ID C163A_HUMAN Reviewed; 1156 AA. AC Q86VB7; Q07898; Q07899; Q07900; Q07901; Q2VLH7; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 20-APR-2010, entry version 64. DE RecName: Full=Scavenger receptor cysteine-rich type 1 protein M130; DE AltName: Full=Hemoglobin scavenger receptor; DE AltName: CD_antigen=CD163; DE Contains: DE RecName: Full=Soluble CD163; DE Short=sCD163; DE Flags: Precursor; GN Name=CD163; Synonyms=M130; 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; 2; 3 AND 4). RX MEDLINE=93380506; PubMed=8370408; DOI=10.1002/eji.1830230940; RA Law S.K.A., Micklem K.J., Shaw J.M., Zhang X.-P., Dong Y., RA Willis A.C., Mason D.Y.; RT "A new macrophage differentiation antigen which is a member of the RT scavenger receptor superfamily."; RL Eur. J. Immunol. 23:2320-2325(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10403791; DOI=10.1006/bbrc.1999.0866; RA Ritter M., Buechler C., Langmann T., Schmitz G.; RT "Genomic organization and chromosomal localization of the human CD163 RT (M130) gene: a member of the scavenger receptor cysteine-rich RT superfamily."; RL Biochem. Biophys. Res. Commun. 260:466-474(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Welch S.-K.W., Calvert J.G., Slade D.E., Shields S.L.; RT "Scavenger receptor cd163 is a cell permissive factor for infection RT with porcine reproductive and respiratory syndrome viruses."; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=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 [5] RP CLEAVAGE. RX PubMed=10066432; DOI=10.1006/bbrc.1999.0294; RA Droste A., Sorg C., Hogger P.; RT "Shedding of CD163, a novel regulatory mechanism for a member of the RT scavenger receptor cysteine-rich family."; RL Biochem. Biophys. Res. Commun. 256:110-113(1999). RN [6] RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION. RX PubMed=10577520; RA Van den Heuvel M.M., Tensen C.P., van As J.H., Van den Berg T.K., RA Fluitsma D.M., Dijkstra C.D., Dopp E.A., Droste A., Van Gaalen F.A., RA Sorg C., Hoegger P., Beelen R.H.J.; RT "Regulation of CD 163 on human macrophages: cross-linking of CD163 RT induces signaling and activation."; RL J. Leukoc. Biol. 66:858-866(1999). RN [7] RP INDUCTION, AND SUBCELLULAR LOCATION. RX PubMed=10648003; RA Buechler C., Ritter M., Orso E., Langmann T., Klucken J., Schmitz G.; RT "Regulation of scavenger receptor CD163 expression in human monocytes RT and macrophages by pro- and antiinflammatory stimuli."; RL J. Leukoc. Biol. 67:97-103(2000). RN [8] RP FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF THR-1072 AND SER-1084, AND RP INTERACTION WITH CSNK2B. RX PubMed=11298324; RX DOI=10.1002/1521-4141(200104)31:4<999::AID-IMMU999>3.0.CO;2-R; RA Ritter M., Buechler C., Kapinsky M., Schmitz G.; RT "Interaction of CD163 with the regulatory subunit of casein kinase II RT (CKII) and dependence of CD163 signaling on CKII and protein kinase RT C."; RL Eur. J. Immunol. 31:999-1009(2001). RN [9] RP FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS RP SPECTROMETRY. RX PubMed=11196644; DOI=10.1038/35051594; RA Kristiansen M., Graversen J.H., Jacobsen C., Sonne O., Hoffman H.-J., RA Law S.K.A., Moestrup S.K.; RT "Identification of the haemoglobin scavenger receptor."; RL Nature 409:198-201(2001). RN [10] RP CLEAVAGE. RX PubMed=12296867; DOI=10.1046/j.1365-2249.2002.01963.x; RA Matsushita N., Kashiwagi M., Wait R., Nagayoshi R., Nakamura M., RA Matsuda T., Hogger P., Guyre P.M., Nagase H., Matsuyama T.; RT "Elevated levels of soluble CD163 in sera and fluids from rheumatoid RT arthritis patients and inhibition of the shedding of CD163 by TIMP- RT 3."; RL Clin. Exp. Immunol. 