ID RHDF2_HUMAN Reviewed; 856 AA. AC Q6PJF5; A6NEM3; A8K801; Q5U607; Q5YGQ8; Q9H6E9; DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 2. DT 22-FEB-2023, entry version 146. DE RecName: Full=Inactive rhomboid protein 2; DE Short=iRhom2; DE AltName: Full=Rhomboid 5 homolog 2; DE AltName: Full=Rhomboid family member 2; DE AltName: Full=Rhomboid veinlet-like protein 5; DE AltName: Full=Rhomboid veinlet-like protein 6; GN Name=RHBDF2; Synonyms=IRHOM2, RHBDL5, RHBDL6; 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] (ISOFORM 2), AND VARIANT LEU-208. RC TISSUE=Liver; RA Kong X., Teng X., Hu L.; RT "Molecular cloning of human RHBDL5."; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP LEU-208. RC TISSUE=Kidney epithelium, Spleen, and Synovium; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-208. RC TISSUE=Eye, and Uterus; 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-325 AND SER-328, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [7] RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND VARIANTS TOC THR-186 AND RP LEU-189. RX PubMed=22265016; DOI=10.1016/j.ajhg.2011.12.008; RA Blaydon D.C., Etheridge S.L., Risk J.M., Hennies H.C., Gay L.J., RA Carroll R., Plagnol V., McRonald F.E., Stevens H.P., Spurr N.K., RA Bishop D.T., Ellis A., Jankowski J., Field J.K., Leigh I.M., South A.P., RA Kelsell D.P.; RT "RHBDF2 mutations are associated with tylosis, a familial esophageal cancer RT syndrome."; RL Am. J. Hum. Genet. 90:340-346(2012). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-113; SER-325 AND RP SER-328, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [9] 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 [10] RP INTERACTION WITH ADAM17 AND FRMD8, AND SUBCELLULAR LOCATION. RX PubMed=29897333; DOI=10.7554/elife.35032; RA Oikonomidi I., Burbridge E., Cavadas M., Sullivan G., Collis B., RA Naegele H., Clancy D., Brezinova J., Hu T., Bileck A., Gerner C., RA Bolado A., von Kriegsheim A., Martin S.J., Steinberg F., Strisovsky K., RA Adrain C.; RT "iTAP, a novel iRhom interactor, controls TNF secretion by policing the RT stability of iRhom/TACE."; RL Elife 7:0-0(2018). RN [11] RP INTERACTION WITH ADAM17 AND FRMD8. RX PubMed=29897336; DOI=10.7554/elife.35012; RA Kuenzel U., Grieve A.G., Meng Y., Sieber B., Cowley S.A., Freeman M.; RT "FRMD8 promotes inflammatory and growth factor signalling by stabilising RT the iRhom/ADAM17 sheddase complex."; RL Elife 7:0-0(2018). CC -!- FUNCTION: Regulates ADAM17 protease, a sheddase of the epidermal growth CC factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, CC cell survival, proliferation, migration and inflammation. Does not CC exhibit any protease activity on its own. CC {ECO:0000250|UniProtKB:Q80WQ6}. CC -!- SUBUNIT: Interacts with EGF (By similarity). Interacts (via cytoplasmic CC N-terminus) with FRMD8/iTAP; this interaction leads to mutual protein CC stabilization (PubMed:29897333, PubMed:29897336). Interacts with CC ADAM17/TACE (PubMed:29897333, PubMed:29897336). CC {ECO:0000250|UniProtKB:Q80WQ6, ECO:0000269|PubMed:29897333, CC ECO:0000269|PubMed:29897336}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q80WQ6}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q80WQ6}. Cell membrane CC {ECO:0000269|PubMed:22265016, ECO:0000269|PubMed:29897333}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6PJF5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6PJF5-2; Sequence=VSP_034368; CC -!- TISSUE SPECIFICITY: Found in the epidermis and esophageal epithelium. CC {ECO:0000269|PubMed:22265016}. CC -!- DISEASE: Tylosis with esophageal cancer (TOC) [MIM:148500]: An CC autosomal dominant syndrome characterized by diffuse palmoplantar CC keratoderma, oral leukokeratosis, and a high lifetime risk of CC esophageal cancer. {ECO:0000269|PubMed:22265016}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH35829.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB15310.