ID ERMAP_HUMAN Reviewed; 475 AA. AC Q96PL5; D3DPW8; Q5VV53; Q6DUE0; Q7Z3X0; Q8NCV8; Q8NCW2; Q8NCW3; Q96PL6; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 02-SEP-2026, entry version 187. DE RecName: Full=Erythroid membrane-associated protein; DE Short=hERMAP; DE AltName: Full=Radin blood group antigen; DE AltName: Full=Scianna blood group antigen; DE Flags: Precursor; GN Name=ERMAP; Synonyms=RD, SC; 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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Fetal liver; RX PubMed=11783959; DOI=10.1006/bcmd.2001.0465; RA Su Y.-Y., Gordon C.T., Ye T.-Z., Perkins A.C., Chui D.H.K.; RT "Human ERMAP: an erythroid adhesion/receptor transmembrane protein."; RL Blood Cells Mol. Dis. 27:938-949(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND RP SUBCELLULAR LOCATION. RC TISSUE=Fetal liver; RX PubMed=11549310; DOI=10.1006/geno.2001.6600; RA Xu H., Foltz L., Sha Y., Madlansacay M.R., Cain C., Lindemann G., RA Vargas J., Nagy D., Harriman B., Mahoney W., Schueler P.A.; RT "Cloning and characterization of human erythroid membrane-associated RT protein, human ERMAP."; RL Genomics 76:2-4(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE SC-3), POLYMORPHISM, AND VARIANTS RP TYR-26; ARG-57 AND ALA-60. RX PubMed=12393480; DOI=10.1182/blood-2002-07-2064; RA Wagner F.F., Poole J., Flegel W.A.; RT "Scianna antigens including Rd are expressed by ERMAP."; RL Blood 101:752-757(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-4; TYR-26; ARG-259 AND RP GLU-263. RG SeattleSNPs variation discovery resource; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [6] 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 [7] 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 [8] 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). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-144, POLYMORPHISM, AND VARIANT RP BLOOD GROUP SC5 LYS-47. RX PubMed=15660834; DOI=10.1111/j.1537-2995.2004.04226.x; RA Hue-Roye K., Chaudhuri A., Velliquette R.W., Fetics S., Thomas R., Balk M., RA Wagner F.F., Flegel W.A., Reid M.E.; RT "STAR: a novel high-prevalence antigen in the Scianna blood group system."; RL Transfusion 45:245-247(2005). RN [10] RP POLYMORPHISM, AND VARIANTS SER-35 AND GLN-81. RX PubMed=16371048; DOI=10.1111/j.1537-2995.2005.00646.x; RA Flegel W.A., Chen Q., Reid M.E., Martin J., Orsini L.A., Poole J., RA Moulds M.K., Wagner F.F.; RT "SCER and SCAN: two novel high-prevalence antigens in the Scianna blood RT group system."; RL Transfusion 45:1940-1944(2005). RN [11] 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). CC -!- FUNCTION: Possible role as a cell-adhesion or receptor molecule of CC erythroid cells. CC -!- INTERACTION: CC Q96PL5; P50402: EMD; NbExp=3; IntAct=EBI-13361852, EBI-489887; CC Q96PL5; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-13361852, EBI-3957694; CC Q96PL5; Q68G75: LEMD1; NbExp=3; IntAct=EBI-13361852, EBI-12268900; CC Q96PL5; Q9Y6G1: TMEM14A; NbExp=3; IntAct=EBI-13361852, EBI-2800360; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11783959}; CC Single-pass type I membrane protein {ECO:0000255}. Cytoplasm CC {ECO:0000269|PubMed:11783959}. CC -!