MFSD6_HUMAN
ID MFSD6_HUMAN Reviewed; 791 AA.
AC Q6ZSS7; D3KSZ4; Q86TH2; Q9NXM3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Major facilitator superfamily domain-containing protein 6;
DE AltName: Full=Macrophage MHC class I receptor 2 homolog;
GN Name=MFSD6; Synonyms=MMR2;
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], VARIANT GLY-205, INTERACTION WITH HLA-B62, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=20123006; DOI=10.1016/j.gene.2010.01.007;
RA Shimizu T., Tashiro-Yamaji J., Hayashi M., Inoue Y., Ibata M., Kubota T.,
RA Tanigawa N., Yoshida R.;
RT "HLA-B62 as a possible ligand for the human homologue of mouse macrophage
RT MHC receptor 2 (MMR2) on monocytes.";
RL Gene 454:31-38(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-205.
RC TISSUE=Colon, and Corpus callosum;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-205.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 247-791.
RC TISSUE=PNS;
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10, AND IDENTIFICATION BY
RP 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).
CC -!- SUBUNIT: May interact with HLA-B62.
CC -!- INTERACTION:
CC Q6ZSS7; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-2858252, EBI-10827839;
CC Q6ZSS7; Q9BVK2: ALG8; NbExp=3; IntAct=EBI-2858252, EBI-3921603;
CC Q6ZSS7; Q96BI3: APH1A; NbExp=3; IntAct=EBI-2858252, EBI-2606935;
CC Q6ZSS7; O95236-2: APOL3; NbExp=3; IntAct=EBI-2858252, EBI-11976321;
CC Q6ZSS7; Q6P5T0: AQP7; NbExp=3; IntAct=EBI-2858252, EBI-10489564;
CC Q6ZSS7; Q8NEA5: C19orf18; NbExp=3; IntAct=EBI-2858252, EBI-18323646;
CC Q6ZSS7; P11912: CD79A; NbExp=3; IntAct=EBI-2858252, EBI-7797864;
CC Q6ZSS7; P00387: CYB5R3; NbExp=3; IntAct=EBI-2858252, EBI-1046040;
CC Q6ZSS7; Q15125: EBP; NbExp=3; IntAct=EBI-2858252, EBI-3915253;
CC Q6ZSS7; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2858252, EBI-781551;
CC Q6ZSS7; P48165: GJA8; NbExp=3; IntAct=EBI-2858252, EBI-17458373;
CC Q6ZSS7; P29033: GJB2; NbExp=3; IntAct=EBI-2858252, EBI-3905204;
CC Q6ZSS7; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-2858252, EBI-13345167;
CC Q6ZSS7; O15529: GPR42; NbExp=3; IntAct=EBI-2858252, EBI-18076404;
CC Q6ZSS7; Q8TED1: GPX8; NbExp=3; IntAct=EBI-2858252, EBI-11721746;
CC Q6ZSS7; Q16553: LY6E; NbExp=3; IntAct=EBI-2858252, EBI-18234679;
CC Q6ZSS7; Q5TF39: MFSD4B; NbExp=3; IntAct=EBI-2858252, EBI-11922631;
CC Q6ZSS7; Q16617: NKG7; NbExp=3; IntAct=EBI-2858252, EBI-3919611;
CC Q6ZSS7; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-2858252, EBI-16427978;
CC Q6ZSS7; A0A0S2Z4U3: SDC3; NbExp=3; IntAct=EBI-2858252, EBI-10204280;
CC Q6ZSS7; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-2858252, EBI-9679163;
CC Q6ZSS7; O95470: SGPL1; NbExp=3; IntAct=EBI-2858252, EBI-1046170;
CC Q6ZSS7; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-2858252, EBI-18037857;
CC Q6ZSS7; Q14973: SLC10A1; NbExp=3; IntAct=EBI-2858252, EBI-3923031;
CC Q6ZSS7; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2858252, EBI-18159983;
CC Q6ZSS7; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-2858252, EBI-17595455;
CC Q6ZSS7; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-2858252, EBI-12898013;
CC Q6ZSS7; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-2858252, EBI-12188413;
CC Q6ZSS7; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-2858252, EBI-17280858;
CC Q6ZSS7; Q86Y82: STX12; NbExp=3; IntAct=EBI-2858252, EBI-2691717;
CC Q6ZSS7; Q9H7V2: SYNDIG1; NbExp=3; IntAct=EBI-2858252, EBI-726331;
CC Q6ZSS7; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-2858252, EBI-11724423;
CC Q6ZSS7; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-2858252, EBI-10982110;
CC Q6ZSS7; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-2858252, EBI-10315004;
CC Q6ZSS7; P61165: TMEM258; NbExp=3; IntAct=EBI-2858252, EBI-12019210;
CC Q6ZSS7; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-2858252, EBI-12345267;
CC Q6ZSS7; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-2858252, EBI-12195249;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expression levels in peripheral
CC blood mononuclear cells are highly variable between individuals,
CC including no expression at all. {ECO:0000269|PubMed:20123006}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. MFSD6 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY24173.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA90987.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAX10868.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB472299; BAI82196.1; -; mRNA.
DR EMBL; AK000167; BAA90987.1; ALT_INIT; mRNA.
DR EMBL; AK127176; BAC86869.1; -; mRNA.
DR EMBL; AC093388; AAY24173.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471058; EAX10868.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471058; EAX10867.1; -; Genomic_DNA.
DR EMBL; BC050537; AAH50537.2; -; mRNA.
DR CCDS; CCDS2306.1; -.
DR RefSeq; NP_060164.3; NM_017694.3.
