ID HM13_MOUSE Reviewed; 378 AA. AC Q9D8V0; A3KGS1; O19444; Q15K37; Q3TXP0; Q542R3; Q811Z6; Q8HWA9; AC Q8HWB5; Q9CQA4; Q9CSK9; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 14-OCT-2015, entry version 132. DE RecName: Full=Minor histocompatibility antigen H13; DE EC=3.4.23.-; DE AltName: Full=Presenilin-like protein 3; DE AltName: Full=Signal peptide peptidase; GN Name=Hm13; Synonyms=H13, Psl3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Placenta; RX PubMed=12972007; DOI=10.1016/S1567-133X(03)00094-2; RA Urny J., Hermans-Borgmeyer I., Gercken G., Chica Schaller H.; RT "Expression of the presenilin-like signal peptide peptidase (SPP) in RT mouse adult brain and during development."; RL Gene Expr. Patterns 3:685-691(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=16730383; DOI=10.1016/j.bbaexp.2006.02.007; RA Urny J., Hermans-Borgmeyer I., Schaller H.C.; RT "Cell-surface expression of a new splice variant of the mouse signal RT peptide peptidase."; RL Biochim. Biophys. Acta 1759:159-165(2006). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=BALB/c; RA Irmler M., Tomiuk S., Korner M.R., Hofmann K., Conradt M.; RT "Characterization of a new protein family with homology to RT presenilins."; RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [GENOMIC DNA] OF 63-344. RC STRAIN=129P3/J; RA Brown A.C., Roopenian D.C.; RT "Genomic analysis of the H13 minor histocompatibility antigen gene."; RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; RC TISSUE=Adipose tissue, Cerebellum, Embryo, Lung, Ovary, Pancreas, RC Thymus, and Uterus; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [7] 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 [8] RP NUCLEOTIDE SEQUENCE OF 119-193 (ISOFORM 3), AND FUNCTION. RC STRAIN=BALB/c, C57BL/10, C57BL/6, C57BL/6J, and LP/J; RC TISSUE=Thymic lymphoma; RX PubMed=9354467; DOI=10.1016/S1074-7613(00)80368-4; RA Mendoza L.M., Paz P., Zuberi A., Christianson G.J., Roopenian D.C., RA Shastri N.; RT "Minors held by majors: the H13 minor histocompatibility locus defined RT as a peptide/MHC class I complex."; RL Immunity 7:461-472(1997). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 203-378 (ISOFORMS 1/3). RC STRAIN=FVB/N; TISSUE=Mammary gland; 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 [10] RP INTERACTION WITH RNF139. RX PubMed=19720873; DOI=10.1083/jcb.200906110; RA Stagg H.R., Thomas M., van den Boomen D., Wiertz E.J., Drabkin H.A., RA Gemmill R.M., Lehner P.J.; RT "The TRC8 E3 ligase ubiquitinates MHC class I molecules before RT dislocation from the ER."; RL J. Cell Biol. 186:685-692(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Liver, Lung, Pancreas, Spleen, and RC Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 169-177 IN COMPLEX WITH H2-D. RX PubMed=11751972; DOI=10.4049/jimmunol.168.1.283; RA Ostrov D.A., Roden M.M., Shi W., Palmieri E., Christianson G.J., RA Mendoza L., Villaflor G., Tilley D., Shastri N., Grey H., Almo S.C., RA Roopenian D.C., Nathenson S.G.; RT "How H13 histocompatibility peptides differing by a single methyl RT group and lacking conventional MHC binding anchor motifs determine RT self-nonself discrimination."; RL J. Immunol. 