ID   LFG2_HUMAN              Reviewed;         316 AA.
AC   Q9BWQ8; A8K1W6; B3KR08; Q9UJY9; Q9Y2F7;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 164.
DE   RecName: Full=Protein lifeguard 2;
DE   AltName: Full=Fas apoptotic inhibitory molecule 2;
DE   AltName: Full=Neural membrane protein 35;
DE   AltName: Full=Transmembrane BAX inhibitor motif-containing protein 2;
GN   Name=FAIM2; Synonyms=KIAA0950, LFG, LFG2, NMP35, TMBIM2;
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 1), FUNCTION, INTERACTION WITH
RP   FAS/TNFRSF6, AND TISSUE SPECIFICITY.
RC   TISSUE=Lung fibroblast;
RX   PubMed=10535980; DOI=10.1073/pnas.96.22.12667;
RA   Somia N.V., Schmitt M.J., Vetter D.E., Van Antwerp D., Heinemann S.F.,
RA   Verma I.M.;
RT   "LFG: an anti-apoptotic gene that provides protection from fas-mediated
RT   cell death.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:12667-12672(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:63-70(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Cerebellum, and Hippocampus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   [7]
RP   GENE FAMILY, AND INTERACTION WITH BAX.
RX   PubMed=16964429;
RA   Reimers K., Choi C.Y., Mau-Thek E., Vogt P.M.;
RT   "Sequence analysis shows that Lifeguard belongs to a new evolutionarily
RT   conserved cytoprotective family.";
RL   Int. J. Mol. Med. 18:729-734(2006).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17635665; DOI=10.1111/j.1471-4159.2007.04767.x;
RA   Fernandez M., Segura M.F., Sole C., Colino A., Comella J.X., Cena V.;
RT   "Lifeguard/neuronal membrane protein 35 regulates Fas ligand-mediated
RT   apoptosis in neurons via microdomain recruitment.";
RL   J. Neurochem. 103:190-203(2007).
RN   [9]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19784873; DOI=10.1007/s10495-009-0402-2;
RA   Hu L., Smith T.F., Goldberger G.;
RT   "LFG: a candidate apoptosis regulatory gene family.";
RL   Apoptosis 14:1255-1265(2009).
RN   [10]
RP   INDUCTION.
RX   PubMed=20336373; DOI=10.1007/s10495-010-0493-9;
RA   Bucan V., Adili M.Y., Choi C.Y., Eddy M.T., Vogt P.M., Reimers K.;
RT   "Transactivation of lifeguard (LFG) by Akt-/LEF-1 pathway in MCF-7 and MDA-
RT   MB 231 human breast cancer cells.";
RL   Apoptosis 15:814-821(2010).
RN   [11]
RP   TISSUE SPECIFICITY.
RX   PubMed=20336406; DOI=10.2478/s11658-010-0009-1;
RA   Bucan V., Reimers K., Choi C.Y., Eddy M.T., Vogt P.M.;
RT   "The anti-apoptotic protein lifeguard is expressed in breast cancer cells
RT   and tissues.";
RL   Cell. Mol. Biol. Lett. 15:296-310(2010).
CC   -!- FUNCTION: Antiapoptotic protein which protects cells uniquely from Fas-
CC       induced apoptosis. Regulates Fas-mediated apoptosis in neurons by
CC       interfering with caspase-8 activation. May play a role in cerebellar
CC       development by affecting cerebellar size, internal granular layer (IGL)
CC       thickness, and Purkinje cell (PC) development.
CC       {ECO:0000269|PubMed:10535980, ECO:0000269|PubMed:17635665}.
CC   -!- SUBUNIT: Interacts with FAS/TNFRSF6 and BAX.
CC       {ECO:0000269|PubMed:10535980, ECO:0000269|PubMed:16964429}.
CC   -!- INTERACTION:
CC       Q9BWQ8; O95208-2: EPN2; NbExp=3; IntAct=EBI-9056723, EBI-12135243;
CC       Q9BWQ8; Q6P531: GGT6; NbExp=3; IntAct=EBI-9056723, EBI-2868927;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Membrane raft {ECO:0000269|PubMed:17635665}.
CC       Postsynaptic cell membrane {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BWQ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BWQ8-2; Sequence=VSP_056989;
CC   -!- TISSUE SPECIFICITY: Highly expressed in breast carcinoma tissues.
CC       Enhanced expression correlates with the grade of the tumor (grade
CC       II/grade III) in primary breast tumors (at protein level). Widely
CC       expressed. Expressed at high levels in the brain especially in the
CC       hippocampus. {ECO:0000269|PubMed:10535980,
CC       ECO:0000269|PubMed:20336406}.
CC   -!- INDUCTION: Regulated by the AKT1/LEF1 pathway in breast cancer cell
CC       lines. {ECO:0000269|PubMed:20336373}.
CC   -!- SIMILARITY: Belongs to the BI1 family. LFG subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF06327.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA76794.1; Type=Erroneous initiation; Note=Extended 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; AF190461; AAF06327.1; ALT_FRAME; mRNA.
DR   EMBL; AB023167; BAA76794.1; ALT_INIT; mRNA.
DR   EMBL; AK090728; BAG52220.1; -; mRNA.
DR   EMBL; AK290031; BAF82720.1; -; mRNA.
DR   EMBL; AC131157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471111; EAW58103.1; -; Genomic_DNA.
DR   EMBL; CH471111; EAW58104.1; -; Genomic_DNA.
DR   EMBL; BC000051; AAH00051.1; -; mRNA.