DR RefSeq; XP_005246711.1; XM_005246654.2.
DR RefSeq; XP_011509670.1; XM_011511368.1.
DR AlphaFoldDB; Q6ZSS7; -.
DR BioGRID; 120193; 40.
DR IntAct; Q6ZSS7; 44.
DR STRING; 9606.ENSP00000376141; -.
DR GlyConnect; 1484; 1 N-Linked glycan (1 site).
DR GlyGen; Q6ZSS7; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q6ZSS7; -.
DR PhosphoSitePlus; Q6ZSS7; -.
DR SwissPalm; Q6ZSS7; -.
DR BioMuta; MFSD6; -.
DR DMDM; 187610244; -.
DR EPD; Q6ZSS7; -.
DR jPOST; Q6ZSS7; -.
DR MassIVE; Q6ZSS7; -.
DR MaxQB; Q6ZSS7; -.
DR PaxDb; Q6ZSS7; -.
DR PeptideAtlas; Q6ZSS7; -.
DR PRIDE; Q6ZSS7; -.
DR ProteomicsDB; 68237; -.
DR Antibodypedia; 19836; 108 antibodies from 22 providers.
DR DNASU; 54842; -.
DR Ensembl; ENST00000281416.11; ENSP00000281416.7; ENSG00000151690.15.
DR Ensembl; ENST00000392328.6; ENSP00000376141.1; ENSG00000151690.15.
DR GeneID; 54842; -.
DR KEGG; hsa:54842; -.
DR MANE-Select; ENST00000392328.6; ENSP00000376141.1; NM_017694.4; NP_060164.3.
DR UCSC; uc002urz.2; human.
DR CTD; 54842; -.
DR DisGeNET; 54842; -.
DR GeneCards; MFSD6; -.
DR HGNC; HGNC:24711; MFSD6.
DR HPA; ENSG00000151690; Low tissue specificity.
DR MIM; 613476; gene.
DR neXtProt; NX_Q6ZSS7; -.
DR OpenTargets; ENSG00000151690; -.
DR PharmGKB; PA164722278; -.
DR VEuPathDB; HostDB:ENSG00000151690; -.
DR eggNOG; KOG3762; Eukaryota.
DR GeneTree; ENSGT00530000063599; -.
DR HOGENOM; CLU_013133_2_0_1; -.
DR InParanoid; Q6ZSS7; -.
DR OMA; IGLDYSE; -.
DR OrthoDB; 628784at2759; -.
DR PhylomeDB; Q6ZSS7; -.
DR TreeFam; TF314366; -.
DR PathwayCommons; Q6ZSS7; -.
DR SignaLink; Q6ZSS7; -.
DR BioGRID-ORCS; 54842; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; MFSD6; human.
DR GenomeRNAi; 54842; -.
DR Pharos; Q6ZSS7; Tbio.
DR PRO; PR:Q6ZSS7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6ZSS7; protein.
DR Bgee; ENSG00000151690; Expressed in substantia nigra pars reticulata and 179 other tissues.
DR ExpressionAtlas; Q6ZSS7; baseline and differential.
DR Genevisible; Q6ZSS7; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 3.
DR InterPro; IPR024989; MFS_assoc_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF12832; MFS_1_like; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..791
FT /note="Major facilitator superfamily domain-containing
FT protein 6"
FT /id="PRO_0000321940"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..599
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 22..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 205
FT /note="R -> G (in dbSNP:rs9646748)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:20123006, ECO:0000269|Ref.4"
FT /id="VAR_039388"
FT CONFLICT 728
FT /note="E -> G (in Ref. 2; BAA90987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 791 AA; 88088 MW; C623C7660D7BC73A CRC64;
MADDKVAILT DDEEEQKRKY VLADPFNGIS REPEPPSNET PSSTETSAIP EEEIDWIEKH
CVKINNDLLI SKVFYFFFYS AYGSLYPLLP VYYKQLGMSP SQSGLLVGIR YFIEFCSAPF
WGVVADRFKK GKIVLLFSLL CWVLFNLGIG FVKPATLRCV PKIRPTTHPT NASHQLTILP
TNSSFTSFLT ISPKMREKRN LLETRLNVSD TVTLPTAPNM NSEPTLQPQT GEITNRMMDL
TLNSSTATPV SPGSVTKETT TVIVTTTKSL PSDQVMLVYD QQEVEAIFLV ILVVVIIGEF
FSASSVTIVD TVTLQYLGKH RDRYGLQRMW GSLGWGLAML SVGIGIDYTH IEVLIDGKGC
KPPEYRNYQI VFIVFGVLMT MALIVATQFR FRYNHFKNDD SKGKEVEIPQ VERNNSTESS
EETPTTTSHS QAFNFWDLIK LLCSVQYGSV LFVAWFMGFG YGFVFTFLYW HLEDLNGTTT
LFGVCSVLSH VSELTAYFFS HKLIELIGHI RVLYIGLACN TARYIYISYL ENAWTVLPME
VLQGVTHAAI WAACISYLSA AVPPELRTSA QGILQGLHLG LGRGCGAMIG GVLVNYFGAA
ATFRGIGMAC LVILLLFALI QWLAVPDEEE DKTMLAERIP VPSSPVPIAT IDLVQQQTED
VMPRIEPRLP PKKTKHQEEQ EDVNKPAWGV SSSPWVTFVY ALYQIKEMMQ LTRDNRASEI
QPLQGTNENR ENSPAGRAQP VPCETHSDPS RNQPSPDAAA SQTQTSPAHP SVDPCTEESE
EQQAQLAAGG H