130:156-161(2002). RN [11] RP FUNCTION. RX PubMed=12208511; DOI=10.1016/S0014-5793(02)03142-3; RA Frings W., Dreier J., Sorg C.; RT "Only the soluble form of the scavenger receptor CD163 acts inhibitory RT on phorbol ester-activated T-lymphocytes, whereas membrane-bound RT protein has no effect."; RL FEBS Lett. 526:93-96(2002). RN [12] RP MISCELLANEOUS. RX PubMed=12377940; RA Hintz K.A., Rassias A.J., Wardwell K., Moss M.L., Morganelli P.M., RA Pioli P.A., Givan A.L., Wallace P.K., Yeager M.P., Guyre P.M.; RT "Endotoxin induces rapid metalloproteinase-mediated shedding followed RT by up-regulation of the monocyte hemoglobin scavenger receptor RT CD163."; RL J. Leukoc. Biol. 72:711-717(2002). RN [13] RP RELEVANCE AS DISEASE MARKER IN INFLAMMATORY CONDITIONS. RX PubMed=15478309; DOI=10.1080/07853890410033171; RA Moestrup S.K., Moller H.J.; RT "CD163: a regulated hemoglobin scavenger receptor with a role in the RT anti-inflammatory response."; RL Ann. Med. 36:347-354(2004). RN [14] RP DOMAIN, AND CLEAVAGE SITES. RX PubMed=15448162; DOI=10.1074/jbc.M409629200; RA Madsen M., Moller H.J., Nielsen M.J., Jacobsen C., Graversen J.H., RA van den Berg T., Moestrup S.K.; RT "Molecular characterization of the haptoglobin.hemoglobin receptor RT CD163. Ligand binding properties of the scavenger receptor cysteine- RT rich domain region."; RL J. Biol. Chem. 279:51561-51567(2004). RN [15] RP CLEAVAGE. RX PubMed=15075364; DOI=10.1189/jlb.1003523; RA Sulahian T.H., Pioli P.A., Wardwell K., Guyre P.M.; RT "Cross-linking of FcgammaR triggers shedding of the hemoglobin- RT haptoglobin scavenger receptor CD163."; RL J. Leukoc. Biol. 76:271-277(2004). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105, AND MASS RP SPECTROMETRY. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [17] RP FUNCTION, MUTAGENESIS OF TYR-1096, AND TISSUE SPECIFICITY. RX PubMed=16434690; DOI=10.1189/jlb.1005602; RA Nielsen M.J., Madsen M., Moller H.J., Moestrup S.K.; RT "The macrophage scavenger receptor CD163: endocytic properties of RT cytoplasmic tail variants."; RL J. Leukoc. Biol. 79:837-845(2006). RN [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105; ASN-140; ASN-767 AND RP ASN-1027, AND MASS SPECTROMETRY. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). CC -!- FUNCTION: Acute phase-regulated receptor involved in clearance and CC endocytosis of hemoglobin/haptoglobin complexes by macrophages and CC may thereby protect tissues from free hemoglobin-mediated CC oxidative damage. May play a role in the uptake and recycling of CC iron, via endocytosis of hemoglobin/haptoglobin and subsequent CC breakdown of heme. Binds hemoglobin/haptoglobin complexes in a CC calcium-dependent and pH-dependent manner. Exhibits a higher CC affinity for complexes of hemoglobin and multimeric haptoglobin of CC HP*1F phenotype than for complexes of hemoglobin and dimeric CC haptoglobin of HP*1S phenotype. Induces a cascade of intracellular CC signals that involves tyrosine kinase-dependent calcium CC mobilization, inositol triphosphate production and secretion of CC IL6 and CSF1. Isoform 3 exhibits the higher capacity for ligand CC endocytosis and the more pronounced surface expression when CC expressed in cells. CC -!