ID T131L_HUMAN Reviewed; 1609 AA. AC A2VDJ0; B3KRV3; D3DP10; Q7LGA7; Q86Y92; Q8WU56; Q9H065; Q9Y2D7; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 2. DT 13-FEB-2019, entry version 98. DE RecName: Full=Transmembrane protein 131-like {ECO:0000312|HGNC:HGNC:29146}; DE Flags: Precursor; GN Name=TMEM131L {ECO:0000312|HGNC:HGNC:29146}; GN Synonyms=KIAA0922 {ECO:0000312|HGNC:HGNC:29146}; 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 [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Uterus; RX PubMed=11230166; DOI=10.1101/gr.GR1547R; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., RA Wambutt R., Korn B., Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and RT analysis of 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1053 (ISOFORM 4). RC TISSUE=Tongue; 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 MRNA] OF 60-1609 (ISOFORM 1), RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 140-1609 (ISOFORM 3), AND RP VARIANT THR-645. RC TISSUE=Lymph, and Muscle; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 820-1609. RC TISSUE=Brain; RX PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1122, AND IDENTIFICATION RP 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORMS 1 AND 5), TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=23690469; DOI=10.4049/jimmunol.1300400; RA Maharzi N., Parietti V., Nelson E., Denti S., Robledo-Sarmiento M., RA Setterblad N., Parcelier A., Pla M., Sigaux F., Gluckman J.C., RA Canque B.; RT "Identification of TMEM131L as a novel regulator of thymocyte RT proliferation in humans."; RL J. Immunol. 190:6187-6197(2013). CC -!- FUNCTION: Isoform 1: Membrane-associated form that antagonizes CC canonical Wnt signaling by triggering lysosome-dependent CC degradation of Wnt-activated LRP6. Regulates thymocyte CC proliferation. {ECO:0000269|PubMed:23690469}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23690469}; CC Single-pass type I membrane protein {ECO:0000305}. Cytoplasm CC {ECO:0000269|PubMed:23690469}. Note=During intrathymic CC development, resides in punctate cytoplasmic structures in DN1 and CC DN2 cells. In DN3 cells, found in large crescent-shaped membrane CC structures, which preferentially localize in cell-to-cell contact CC zones. {ECO:0000269|PubMed:23690469}. CC -!- SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum CC {ECO:0000269|PubMed:23690469}. Note=Transmembrane localization is CC essential for Wnt signaling inhibition. CC {ECO:0000269|PubMed:23690469}. CC -!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm CC {ECO:0000269|PubMed:23690469}. Note=Scattered throughout the CC cytoplasm in small-sized punctate structures. CC {ECO:0000269|PubMed:23690469}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=L {ECO:0000303|PubMed:23690469}; CC IsoId=A2VDJ0-1; Sequence=Displayed; CC Name=2; CC IsoId=A2VDJ0-2; Sequence=VSP_032826, VSP_032828; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=A2VDJ0-3; Sequence=VSP_032827, VSP_032829; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=A2VDJ0-5; Sequence=VSP_032827; CC Note=No experimental confirmation available.; CC Name=5; Synonyms=S {ECO:0000303|PubMed:23690469}; CC IsoId=A2VDJ0-6; Sequence=VSP_057633, VSP_032827; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Expressed in thymocytes. CC {ECO:0000269|PubMed:23690469}. CC -!