168:283-289(2002). CC -!- FUNCTION: Catalyzes intramembrane proteolysis of some signal CC peptides after they have been cleaved from a preprotein, resulting CC in the release of the fragment from the ER membrane into the CC cytoplasm. Required to generate lymphocyte cell surface (HLA-E) CC epitopes derived from MHC class I signal peptides. Involved in the CC intramembrane cleavage of the integral membrane protein PSEN1. CC Cleaves the integral membrane protein XBP1 isoform 1 in a CC DERL1/RNF139-dependent manner (By similarity). May play a role in CC graft rejection (PubMed:9354467). {ECO:0000250|UniProtKB:Q8TCT9, CC ECO:0000269|PubMed:9354467}. CC -!- SUBUNIT: Monomer. Homodimer (By similarity). Interacts with RNF139 CC (PubMed:19720873). Interacts with DERL1 and XBP1 isoform 1 (By CC similarity). {ECO:0000250|UniProtKB:Q8TCT9, CC ECO:0000269|PubMed:19720873}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:12972007, ECO:0000269|PubMed:16730383}; Multi- CC pass membrane protein {ECO:0000305}. Membrane CC {ECO:0000250|UniProtKB:Q8TCT9}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q8TCT9}; Lumenal side CC {ECO:0000250|UniProtKB:Q8TCT9}. CC -!- SUBCELLULAR LOCATION: Isoform 4: Cell membrane CC {ECO:0000269|PubMed:16730383}; Multi-pass membrane protein CC {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=SPP-alpha; CC IsoId=Q9D8V0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9D8V0-2; Sequence=VSP_005199, VSP_005200; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=Q9D8V0-3; Sequence=VSP_005201, VSP_005202; CC Name=4; Synonyms=SPP-beta; CC IsoId=Q9D8V0-4; Sequence=VSP_039805; CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in liver CC and kidney. In the brain, expressed predominantly in hippocampus, CC amygdala, piriform cortex, choroid plexus and arcuate nucleus of CC the hypothalamic area. Isoform 1 is more strongly expressed than CC isoform 4 in most tissues except brain and skeletal muscle where CC isoform 4 is the dominant isoform and in testis where isoform 1 CC and isoform 4 are expressed at similar levels. In the brain, CC isoform 4 is not detected in the choroid plexus. CC {ECO:0000269|PubMed:12972007, ECO:0000269|PubMed:16730383}. CC -!- DEVELOPMENTAL STAGE: In the embryo, expression starts at day 6.5. CC {ECO:0000269|PubMed:12972007}. CC -!- DOMAIN: The first transmembrane domain may act as a type I signal CC anchor. The PAL motif is required for normal active site CC conformation. {ECO:0000250|UniProtKB:P49768, CC ECO:0000250|UniProtKB:Q8TCT9}. CC -!