- TISSUE SPECIFICITY: Expressed in erythroid-enriched bone marrow (at CC protein level). Highly expressed in bone marrow and to a lower extent CC in leukocytes, thymus, lymph node and spleen. CC {ECO:0000269|PubMed:11549310, ECO:0000269|PubMed:11783959}. CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver blood cells (at protein CC level). Highly expressed in fetal liver. {ECO:0000269|PubMed:11549310, CC ECO:0000269|PubMed:11783959}. CC -!- PTM: Glycosylated. CC -!- POLYMORPHISM: ERMAP is responsible for the Scianna/Radin blood group CC system which comprises seven different antigens (PubMed:12393480). The CC Sc1 and Sc2 antigens are resulting from a single variation in position CC 57; Arg-57 corresponds to the Sc2 antigen and Gly-57 to the Sc1 CC antigen. The Sc2 antigen is rare with an occurrence of less than 1% in CC the population while Sc1 is more frequent. Sc3 is not expressed by CC individuals homozygous for a null allele encoding a truncated protein CC lacking its extracellular part (Sc-3). The Sc4 antigen corresponding to CC the previously defined Radin blood group antigen (Rd) is due to a CC single variation in position 60; Ala-60 corresponds to Sc4/Rd(+), the CC antigenic form of the protein. Sc4 is found in less than 1% of the CC population. Sc5/STAR, Sc6/SCER and Sc7/SCAN antigens are due to single CC variations in positions 47, 81 and 35 respectively. Alloantibodies to CC the low frequency Sc2 and Sc4 antigens are the cause of hemolytic CC disease in the newborn (PubMed:15660834, PubMed:16371048). CC {ECO:0000269|PubMed:12393480, ECO:0000269|PubMed:15660834, CC ECO:0000269|PubMed:16371048}. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family. CC {ECO:0000305}. 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; AY049028; AAL11456.1; -; mRNA. DR EMBL; AF311284; AAL08411.1; -; mRNA. DR EMBL; AF311285; AAL08412.1; -; mRNA. DR EMBL; AJ505028; CAD43739.1; -; Genomic_DNA. DR EMBL; AJ505036; CAD43740.1; -; Genomic_DNA. DR EMBL; AJ505037; CAD43740.1; JOINED; Genomic_DNA. DR EMBL; AJ505038; CAD43740.1; JOINED; Genomic_DNA. DR EMBL; AJ505039; CAD43740.1; JOINED; Genomic_DNA. DR EMBL; AJ505040; CAD43740.1; JOINED; Genomic_DNA. DR EMBL; AJ505041; CAD43740.1; JOINED; Genomic_DNA. DR EMBL; AJ505042; CAD43740.1; JOINED; Genomic_DNA. DR EMBL; AJ505044; CAD43741.1; -; Genomic_DNA. DR EMBL; AJ505045; CAD43741.1; JOINED; Genomic_DNA. DR EMBL; AJ505046; CAD43741.1; JOINED; Genomic_DNA. DR EMBL; AJ505047; CAD43741.1; JOINED; Genomic_DNA. DR EMBL; AJ505048; CAD43741.1; JOINED; Genomic_DNA. DR EMBL; AJ505049; CAD43741.1; JOINED; Genomic_DNA. DR EMBL; AJ505050; CAD43741.1; JOINED; Genomic_DNA. DR EMBL; BX537371; CAD97613.2; -; mRNA. DR EMBL; DQ090843; AAY88736.1; -; Genomic_DNA. DR EMBL; AL512353; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07130.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07133.1; -; Genomic_DNA. DR EMBL; BC099703; AAH99703.1; -; mRNA. DR EMBL; BC099707; AAH99707.1; -; mRNA. DR EMBL; BC099712; AAH99712.1; -; mRNA. DR EMBL; BC099713; AAH99713.1; -; mRNA. DR EMBL; AY644424; AAT66409.1; -; Genomic_DNA. DR CCDS; CCDS475.1; -. DR RefSeq; NP_001017922.1; NM_001017922.2. DR RefSeq; NP_061008.2; NM_018538.4. DR RefSeq; XP_006710376.1; XM_006710313.5. DR RefSeq; XP_011538872.1; XM_011540570.4. DR RefSeq; XP_047299547.1; XM_047443591.1. DR RefSeq; XP_054190060.1; XM_054334085.1. DR