- FUNCTION: After shedding, the soluble form (sCD163) may play an CC anti-inflammatory role, and may be a valuable diagnostic parameter CC for monitoring macrophage activation in inflammatory conditions. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.0 nM for hemoglobin/haptoglobin of HP*1S phenotype; CC KM=0.2 nM for hemoglobin/haptoglobin of HP*1F phenotype; CC -!- SUBUNIT: Interacts with CSNK2B. CC -!- SUBCELLULAR LOCATION: Soluble CD163: Secreted. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Note=Isoform 1 and isoform 2 show a lower surface CC expression when expressed in cells. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Long tail variant 1; CC IsoId=Q86VB7-1; Sequence=Displayed; CC Name=2; Synonyms=Long tail variant 2; CC IsoId=Q86VB7-2; Sequence=VSP_019014; CC Name=3; Synonyms=Short tail variant; CC IsoId=Q86VB7-3; Sequence=VSP_019015; CC Name=4; CC IsoId=Q86VB7-4; Sequence=VSP_019013, VSP_019015; CC -!- TISSUE SPECIFICITY: Expressed in monocytes and mature macrophages CC such as Kupffer cells in the liver, red pulp macrophages in the CC spleen, cortical macrophages in the thymus, resident bone marrow CC macrophages and meningeal macrophages of the central nervous CC system. Expressed also in blood. Isoform 1 is the lowest abundant CC in the blood. Isoform 2 is the lowest abundant in the liver and CC the spleen. Isoform 3 is the predominant isoform detected in the CC blood. CC -!- INDUCTION: Induced by anti-inflammatory mediators such as CC glucocorticoids, IL6 and IL10; suppressed by proinflammatory CC mediators like lipopolysaccharide (LPS), Interferon gamma/IFNG, CC and tumor necrosis factor alpha. CC -!- DOMAIN: The SRCR domain 3 mediates calcium-sensitive interaction CC with hemoglobin/haptoglobin complexes. CC -!- PTM: A soluble form (sCD163) is produced by proteolytic shedding CC which can be induced by lipopolysaccharide, phorbol ester and Fc CC region of immunoglobulin gamma. This cleavage is dependent on CC protein kinase C and tyrosine kinases and can be blocked by CC protease inhibitors. The shedding is inhibited by the tissue CC inhibitor of metalloproteinase TIMP3, and thus probably induced by CC membrane-bound metalloproteinases ADAMs. CC -!- PTM: Phosphorylated (Probable). CC -!- MISCELLANEOUS: Intravenous lipopolysaccharide (LPS) produces a CC rapid rise of sCD163 in plasma of patient as it induces CC metalloproteinase-mediated shedding from monocytes surface. Long- CC term LPS infusion finally increases expression of the membrane- CC bound form on circulating monocytes. CC -!- MISCELLANEOUS: The soluble form (sCD163) in plasma is a novel CC parameter in diseases affecting macrophage function and CC monocyte/macrophage load in the body. The concentration of sCD163 CC is probably reflecting the number of macrophages of the CC 'alternative macrophage activation' phenotype with a high CD163 CC expression playing a major role in dampening the inflammatory CC response and scavenging components of damaged cells. This has CC initiated a number of clinical studies for evaluation of sCD163 as CC a disease marker in inflammatory conditions e.g. infection, CC autoimmune disease, transplantation, atherosclerosis and cancer. CC -!- SIMILARITY: Contains 9 SRCR domains. CC -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator. CC -!