- DEVELOPMENTAL STAGE: During intrathymic development, transcript CC levels strongly increase from pro-DN1 thymocytes to DN3a cells, in CC which they peak, and drop immediately after beta-selection in CC their DN3b successors. The subcellular location of the protein CC also varies, from punctate cytoplasmic structures in DN1 and DN2 CC cells to large crescent-shaped membrane structures in DN3 cells, CC which preferentially localize in cell-to-cell contact zones. CC {ECO:0000269|PubMed:23690469}. CC -!- SIMILARITY: Belongs to the TMEM131 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; AL136932; CAB66866.1; -; mRNA. DR EMBL; AC106865; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC116648; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471056; EAX04957.1; -; Genomic_DNA. DR EMBL; CH471056; EAX04958.1; -; Genomic_DNA. DR EMBL; AK092270; BAG52515.1; -; mRNA. DR EMBL; BC044932; AAH44932.1; -; mRNA. DR EMBL; BC131505; AAI31506.1; -; mRNA. DR EMBL; AB023139; BAA76766.1; -; mRNA. DR CCDS; CCDS3783.2; -. [A2VDJ0-1] DR CCDS; CCDS47148.1; -. [A2VDJ0-5] DR RefSeq; NP_001124479.1; NM_001131007.1. [A2VDJ0-5] DR RefSeq; NP_056011.3; NM_015196.3. [A2VDJ0-1] DR UniGene; Hs.732450; -. DR ProteinModelPortal; A2VDJ0; -. DR BioGrid; 116844; 30. DR IntAct; A2VDJ0; 1. DR STRING; 9606.ENSP00000386787; -. DR iPTMnet; A2VDJ0; -. DR PhosphoSitePlus; A2VDJ0; -. DR SwissPalm; A2VDJ0; -. DR BioMuta; TMEM131L; -. DR EPD; A2VDJ0; -. DR jPOST; A2VDJ0; -. DR MaxQB; A2VDJ0; -. DR PaxDb; A2VDJ0; -. DR PRIDE; A2VDJ0; -. DR ProteomicsDB; 541; -. DR ProteomicsDB; 542; -. [A2VDJ0-2] DR ProteomicsDB; 543; -. [A2VDJ0-3] DR ProteomicsDB; 544; -. [A2VDJ0-5] DR Ensembl; ENST00000409663; ENSP00000386574; ENSG00000121210. [A2VDJ0-1] DR Ensembl; ENST00000409959; ENSP00000386787; ENSG00000121210. [A2VDJ0-5] DR GeneID; 23240; -. DR KEGG; hsa:23240; -. DR UCSC; uc003inm.5; human. [A2VDJ0-1] DR CTD; 23240; -. DR EuPathDB; HostDB:ENSG00000121210.15; -. DR GeneCards; TMEM131L; -. DR H-InvDB; HIX0004579; -. DR HGNC; HGNC:29146; TMEM131L. DR HPA; HPA043472; -. DR HPA; HPA048443; -. DR MIM; 616243; gene. DR neXtProt; NX_A2VDJ0; -. DR OpenTargets; ENSG00000121210; -. DR PharmGKB; PA128394615; -. DR eggNOG; KOG3620; Eukaryota. DR eggNOG; ENOG410Z7NH; LUCA. DR GeneTree; ENSGT00530000063614; -. DR HOGENOM; HOG000154480; -. DR HOVERGEN; HBG108533; -. DR InParanoid; A2VDJ0; -. DR OMA; SESFVFF; -. DR OrthoDB; 826997at2759; -. DR PhylomeDB; A2VDJ0; -. DR TreeFam; TF321435; -. DR ChiTaRS; KIAA0922; human. DR GeneWiki; KIAA0922; -. DR GenomeRNAi; 23240; -. DR PRO; PR:A2VDJ0; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; ENSG00000121210; Expressed in 188 organ(s), highest expression level in secondary oocyte. DR ExpressionAtlas; A2VDJ0; baseline and differential. DR Genevisible; A2VDJ0; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0033088; P:negative regulation of immature T cell proliferation in thymus; IMP:UniProtKB. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR InterPro; IPR039877; TMEM131-like. DR InterPro; IPR022113; TMEM131-like_dom. DR PANTHER; PTHR22050; PTHR22050; 1. DR Pfam; PF12371; TMEM131_like; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; KW Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein; KW Polymorphism; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Wnt signaling pathway. FT SIGNAL 1 40 {ECO:0000255}. FT CHAIN 41 1609 Transmembrane protein 131-like. FT /FTId=PRO_0000328865. FT TOPO_DOM 41 869 Extracellular. {ECO:0000255}. FT TRANSMEM 870 890 Helical. {ECO:0000255}. FT TOPO_DOM 891 1609 