RefSeq; XP_054190061.1; XM_054334086.1. DR RefSeq; XP_054190062.1; XM_054334087.1. DR AlphaFoldDB; Q96PL5; -. DR SMR; Q96PL5; -. DR BioGRID; 125328; 28. DR FunCoup; Q96PL5; 434. DR IntAct; Q96PL5; 25. DR MINT; Q96PL5; -. DR NDEx; IQUERY-CP-ERMAP; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000361595; -. DR GlyCosmos; Q96PL5; 1 site, No reported glycans. DR GlyGen; Q96PL5; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q96PL5; -. DR PhosphoSitePlus; Q96PL5; -. DR BioMuta; ERMAP; -. DR DMDM; 74761033; -. DR jPOST; Q96PL5; -. DR MassIVE; Q96PL5; -. DR PaxDb; 9606-ENSP00000361595; -. DR PeptideAtlas; Q96PL5; -. DR ProteomicsDB; 77708; -. DR Pumba; Q96PL5; -. DR Antibodypedia; 18175; 325 antibodies from 28 providers. DR DNASU; 114625; -. DR Ensembl; ENST00000372514.7; ENSP00000361592.3; ENSG00000164010.16. DR Ensembl; ENST00000372517.8; ENSP00000361595.2; ENSG00000164010.16. DR Ensembl; ENST00000881413.1; ENSP00000551472.1; ENSG00000164010.16. DR Ensembl; ENST00000881416.1; ENSP00000551475.1; ENSG00000164010.16. DR Ensembl; ENST00000881418.1; ENSP00000551477.1; ENSG00000164010.16. DR Ensembl; ENST00000881419.1; ENSP00000551478.1; ENSG00000164010.16. DR Ensembl; ENST00000881420.1; ENSP00000551479.1; ENSG00000164010.16. DR Ensembl; ENST00000968887.1; ENSP00000638946.1; ENSG00000164010.16. DR Ensembl; ENST00000968888.1; ENSP00000638947.1; ENSG00000164010.16. DR GeneID; 114625; -. DR KEGG; hsa:114625; -. DR MANE-Select; ENST00000372517.8; ENSP00000361595.2; NM_001017922.2; NP_001017922.1. DR UCSC; uc001cic.2; human. DR AGR; HGNC:15743; -. DR ClinPGx; PA27860; -. DR CTD; 114625; -. DR DisGeNET; 114625; -. DR GeneCards; ERMAP; -. DR HGNC; HGNC:15743; ERMAP. DR HPA; ENSG00000164010; Low tissue specificity. DR MalaCards; ERMAP; -. DR MIM; 111620; phenotype. DR MIM; 111750; phenotype. DR MIM; 609017; gene. DR OpenTargets; ENSG00000164010; -. DR VEuPathDB; HostDB:ENSG00000164010; -. DR eggNOG; KOG2177; Eukaryota. DR GeneTree; ENSGT00940000160531; -. DR InParanoid; Q96PL5; -. DR OMA; LGDRKQP; -. DR OrthoDB; 6270329at2759; -. DR PAN-GO; Q96PL5; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q96PL5; -. DR PathwayCommons; Q96PL5; -. DR SignaLink; Q96PL5; -. DR SIGNOR; Q96PL5; -. DR Agora; ENSG00000164010; -. DR BioGRID-ORCS; 114625; 15 hits in 1151 CRISPR screens. DR ChiTaRS; ERMAP; human. DR GeneWiki; ERMAP; -. DR GenomeRNAi; 114625; -. DR Pharos; Q96PL5; Tbio. DR PRO; PR:Q96PL5; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q96PL5; protein. DR Bgee; ENSG00000164010; Expressed in monocyte and 124 other cell types or tissues. DR ExpressionAtlas; Q96PL5; baseline and differential. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central. DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central. DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central. DR CDD; cd15813; SPRY_PRY_TRIM20; 1. DR FunFam; 2.60.120.920:FF:000004; Butyrophilin subfamily 1 member A1; 1. DR FunFam; 2.60.40.10:FF:001695; Erythroblast membrane associated protein (Scianna blood group); 1. DR Gene3D; 2.60.120.920; -; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR001870; B30.2/SPRY. DR InterPro; IPR043136; B30.2/SPRY_sf. DR InterPro; IPR003879; Butyrophylin_SPRY. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR InterPro; IPR006574; PRY. DR InterPro; IPR003877; SPRY_dom. DR InterPro; IPR050143; TRIM/RBCC. DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1. DR Pfam; PF13765; PRY; 1. DR Pfam; PF00622; SPRY; 1. DR Pfam; PF07686; V-set; 1. DR PRINTS; PR01407; BUTYPHLNCDUF. DR SMART; SM00409; IG; 1. DR SMART; SM00406; IGv; 1. DR SMART; SM00589; PRY; 1. DR SMART; SM00449; SPRY; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR PROSITE; PS50188; B302_SPRY; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Blood group antigen; Cell membrane; Cytoplasm; Disulfide bond; KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein; KW Proteomics identification; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..475 FT /note="Erythroid membrane-associated protein" FT /id="PRO_0000226088" FT TOPO_DOM 30..155 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 156..176 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 177..475 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 30..140 FT /note="Ig-like V-type" FT DOMAIN 220..418 FT /note="B30.2/SPRY" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548" FT MOD_RES 418 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLN5" FT CARBOHYD 132 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 50..126 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VARIANT 4 FT /note="A -> V (in dbSNP:rs35757049)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_025478" FT VARIANT 26 FT /note="H -> Y (in dbSNP:rs33953680)" FT /evidence="ECO:0000269|PubMed:12393480, ECO:0000269|Ref.5" FT /id="VAR_025479" FT VARIANT 35 FT /note="G -> S (in Sc7 antigen; dbSNP:rs146429994)" FT /evidence="ECO:0000269|PubMed:16371048" FT /id="VAR_025480" FT VARIANT 47 FT /note="E -> K (in Sc5 antigen; dbSNP:rs56047316)" FT /evidence="ECO:0000269|PubMed:15660834" FT /id="VAR_025481" FT VARIANT 57 FT /note="G -> R (in Sc2 antigen; dbSNP:rs56025238)" FT /evidence="ECO:0000269|PubMed:12393480" FT /id="VAR_025482" FT VARIANT 60 FT /note="P -> A (in Sc4 antigen; dbSNP:rs56136737)" FT /evidence="ECO:0000269|PubMed:12393480" FT /id="VAR_025483" FT VARIANT 81 FT /note="R -> Q (in Sc6 antigen; dbSNP:rs368064875)" FT /evidence="ECO:0000269|PubMed:16371048" FT /id="VAR_025484" FT VARIANT 103..113 FT /note="DAQEGSVTLQI -> CPRGKCHSADP (in Sc-3 allele)" FT /id="VAR_025485" FT VARIANT 114..475 FT /note="Missing (in Sc-3 allele)" FT /id="VAR_025486" FT VARIANT 259 FT /note="C -> R (in dbSNP:rs35147822)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_025487" FT VARIANT 263 FT /note="G -> E (in dbSNP:rs34441268)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_025488" FT CONFLICT 452 FT /note="L -> P (in Ref. 4; CAD97613)" FT /evidence="ECO:0000305" SQ SEQUENCE 475 AA; 52605 MW; D796B0951EA02E0F CRC64; MEMASSAGSW LSGCLIPLVF LRLSVHVSGH AGDAGKFHVA LLGGTAELLC PLSLWPGTVP KEVRWLRSPF PQRSQAVHIF RDGKDQDEDL MPEYKGRTVL VRDAQEGSVT LQILDVRLED QGSYRCLIQV GNLSKEDTVI LQVAAPSVGS LSPSAVALAV ILPVLVLLIM VCLCLIWKQR RAKEKLLYEH VTEVDNLLSD HAKEKGKLHK AVKKLRSELK LKRAAANSGW RRARLHFVAV TLDPDTAHPK LILSEDQRCV RLGDRRQPVP DNPQRFDFVV SILGSEYFTT GCHYWEVYVG DKTKWILGVC SESVSRKGKV TASPANGHWL LRQSRGNEYE ALTSPQTSFR LKEPPRCVGI FLDYEAGVIS FYNVTNKSHI FTFTHNFSGP LRPFFEPCLH DGGKNTAPLV ICSELHKSEE SIVPRPEGKG HANGDVSLKV NSSLLPPKAP ELKDIILSLP PDLGPALQEL KAPSF //