- SEQUENCE CAUTION: CC Sequence=CAA80541.1; Type=Erroneous initiation; CC Sequence=CAA80542.1; Type=Erroneous initiation; CC Sequence=CAA80543.1; Type=Erroneous initiation; CC Sequence=CAA80544.1; Type=Erroneous initiation; CC Sequence=CAB45233.1; Type=Erroneous initiation; 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; Z22968; CAA80541.1; ALT_INIT; mRNA. DR EMBL; Z22969; CAA80542.1; ALT_INIT; mRNA. DR EMBL; Z22970; CAA80543.1; ALT_INIT; mRNA. DR EMBL; Z22971; CAA80544.1; ALT_INIT; mRNA. DR EMBL; Y18388; CAB45233.1; ALT_INIT; Genomic_DNA. DR EMBL; Y18389; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18390; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18391; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18392; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18393; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18394; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18395; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18396; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18397; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18398; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18399; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18400; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18401; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18402; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; Y18403; CAB45233.1; JOINED; Genomic_DNA. DR EMBL; DQ058615; AAY99762.1; -; mRNA. DR EMBL; BC051281; AAH51281.1; -; mRNA. DR IPI; IPI00104074; -. DR IPI; IPI00513892; -. DR IPI; IPI00759642; -. DR IPI; IPI00953368; -. DR PIR; I38004; I38004. DR PIR; I38005; I38005. DR PIR; I38006; I38006. DR RefSeq; NP_004235.3; -. DR RefSeq; NP_981961.1; -. DR UniGene; Hs.504641; -. DR SMR; Q86VB7; 714-823, 926-1031. DR STRING; Q86VB7; -. DR PhosphoSite; Q86VB7; -. DR PRIDE; Q86VB7; -. DR Ensembl; ENST00000359156; ENSP00000352071; ENSG00000177575; Homo sapiens. DR GeneID; 9332; -. DR KEGG; hsa:9332; -. DR UCSC; uc001qsz.2; human. DR UCSC; uc001qta.2; human. DR UCSC; uc009zfw.1; human. DR CTD; 9332; -. DR GeneCards; GC12M007518; -. DR H-InvDB; HIX0026509; -. DR HGNC; HGNC:1631; CD163. DR HPA; CAB002432; -. DR MIM; 605545; gene. DR PharmGKB; PA26190; -. DR eggNOG; prNOG07926; -. DR HOVERGEN; HBG080943; -. DR InParanoid; Q86VB7; -. DR NextBio; 34955; -. DR ArrayExpress; Q86VB7; -. DR Bgee; Q86VB7; -. DR CleanEx; HS_CD163; -. DR Genevestigator; Q86VB7; -. DR GermOnline; ENSG00000177575; Homo sapiens. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0005044; F:scavenger receptor activity; NAS:UniProtKB. DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. DR InterPro; IPR001190; Srcr_rcpt. DR InterPro; IPR017448; Srcr_rcpt-rel. DR Pfam; PF00530; SRCR; 9. DR PRINTS; PR00258; SPERACTRCPTR. DR SMART; SM00202; SR; 9. DR SUPFAM; SSF56487; Srcr_receptor; 9. DR PROSITE; PS00420; SRCR_1; 4. DR PROSITE; PS50287; SRCR_2; 9. PE 1: Evidence at protein level; KW Acute phase; Alternative splicing; Cell membrane; Complete proteome; KW Disulfide bond; Glycoprotein; Inflammatory response; Membrane; KW Phosphoprotein; Polymorphism; Repeat; Secreted; Signal; Transmembrane. FT SIGNAL 1 41 Potential. FT CHAIN 42 1156 Scavenger receptor cysteine-rich type 1 FT protein M130. FT /FTId=PRO_0000238938. FT CHAIN 42 ? Soluble CD163. FT /FTId=PRO_0000238939. FT TOPO_DOM 42 1050 Extracellular (Potential). FT TRANSMEM 1051 1071 Potential. FT TOPO_DOM 1072 1156 Cytoplasmic (Potential). FT DOMAIN 51 152 SRCR 1. FT DOMAIN 159 259 SRCR 2. FT DOMAIN 266 366 SRCR 3. FT DOMAIN 373 473 SRCR 4. FT DOMAIN 478 578 SRCR 5. FT DOMAIN 583 683 SRCR 6. FT DOMAIN 719 819 SRCR 7. FT DOMAIN 824 