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AY500247; AAS77567.1; -; mRNA. DR EMBL; AK025994; BAB15310.1; ALT_INIT; mRNA. DR EMBL; AK292135; BAF84824.1; -; mRNA. DR EMBL; AK292166; BAF84855.1; -; mRNA. DR EMBL; AC015802; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC035829; AAH35829.1; ALT_INIT; mRNA. DR EMBL; BC016034; AAH16034.2; -; mRNA. DR CCDS; CCDS32743.1; -. [Q6PJF5-1] DR CCDS; CCDS32744.1; -. [Q6PJF5-2] DR RefSeq; NP_001005498.2; NM_001005498.3. [Q6PJF5-2] DR RefSeq; NP_078875.4; NM_024599.5. [Q6PJF5-1] DR RefSeq; XP_005257726.1; XM_005257669.3. [Q6PJF5-1] DR RefSeq; XP_005257727.1; XM_005257670.1. DR RefSeq; XP_011523551.1; XM_011525249.2. [Q6PJF5-2] DR RefSeq; XP_011523552.1; XM_011525250.2. [Q6PJF5-2] DR RefSeq; XP_011523553.1; XM_011525251.2. [Q6PJF5-2] DR RefSeq; XP_016880568.1; XM_017025079.1. DR AlphaFoldDB; Q6PJF5; -. DR BioGRID; 122779; 201. DR ELM; Q6PJF5; -. DR IntAct; Q6PJF5; 11. DR STRING; 9606.ENSP00000322775; -. DR MEROPS; S54.953; -. DR GlyGen; Q6PJF5; 1 site. DR iPTMnet; Q6PJF5; -. DR PhosphoSitePlus; Q6PJF5; -. DR BioMuta; RHBDF2; -. DR DMDM; 193806488; -. DR EPD; Q6PJF5; -. DR jPOST; Q6PJF5; -. DR MassIVE; Q6PJF5; -. DR MaxQB; Q6PJF5; -. DR PaxDb; Q6PJF5; -. DR PeptideAtlas; Q6PJF5; -. DR ProteomicsDB; 67199; -. [Q6PJF5-1] DR ProteomicsDB; 67200; -. [Q6PJF5-2] DR Antibodypedia; 19692; 101 antibodies from 22 providers. DR DNASU; 79651; -. DR Ensembl; ENST00000313080.8; ENSP00000322775.3; ENSG00000129667.13. [Q6PJF5-1] DR Ensembl; ENST00000591885.5; ENSP00000466867.1; ENSG00000129667.13. [Q6PJF5-2] DR Ensembl; ENST00000675367.1; ENSP00000501790.1; ENSG00000129667.13. [Q6PJF5-2] DR GeneID; 79651; -. DR KEGG; hsa:79651; -. DR MANE-Select; ENST00000675367.1; ENSP00000501790.1; NM_001005498.4; NP_001005498.2. [Q6PJF5-2] DR UCSC; uc002jrq.3; human. [Q6PJF5-1] DR AGR; HGNC:20788; -. DR CTD; 79651; -. DR DisGeNET; 79651; -. DR GeneCards; RHBDF2; -. DR HGNC; HGNC:20788; RHBDF2. DR HPA; ENSG00000129667; Low tissue specificity. DR MalaCards; RHBDF2; -. DR MIM; 148500; phenotype. DR MIM; 614404; gene. DR neXtProt; NX_Q6PJF5; -. DR OpenTargets; ENSG00000129667; -. DR Orphanet; 2198; Palmoplantar keratoderma-esophageal carcinoma syndrome. DR PharmGKB; PA134980674; -. DR VEuPathDB; HostDB:ENSG00000129667; -. DR eggNOG; KOG2290; Eukaryota. DR GeneTree; ENSGT00940000159027; -. DR HOGENOM; CLU_011531_1_1_1; -. DR InParanoid; Q6PJF5; -. DR OMA; IKRSFAY; -. DR OrthoDB; 315491at2759; -. DR PhylomeDB; Q6PJF5; -. DR TreeFam; TF312988; -. DR PathwayCommons; Q6PJF5; -. DR Reactome; R-HSA-9662834; CD163 mediating an anti-inflammatory response. DR SignaLink; Q6PJF5; -. DR BioGRID-ORCS; 79651; 13 hits in 1147 CRISPR screens. DR ChiTaRS; RHBDF2; human. DR GeneWiki; RHBDF2; -. DR GenomeRNAi; 79651; -. DR Pharos; Q6PJF5; Tbio. DR PRO; PR:Q6PJF5; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q6PJF5; protein. DR Bgee; ENSG00000129667; Expressed in granulocyte and 158 other tissues. DR ExpressionAtlas; Q6PJF5; baseline and differential. DR Genevisible; Q6PJF5; HS. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW. DR GO; GO:0140318; F:protein transporter activity; TAS:Reactome. DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; TAS:Reactome. DR GO; GO:0050709; P:negative regulation of protein secretion; ISS:UniProtKB. DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IBA:GO_Central. DR GO; GO:1904683; P:regulation of metalloendopeptidase activity; IEA:Ensembl. DR GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central. DR Gene3D; 1.20.1540.10; Rhomboid-like; 1. DR InterPro; IPR022241; iRhom1/2. DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom. DR InterPro; IPR035952; Rhomboid-like_sf. DR PANTHER; PTHR45965; INACTIVE RHOMBOID PROTEIN; 1. DR PANTHER; PTHR45965:SF2; INACTIVE RHOMBOID PROTEIN 2; 1. DR Pfam; PF01694; Rhomboid; 1. DR Pfam; PF12595; Rhomboid_SP; 1. DR