Blanco-Vaca F., 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver 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 RT synthesized 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., RA Armengol C., Borras F.E., Sarrias M.R.; RT "The human CD5L/AIM-CD36 axis: A novel autophagy inducer in RT macrophages 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 CC inflammed tissues and regulates mechanisms in inflammatory CC responses, such as infection or atherosclerosis. Able to inhibit CC lipid droplet size in adipocytes. Following incorporation into CC mature adipocytes via CD36-mediated endocytosis, associates with CC cytosolic FASN, inhibiting fatty acid synthase activity and CC leading to lipolysis, the degradation of triacylglycerols into CC glycerol and free fatty acids (FFA). CD5L-induced lipolysis occurs CC with progression of obesity: participates in obesity-associated CC inflammation following recruitment of inflammatory macrophages CC into adipose tissues, a cause of insulin resistance and obesity- CC 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 CC regulator of metabolic switch in T-helper Th17 cells. Regulates CC the expression of pro-inflammatory genes in Th17 cells by altering CC the lipid content and limiting synthesis of cholesterol ligand of CC RORC, the master transcription factor of Th17-cell CC differentiation. CD5L is mainly present in non-pathogenic Th17 CC cells, where it decreases the content of polyunsaturated fatty CC acyls (PUFA), affecting two metabolic proteins MSMO1 and CYP51A1, CC which synthesize ligands of RORC, limiting RORC activity and CC expression of pro-inflammatory genes. Participates in obesity- CC associated autoimmunity via its association with IgM, interfering CC with the binding of IgM to Fcalpha/mu receptor and enhancing the CC development of long-lived plasma cells that produce high-affinity CC IgG autoantibodies (By similarity). Also acts as an inhibitor of CC 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 CC infection against various pathogens by acting as a pattern CC recognition receptor and by promoting autophagy (PubMed:16030018, CC PubMed:24223991, PubMed:24583716, PubMed:25713983). CC {ECO:0000250|UniProtKB:Q9QWK4, ECO:0000269|PubMed:16030018, CC ECO:0000269|PubMed:24223991, ECO:0000269|PubMed:24295828, CC ECO:0000269|PubMed:24583716, ECO:0000269|PubMed:25713983}. CC -!- SUBUNIT: Interacts with FASN; the interaction is direct (By CC similarity). Interacts with IgM; protecting CD5L from renal CC excretion and leading to increased CD5L levels in circulating CC blood (PubMed:8034987, PubMed:24804991). CC {ECO:0000250|UniProtKB:Q9QWK4, ECO:0000269|PubMed:24804991, CC ECO:0000269|PubMed:8034987}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24223991, CC ECO:0000269|PubMed:24804991}. Cytoplasm CC {ECO:0000250|UniProtKB:Q9QWK4}. Note=Secreted by macrophages and CC circulates in the blood (PubMed:24223991, PubMed:24804991). CC Transported in the cytoplasm via CD36-mediated endocytosis (By CC similarity). {ECO:0000250|UniProtKB:Q9QWK4, CC ECO:0000269|PubMed:24223991, 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- CC glycosylated (PubMed:23236605). {ECO:0000269|PubMed:23236605}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- 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 UniGene; Hs.134035; -. DR ProteinModelPortal; O43866; -. DR SMR; O43866; -. DR IntAct; O43866; 7. DR STRING; 9606.ENSP00000357156; -. DR iPTMnet; O43866; -. DR PhosphoSitePlus; O43866; -. DR BioMuta; CD5L; -. DR jPOST; O43866; -. DR PaxDb; O43866; -. DR PeptideAtlas; O43866; -. DR PRIDE; O43866; -. DR ProteomicsDB; 49213; -. DR DNASU; 922; -. DR Ensembl; ENST00000368174; ENSP00000357156; ENSG00000073754. DR GeneID; 922; -. DR KEGG; hsa:922; -. DR UCSC; uc001frk.5; human. DR CTD; 922; -. DR DisGeNET; 922; -. DR EuPathDB; HostDB:ENSG00000073754.5; -. DR GeneCards; CD5L; -. DR HGNC; HGNC:1690; CD5L. DR HPA; HPA065686; -. DR HPA; HPA068384; -. DR MIM; 602592; gene. DR neXtProt; NX_O43866; -. DR OpenTargets; ENSG00000073754; -. DR PharmGKB; PA26229; -. DR eggNOG; ENOG410IKHN; Eukaryota. DR eggNOG; ENOG4110209; LUCA. DR GeneTree; ENSGT00940000161974; -. DR HOGENOM; HOG000290652; -. DR HOVERGEN; HBG031373; -. DR InParanoid; O43866; -. DR OMA; YHGEDAS; -. DR OrthoDB; 158600at2759; -. DR PhylomeDB; O43866; -. DR TreeFam; TF329295; -. DR ChiTaRS; CD5L; human. DR GeneWiki; CD5L; -. DR GenomeRNAi; 922; -. DR PRO; PR:O43866; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000073754; Expressed in 61 organ(s), highest expression level in spleen. DR Genevisible; O43866; HS. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. 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:0016020; C:membrane; IEA:InterPro. DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro. 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 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; Complete proteome; Cytoplasm; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Immunity; Inflammatory response; KW Polymorphism; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1 19 {ECO:0000269|PubMed:15340161, FT ECO:0000269|PubMed:8034987, FT ECO:0000269|PubMed:9045627}. FT CHAIN 20 347 CD5 antigen-like. FT /FTId=PRO_0000033225. FT DOMAIN 24 125 SRCR 1. {ECO:0000255|PROSITE- FT ProRule:PRU00196}. FT DOMAIN 138 239 SRCR 2. {ECO:0000255|PROSITE- FT ProRule:PRU00196}. FT DOMAIN 244 346 SRCR 3. {ECO:0000255|PROSITE- FT ProRule:PRU00196}. FT DISULFID 33 67 {ECO:0000255|PROSITE-ProRule:PRU00196}. FT DISULFID 49 114 {ECO:0000255|PROSITE-ProRule:PRU00196}. FT DISULFID 62 124 {ECO:0000255|PROSITE-ProRule:PRU00196}. FT DISULFID 96 106 {ECO:0000255|PROSITE-ProRule:PRU00196}. FT DISULFID 163 228 {ECO:0000255|PROSITE-ProRule:PRU00196}. FT DISULFID 176 238 {ECO:0000255|PROSITE-ProRule:PRU00196}. FT DISULFID 208 218 {ECO:0000255|PROSITE-ProRule:PRU00196}. FT DISULFID 253 287 {ECO:0000255|PROSITE-ProRule:PRU00196}. FT DISULFID 269 335 {ECO:0000255|PROSITE-ProRule:PRU00196}. FT DISULFID 282 345 {ECO:0000255|PROSITE-ProRule:PRU00196}. FT DISULFID 315 325 {ECO:0000255|PROSITE-ProRule:PRU00196}. FT VARIANT 117 117 D -> E (in dbSNP:rs11537583). FT /FTId=VAR_033728. FT MUTAGEN 123 123 S->A: No effect; when associated with FT 129-A--A-132. FT {ECO:0000269|PubMed:23236605}. FT MUTAGEN 129 132 SSFS->AAFA: No effect; when associated FT with A-123. FT {ECO:0000269|PubMed:23236605}. FT CONFLICT 347 347 G -> V (in Ref. 3; AAQ88858). FT {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 //