926 SRCR 8. FT DOMAIN 929 1029 SRCR 9. FT MOTIF 1096 1099 Internalization signal. FT SITE 269 270 Cleavage; in calcium-free condition. FT SITE 281 282 Cleavage; in calcium-free condition. FT SITE 333 334 Cleavage; in calcium-free condition. FT SITE 360 361 Cleavage; in calcium-free condition. FT MOD_RES 14 14 Phosphoserine (By similarity). FT MOD_RES 1101 1101 Phosphoserine (By similarity). FT CARBOHYD 105 105 N-linked (GlcNAc...). FT CARBOHYD 140 140 N-linked (GlcNAc...). FT CARBOHYD 767 767 N-linked (GlcNAc...). FT CARBOHYD 1027 1027 N-linked (GlcNAc...). FT DISULFID 76 141 By similarity. FT DISULFID 89 151 By similarity. FT DISULFID 120 130 By similarity. FT DISULFID 184 248 By similarity. FT DISULFID 197 258 By similarity. FT DISULFID 228 238 By similarity. FT DISULFID 291 355 By similarity. FT DISULFID 304 365 By similarity. FT DISULFID 335 345 By similarity. FT DISULFID 398 462 By similarity. FT DISULFID 411 472 By similarity. FT DISULFID 442 452 By similarity. FT DISULFID 503 567 By similarity. FT DISULFID 516 577 By similarity. FT DISULFID 547 557 By similarity. FT DISULFID 608 672 By similarity. FT DISULFID 621 682 By similarity. FT DISULFID 652 662 By similarity. FT DISULFID 744 808 By similarity. FT DISULFID 757 818 By similarity. FT DISULFID 788 798 By similarity. FT DISULFID 864 925 By similarity. FT DISULFID 895 905 By similarity. FT DISULFID 954 1018 By similarity. FT DISULFID 967 1028 By similarity. FT DISULFID 998 1008 By similarity. FT VAR_SEQ 579 579 R -> SKTQKTSLIGSYTVKGTGLGSHSCLFLKPCLLPG FT (in isoform 4). FT /FTId=VSP_019013. FT VAR_SEQ 1115 1156 ENSHESADFSAAELISVSKFLPISGMEKEAILSHTEKENGN FT L -> GLWVLGGSIAQGFRSVAAVEAQTFYFDKQLKKSKNV FT IGSLDAYNGQE (in isoform 2). FT /FTId=VSP_019014. FT VAR_SEQ 1115 1156 ENSHESADFSAAELISVSKFLPISGMEKEAILSHTEKENGN FT L -> GGHSEPH (in isoform 3 and isoform FT 4). FT /FTId=VSP_019015. FT VARIANT 342 342 V -> I (in dbSNP:rs4883263). FT /FTId=VAR_026574. FT MUTAGEN 1072 1072 T->A: Impaired phosphorylation by PRKCA. FT MUTAGEN 1084 1084 S->A: Impaired phosphorylation by PRKCA. FT MUTAGEN 1096 1096 Y->A: Massive decrease of endocytotic FT activity. SQ SEQUENCE 1156 AA; 125437 MW; 60077F1A0EA691D4 CRC64; MSKLRMVLLE DSGSADFRRH FVNLSPFTIT VVLLLSACFV TSSLGGTDKE LRLVDGENKC SGRVEVKVQE EWGTVCNNGW SMEAVSVICN QLGCPTAIKA PGWANSSAGS GRIWMDHVSC RGNESALWDC KHDGWGKHSN CTHQQDAGVT CSDGSNLEMR LTRGGNMCSG RIEIKFQGRW GTVCDDNFNI DHASVICRQL ECGSAVSFSG SSNFGEGSGP IWFDDLICNG NESALWNCKH QGWGKHNCDH AEDAGVICSK GADLSLRLVD GVTECSGRLE VRFQGEWGTI CDDGWDSYDA AVACKQLGCP TAVTAIGRVN ASKGFGHIWL DSVSCQGHEP AVWQCKHHEW GKHYCNHNED AGVTCSDGSD LELRLRGGGS RCAGTVEVEI QRLLGKVCDR GWGLKEADVV CRQLGCGSAL KTSYQVYSKI QATNTWLFLS SCNGNETSLW DCKNWQWGGL TCDHYEEAKI TCSAHREPRL VGGDIPCSGR VEVKHGDTWG SICDSDFSLE AASVLCRELQ CGTVVSILGG AHFGEGNGQI WAEEFQCEGH ESHLSLCPVA PRPEGTCSHS RDVGVVCSRY TEIRLVNGKT PCEGRVELKT LGAWGSLCNS HWDIEDAHVL CQQLKCGVAL STPGGARFGK GNGQIWRHMF HCTGTEQHMG DCPVTALGAS LCPSEQVASV ICSGNQSQTL SSCNSSSLGP TRPTIPEESA VACIESGQLR LVNGGGRCAG RVEIYHEGSW GTICDDSWDL SDAHVVCRQL GCGEAINATG SAHFGEGTGP IWLDEMKCNG KESRIWQCHS HGWGQQNCRH KEDAGVICSE FMSLRLTSEA SREACAGRLE VFYNGAWGTV GKSSMSETTV GVVCRQLGCA DKGKINPASL DKAMSIPMWV DNVQCPKGPD TLWQCPSSPW EKRLASPSEE TWITCDNKIR LQEGPTSCSG RVEIWHGGSW GTVCDDSWDL DDAQVVCQQL GCGPALKAFK EAEFGQGTGP IWLNEVKCKG NESSLWDCPA RRWGHSECGH KEDAAVNCTD ISVQKTPQKA TTGRSSRQSS FIAVGILGVV LLAIFVALFF LTKKRRQRQR LAVSSRGENL VHQIQYREMN SCLNADDLDL MNSSENSHES ADFSAAELIS VSKFLPISGM EKEAILSHTE KENGNL //