DR   CCDS; CCDS8791.1; -. [Q9BWQ8-1]
DR   RefSeq; NP_036438.2; NM_012306.3. [Q9BWQ8-1]
DR   RefSeq; XP_016874529.1; XM_017019040.1.
DR   AlphaFoldDB; Q9BWQ8; -.
DR   SMR; Q9BWQ8; -.
DR   BioGRID; 116659; 12.
DR   IntAct; Q9BWQ8; 3.
DR   MINT; Q9BWQ8; -.
DR   STRING; 9606.ENSP00000321951; -.
DR   TCDB; 1.A.14.3.16; the calcium transporter a (cata) family (formerly the testis-enhanced gene transfer (tegt) family).
DR   GlyCosmos; Q9BWQ8; 1 site, No reported glycans.
DR   GlyGen; Q9BWQ8; 1 site.
DR   iPTMnet; Q9BWQ8; -.
DR   PhosphoSitePlus; Q9BWQ8; -.
DR   BioMuta; FAIM2; -.
DR   DMDM; 38503167; -.
DR   MassIVE; Q9BWQ8; -.
DR   PaxDb; 9606-ENSP00000321951; -.
DR   PeptideAtlas; Q9BWQ8; -.
DR   ProteomicsDB; 3573; -.
DR   ProteomicsDB; 79305; -. [Q9BWQ8-1]
DR   Antibodypedia; 14095; 288 antibodies from 32 providers.
DR   DNASU; 23017; -.
DR   Ensembl; ENST00000320634.8; ENSP00000321951.3; ENSG00000135472.9. [Q9BWQ8-1]
DR   Ensembl; ENST00000550890.5; ENSP00000450132.1; ENSG00000135472.9. [Q9BWQ8-2]
DR   GeneID; 23017; -.
DR   KEGG; hsa:23017; -.
DR   MANE-Select; ENST00000320634.8; ENSP00000321951.3; NM_012306.4; NP_036438.2.
DR   UCSC; uc001rvi.3; human. [Q9BWQ8-1]
DR   AGR; HGNC:17067; -.
DR   CTD; 23017; -.
DR   DisGeNET; 23017; -.
DR   GeneCards; FAIM2; -.
DR   HGNC; HGNC:17067; FAIM2.
DR   HPA; ENSG00000135472; Tissue enhanced (brain, parathyroid gland).
DR   MIM; 604306; gene.
DR   neXtProt; NX_Q9BWQ8; -.
DR   OpenTargets; ENSG00000135472; -.
DR   PharmGKB; PA134879081; -.
DR   VEuPathDB; HostDB:ENSG00000135472; -.
DR   eggNOG; KOG2322; Eukaryota.
DR   GeneTree; ENSGT01050000244890; -.
DR   HOGENOM; CLU_058671_3_2_1; -.
DR   InParanoid; Q9BWQ8; -.
DR   OMA; FTGWYVY; -.
DR   OrthoDB; 377780at2759; -.
DR   PhylomeDB; Q9BWQ8; -.
DR   TreeFam; TF319996; -.
DR   PathwayCommons; Q9BWQ8; -.
DR   SignaLink; Q9BWQ8; -.
DR   BioGRID-ORCS; 23017; 23 hits in 1144 CRISPR screens.
DR   ChiTaRS; FAIM2; human.
DR   GenomeRNAi; 23017; -.
DR   Pharos; Q9BWQ8; Tbio.
DR   PRO; PR:Q9BWQ8; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9BWQ8; Protein.
DR   Bgee; ENSG00000135472; Expressed in right frontal lobe and 149 other cell types or tissues.
DR   ExpressionAtlas; Q9BWQ8; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0021681; P:cerebellar granular layer development; ISS:UniProtKB.
DR   GO; GO:0021702; P:cerebellar Purkinje cell differentiation; ISS:UniProtKB.
DR   GO; GO:0021680; P:cerebellar Purkinje cell layer development; ISS:UniProtKB.
DR   GO; GO:0021549; P:cerebellum development; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB.
DR   GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IBA:GO_Central.
DR   GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:UniProtKB.
DR   GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR   CDD; cd10428; LFG_like; 1.
DR   InterPro; IPR006214; Bax_inhibitor_1-related.
DR   PANTHER; PTHR23291; BAX INHIBITOR-RELATED; 1.
DR   PANTHER; PTHR23291:SF18; PROTEIN LIFEGUARD 2; 1.
DR   Pfam; PF01027; Bax1-I; 1.
DR   Genevisible; Q9BWQ8; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cell membrane; Glycoprotein; Membrane;
KW   Postsynaptic cell membrane; Reference proteome; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..316
FT                   /note="Protein lifeguard 2"
FT                   /id="PRO_0000179087"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..46
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056989"
FT   CONFLICT        3
FT                   /note="Q -> R (in Ref. 1; AAF06327)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   316 AA;  35110 MW;  574128C7ADCC51C0 CRC64;
     MTQGKLSVAN KAPGTEGQQQ VHGEKKEAPA VPSAPPSYEE ATSGEGMKAG AFPPAPTAVP
     LHPSWAYVDP SSSSSYDNGF PTGDHELFTT FSWDDQKVRR VFVRKVYTIL LIQLLVTLAV
     VALFTFCDPV KDYVQANPGW YWASYAVFFA TYLTLACCSG PRRHFPWNLI LLTVFTLSMA
     YLTGMLSSYY NTTSVLLCLG ITALVCLSVT VFSFQTKFDF TSCQGVLFVL LMTLFFSGLI
     LAILLPFQYV PWLHAVYAAL GAGVFTLFLA LDTQLLMGNR RHSLSPEEYI FGALNIYLDI
     IYIFTFFLQL FGTNRE
//