- SIMILARITY: Belongs to the peptidase A22B family. {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; AF515662; AAN77098.1; -; mRNA. DR EMBL; DQ168449; ABA56162.1; -; mRNA. DR EMBL; AJ345032; CAC87793.1; -; mRNA. DR EMBL; AF483214; AAM22075.1; -; mRNA. DR EMBL; AF483216; AAM22077.1; -; Genomic_DNA. DR EMBL; AK004690; BAB23476.1; -; mRNA. DR EMBL; AK007664; BAB25172.1; -; mRNA. DR EMBL; AK012600; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK019877; BAB31897.1; -; mRNA. DR EMBL; AK028109; BAC25752.1; -; mRNA. DR EMBL; AK049101; BAC33543.1; -; mRNA. DR EMBL; AK050664; BAC34369.1; -; mRNA. DR EMBL; AK080966; BAC38098.1; -; mRNA. DR EMBL; AK159176; BAE34875.1; -; mRNA. DR EMBL; AK169922; BAE41461.1; -; mRNA. DR EMBL; AL845162; CAM46159.1; -; Genomic_DNA. DR EMBL; AL845162; CAM46160.1; -; Genomic_DNA. DR EMBL; CH466551; EDL05980.1; -; Genomic_DNA. DR EMBL; CH466551; EDL05981.1; -; Genomic_DNA. DR EMBL; AF017785; AAB81863.1; -; mRNA. DR EMBL; BC034217; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS16896.1; -. [Q9D8V0-1] DR CCDS; CCDS50752.1; -. [Q9D8V0-4] DR RefSeq; NP_001153023.1; NM_001159551.1. [Q9D8V0-4] DR RefSeq; NP_001153025.1; NM_001159553.1. [Q9D8V0-2] DR RefSeq; NP_034506.1; NM_010376.4. [Q9D8V0-1] DR UniGene; Mm.277327; -. DR PDB; 1INQ; X-ray; 2.20 A; C=169-177. DR PDB; 1JUF; X-ray; 2.00 A; C=169-177. DR PDBsum; 1INQ; -. DR PDBsum; 1JUF; -. DR ProteinModelPortal; Q9D8V0; -. DR MINT; MINT-1836977; -. DR MEROPS; A22.003; -. DR PhosphoSite; Q9D8V0; -. DR MaxQB; Q9D8V0; -. DR PaxDb; Q9D8V0; -. DR PRIDE; Q9D8V0; -. DR Ensembl; ENSMUST00000089059; ENSMUSP00000086460; ENSMUSG00000019188. [Q9D8V0-4] DR Ensembl; ENSMUST00000125366; ENSMUSP00000120068; ENSMUSG00000019188. [Q9D8V0-1] DR GeneID; 14950; -. DR KEGG; mmu:14950; -. DR UCSC; uc008nfz.2; mouse. [Q9D8V0-2] DR UCSC; uc008ngb.2; mouse. [Q9D8V0-1] DR UCSC; uc008ngc.2; mouse. [Q9D8V0-4] DR CTD; 14950; -. DR MGI; MGI:95886; H13. DR eggNOG; NOG313636; -. DR GeneTree; ENSGT00530000062920; -. DR HOVERGEN; HBG024161; -. DR InParanoid; Q9D8V0; -. DR KO; K09595; -. DR OMA; NYEFDAK; -. DR OrthoDB; EOG7Z3F4N; -. DR PhylomeDB; Q9D8V0; -. DR TreeFam; TF105854; -. DR EvolutionaryTrace; Q9D8V0; -. DR NextBio; 287291; -. DR PRO; PR:Q9D8V0; -. DR Proteomes; UP000000589; Chromosome 2. DR Bgee; Q9D8V0; -. DR CleanEx; MM_H13; -. DR ExpressionAtlas; Q9D8V0; baseline and differential. DR Genevisible; Q9D8V0; MM. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; ISO:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI. DR GO; GO:0071458; C:integral component of cytoplasmic side of endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; ISS:UniProtKB. DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0033619; P:membrane protein proteolysis; ISS:UniProtKB. DR GO; GO:1904211; P:membrane protein proteolysis involved in retrograde protein transport, ER to cytosol; ISO:MGI. DR InterPro; IPR007369; Peptidase_A22B_SPP. DR InterPro; IPR006639; Preselin/SPP. DR PANTHER; PTHR12174; PTHR12174; 1. DR Pfam; PF04258; Peptidase_A22B; 1. DR SMART; SM00730; PSN; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Complete proteome; KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; KW Phosphoprotein; Protease; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 378 Minor histocompatibility antigen H13. FT /FTId=PRO_0000073908. FT TOPO_DOM 1 31 Lumenal. {ECO:0000250|UniProtKB:Q8TCT9}. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TOPO_DOM 53 77 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 78 98 Helical. {ECO:0000255}. FT TOPO_DOM 99 100 Lumenal. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TOPO_DOM 122 157 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 158 178 Helical. {ECO:0000255}. FT TOPO_DOM 179 181 Lumenal. {ECO:0000255}. FT TRANSMEM 182 202 Helical. {ECO:0000255}. FT TOPO_DOM 203 209 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 210 230 Helical. {ECO:0000255}. FT TOPO_DOM 231 256 Lumenal. {ECO:0000250|UniProtKB:Q8TCT9}. FT TRANSMEM 257 277 Helical. {ECO:0000255}. FT TOPO_DOM 278 290 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 291 311 Helical. {ECO:0000255}. FT TOPO_DOM 312 314 Lumenal. {ECO:0000255}. FT TRANSMEM 315 335 Helical. {ECO:0000255}. FT TOPO_DOM 336 378 Cytoplasmic. FT {ECO:0000250|UniProtKB:Q8TCT9}. FT MOTIF 317 319 PAL. FT ACT_SITE 219 219 {ECO:0000250|UniProtKB:P49810}. FT ACT_SITE 265 265 {ECO:0000250|UniProtKB:P49810}. FT MOD_RES 368 368 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8TCT9}. FT CARBOHYD 10 10 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 20 20 N-linked (GlcNAc...). {ECO:0000255}. FT VAR_SEQ 119 151 HTISPFMNKFFPANFPNRQYQLLFTQGSGENKE -> DDAD FT SHALLQALTGWGWGGSLTLGSELIWPLCP (in isoform FT 3). {ECO:0000305}. FT /FTId=VSP_005201. FT VAR_SEQ 122 173 SPFMNKFFPANFPNRQYQLLFTQGSGENKEEIINYEFDTKD FT LVCLGLSSVVG -> RSEGISRQPLKLLSQEPVQGLGWEHG FT LLCHSEPGLNPGCKIQGNLPSRQHYT (in isoform FT 2). {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_005199. FT VAR_SEQ 174 378 Missing (in isoform 2). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_005200. FT VAR_SEQ 181 193 HWIANNLFGLAFS -> VSQSLRRRGGWAD (in FT isoform 3). {ECO:0000305}. FT /FTId=VSP_005202. FT VAR_SEQ 348 378 ESNPKDPAAETESKEESTEASASKRLEKKEK -> SSAVIL FT PHTPRLTHFPTVSGSPASLADSMQQKLAGPRRRRPQNPSAM FT (in isoform 4). FT {ECO:0000303|PubMed:16730383}. FT /FTId=VSP_039805. FT CONFLICT 42 42 M -> T (in Ref. 2; ABA56162). FT {ECO:0000305}. FT CONFLICT 53 53 R -> P (in Ref. 3; CAC87793 and 4; FT AAM22075). {ECO:0000305}. FT CONFLICT 73 73 R -> Q (in Ref. 4; AAM22077). FT {ECO:0000305}. FT CONFLICT 172 172 V -> I (in Ref. 1; AAN77098, 4; AAM22077 FT and 5; BAE34875). {ECO:0000305}. FT CONFLICT 294 294 S -> E (in Ref. 5; BAC25752). FT {ECO:0000305}. FT CONFLICT 357 357 E -> V (in Ref. 1; AAN77098, 3; CAC87793, FT 4; AAM22075 and 5; BAE34875). FT {ECO:0000305}. SQ SEQUENCE 378 AA; 41748 MW; FB3B047323239A0D CRC64; MDSAVSDPHN GSAEAGTPAN GTTRPPSTPE GIALAYGSLL LMALLPIFFG ALRSVRCARG KSSSDMPETI TSRDAARFPI IASCTLLGLY LFFKIFSQEY INLLLSMYFF VLGILALSHT ISPFMNKFFP ANFPNRQYQL LFTQGSGENK EEIINYEFDT KDLVCLGLSS VVGVWYLLRK HWIANNLFGL AFSLNGVELL HLNNVSTGCI LLGGLFIYDI FWVFGTNVMV TVAKSFEAPI KLVFPQDLLE KGLEADNFAM LGLGDIVIPG IFIALLLRFD ISLKKNTHTY FYTSFAAYIF GLGLTIFIMH IFKHAQPALL YLVPACIGFP VLVALAKGEV AEMFSYEESN PKDPAAETES KEESTEASAS KRLEKKEK //