Cytoplasmic. {ECO:0000255}. FT REGION 696 916 Required for Wnt-signaling inhibition and FT LRP6 degradation. FT {ECO:0000269|PubMed:23690469}. FT COMPBIAS 910 913 Poly-Ser. FT COMPBIAS 1302 1331 Ser-rich. FT MOD_RES 1122 1122 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT CARBOHYD 343 343 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 439 439 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 522 522 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 593 593 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 709 709 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 846 846 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT VAR_SEQ 1 370 Missing (in isoform 2). FT {ECO:0000303|PubMed:11230166}. FT /FTId=VSP_032826. FT VAR_SEQ 1 148 Missing (in isoform 5). FT /FTId=VSP_057633. FT VAR_SEQ 353 353 K -> KA (in isoform 3, isoform 4 and FT isoform 5). {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.3}. FT /FTId=VSP_032827. FT VAR_SEQ 371 380 TPTLKACLFS -> MLLVLECVLF (in isoform 2). FT {ECO:0000303|PubMed:11230166}. FT /FTId=VSP_032828. FT VAR_SEQ 557 640 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_032829. FT VARIANT 604 604 I -> V (in dbSNP:rs7669418). FT /FTId=VAR_042551. FT VARIANT 645 645 M -> T (in dbSNP:rs17370297). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_042552. FT VARIANT 1110 1110 S -> Y (in dbSNP:rs755078). FT /FTId=VAR_042553. FT VARIANT 1254 1254 N -> S (in dbSNP:rs35018723). FT /FTId=VAR_042554. FT VARIANT 1392 1392 A -> P (in dbSNP:rs35543386). FT /FTId=VAR_042555. FT CONFLICT 171 171 F -> S (in Ref. 4; BAG52515). FT {ECO:0000305}. SQ SEQUENCE 1609 AA; 179339 MW; 7F9D2EC0BC959210 CRC64; MAGLRRPQPG CYCRTAAAVN LLLGVFQVLL PCCRPGGAQG QAIEPLPNVV ELWQAEEGEL LLPTQGDSEE GLEEPSQEQS FSDKLFSGKG LHFQPSVLDF GIQFLGHPVA KILHAYNPSR DSEVVVNSVF AAAGHFHVPP VPCRVIPAMG KTSFRIIFLP TEEGSIESSL FINTSSYGVL SYHVSGIGTR RISTEGSAKQ LPNAYFLLPK VQSIQLSQMQ AETTNTSLLQ VQLECSLHNK VCQQLKGCYL ESDDVLRLQM SIMVTMENFS KEFEENTQHL LDHLSIVYVA TDESETSDDS AVNMYILHSG NSLIWIQDIR HFSQRDALSL QFEPVLLPTS TTNFTKIASF TCKATSCDSG IIEDVKKTTH TPTLKACLFS SVAQGYFRMD SSATQFHIET HENTSGLWSI WYRNHFDRSV VLNDVFLSKE TKHMLKILNF TGPLFLPPGC WNIFSLKLAV KDIAINLFTN VFLTTNIGAI FAIPLQIYSA PTKEGSLGFE VIAHCGMHYF MGKSKAGNPN WNGSLSLDQS TWNVDSELAN KLYERWKKYK NGDVCKRNVL GTTRFAHLKK SKESESFVFF LPRLIAEPGL MLNFSATALR SRMIKYFVVQ NPSSWPVSLQ LLPLSLYPKP EALVHLLHRW FGTDMQMINF TTGEFQLTEA CPYLGTHSEE SRFGILHLHL QPLEMKRVGV VFTPADYGKV TSLILIRNNL TVIDMIGVEG FGARELLKVG GRLPGAGGSL RFKVPESTLM DCRRQLKDSK QILSITKNFK VENIGPLPIT VSSLKINGYN CQGYGFEVLD CHQFSLDPNT SRDISIVFTP DFTSSWVIRD LSLVTAADLE FRFTLNVTLP HHLLPLCADV VPGPSWEESF WRLTVFFVSL SLLGVILIAF QQAQYILMEF MKTRQRQNAS SSSQQNNGPM DVISPHSYKS NCKNFLDTYG PSDKGRGKNC LPVNTPQSRI QNAAKRSPAT YGHSQKKHKC SVYYSKHKTS TAAASSTSTT TEEKQTSPLG SSLPAAKEDI CTDAMRENWI SLRYASGINV NLQKNLTLPK NLLNKEENTL KNTIVFSNPS SECSMKEGIQ TCMFPKETDI KTSENTAEFK ERELCPLKTS KKLPENHLPR NSPQYHQPDL PEISRKNNGN NQQVPVKNEV DHCENLKKVD TKPSSEKKIH KTSREDMFSE KQDIPFVEQE DPYRKKKLQE KREGNLQNLN WSKSRTCRKN KKRGVAPVSR PPEQSDLKLV CSDFERSELS SDINVRSWCI QESTREVCKA DAEIASSLPA AQREAEGYYQ KPEKKCVDKF CSDSSSDCGS SSGSVRASRG SWGSWSSTSS SDGDKKPMVD AQHFLPAGDS VSQNDFPSEA PISLNLSHNI CNPMTVNSLP QYAEPSCPSL PAGPTGVEED KGLYSPGDLW PTPPVCVTSS LNCTLENGVP CVIQESAPVH NSFIDWSATC EGQFSSAYCP LELNDYNAFP EENMNYANGF PCPADVQTDF IDHNSQSTWN TPPNMPAAWG HASFISSPPY LTSTRSLSPM SGLFGSIWAP QSDVYENCCP INPTTEHSTH MENQAVVCKE YYPGFNPFRA YMNLDIWTTT ANRNANFPLS RDSSYCGNV //