SUPFAM; SSF144091; Rhomboid-like; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Disease variant; KW Endoplasmic reticulum; Growth factor binding; Membrane; KW Palmoplantar keratoderma; Phosphoprotein; Protein transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..856 FT /note="Inactive rhomboid protein 2" FT /id="PRO_0000341938" FT TOPO_DOM 1..409 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 410..430 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 431..660 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 661..681 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 682..692 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 693..713 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 714..715 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 716..736 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 737..747 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 748..768 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 769..773 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 774..794 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 795..802 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 803..823 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 824..856 FT /note="Lumenal" FT /evidence="ECO:0000255" FT REGION 1..115 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 165..184 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 191..271 FT /note="Involved in interaction with FRMD8" FT /evidence="ECO:0000269|PubMed:29897333" FT REGION 531..553 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..26 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 90 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 113 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 117 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80WQ6" FT MOD_RES 323 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80WQ6" FT MOD_RES 325 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 328 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 51..79 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1" FT /id="VSP_034368" FT VARIANT 186 FT /note="I -> T (in TOC; dbSNP:rs387907129)" FT /evidence="ECO:0000269|PubMed:22265016" FT /id="VAR_067827" FT VARIANT 189 FT /note="P -> L (in TOC; dbSNP:rs387907130)" FT /evidence="ECO:0000269|PubMed:22265016" FT /id="VAR_067828" FT VARIANT 208 FT /note="P -> L (in dbSNP:rs3744045)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1" FT /id="VAR_044125" FT VARIANT 249 FT /note="A -> T (in dbSNP:rs34814954)" FT /id="VAR_044126" FT VARIANT 528 FT /note="D -> Y (in dbSNP:rs11553545)" FT /id="VAR_044127" FT CONFLICT 67 FT /note="A -> S (in Ref. 2; BAF84824 and 4; AAH16034)" FT /evidence="ECO:0000305" FT CONFLICT 705 FT /note="N -> D (in Ref. 2; BAF84855)" FT /evidence="ECO:0000305" FT CONFLICT 852 FT /note="D -> G (in Ref. 2; BAF84855)" FT /evidence="ECO:0000305" SQ SEQUENCE 856 AA; 96686 MW; 69C40A21EBDBDDC0 CRC64; MASADKNGGS VSSVSSSRLQ SRKPPNLSIT IPPPEKETQA PGEQDSMLPE GFQNRRLKKS QPRTWAAHTT ACPPSFLPKR KNPAYLKSVS LQEPRSRWQE SSEKRPGFRR QASLSQSIRK GAAQWFGVSG DWEGQRQQWQ RRSLHHCSMR YGRLKASCQR DLELPSQEAP SFQGTESPKP CKMPKIVDPL ARGRAFRHPE EMDRPHAPHP PLTPGVLSLT SFTSVRSGYS HLPRRKRMSV AHMSLQAAAA LLKGRSVLDA TGQRCRVVKR SFAFPSFLEE DVVDGADTFD SSFFSKEEMS SMPDDVFESP PLSASYFRGI PHSASPVSPD GVQIPLKEYG RAPVPGPRRG KRIASKVKHF AFDRKKRHYG LGVVGNWLNR SYRRSISSTV QRQLESFDSH RPYFTYWLTF VHVIITLLVI CTYGIAPVGF AQHVTTQLVL RNKGVYESVK YIQQENFWVG PSSIDLIHLG AKFSPCIRKD GQIEQLVLRE RDLERDSGCC VQNDHSGCIQ TQRKDCSETL ATFVKWQDDT GPPMDKSDLG QKRTSGAVCH QDPRTCEEPA SSGAHIWPDD ITKWPICTEQ ARSNHTGFLH MDCEIKGRPC CIGTKGSCEI TTREYCEFMH GYFHEEATLC SQVHCLDKVC GLLPFLNPEV PDQFYRLWLS LFLHAGVVHC LVSVVFQMTI LRDLEKLAGW HRIAIIFILS GITGNLASAI FLPYRAEVGP AGSQFGLLAC LFVELFQSWP LLERPWKAFL NLSAIVLFLF ICGLLPWIDN IAHIFGFLSG LLLAFAFLPY ITFGTSDKYR KRALILVSLL AFAGLFAALV LWLYIYPINW PWIEHLTCFP FTSRFCEKYE LDQVLH //