TAP1_MOUSE
ID TAP1_MOUSE Reviewed; 724 AA.
AC P21958; Q62427;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Antigen peptide transporter 1;
DE Short=APT1;
DE EC=7.4.2.- {ECO:0000250|UniProtKB:Q03518};
DE AltName: Full=ATP-binding cassette sub-family B member 2;
DE AltName: Full=Histocompatibility antigen modifier 1;
DE AltName: Full=Peptide transporter TAP1;
GN Name=Tap1; Synonyms=Abcb2, Ham-1, Ham1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=WEHI-3; TISSUE=T-cell lymphoma;
RX PubMed=9164943;
RA Marusina K., Iyer M., Monaco J.J.;
RT "Allelic variation in the mouse Tap-1 and Tap-2 transporter genes.";
RL J. Immunol. 158:5251-5256(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 148-724.
RX PubMed=2270487; DOI=10.1126/science.2270487;
RA Monaco J.J., Cho S., Attaya M.;
RT "Transport protein genes in the murine MHC: possible implications for
RT antigen processing.";
RL Science 250:1723-1726(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 148-724.
RC STRAIN=BALB/cJ;
RA Sun X.Y., Zhou J., Frazer I.;
RL Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Lung, and Spleen;
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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: ABC transporter associated with antigen processing. In
CC complex with TAP2 mediates unidirectional translocation of peptide
CC antigens from cytosol to endoplasmic reticulum (ER) for loading onto
CC MHC class I (MHCI) molecules. Uses the chemical energy of ATP to export
CC peptides against the concentration gradient. During the transport cycle
CC alternates between 'inward-facing' state with peptide binding site
CC facing the cytosol to 'outward-facing' state with peptide binding site
CC facing the ER lumen. Peptide antigen binding to ATP-loaded TAP1-TAP2
CC induces a switch to hydrolysis-competent 'outward-facing' conformation
CC ready for peptide loading onto nascent MHCI molecules. Subsequently ATP
CC hydrolysis resets the transporter to the 'inward facing' state for a
CC new cycle. As a component of the peptide loading complex (PLC), acts as
CC a molecular scaffold essential for peptide-MHCI assembly and antigen
CC presentation. {ECO:0000250|UniProtKB:Q03518}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a peptide antigen(in) + ATP + H2O = a peptide antigen(out) +
CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:65972, Rhea:RHEA-COMP:16941,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:166823, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q03518};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65973;
CC Evidence={ECO:0000250|UniProtKB:Q03518};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q03518};
CC -!- SUBUNIT: Heterodimer of TAP1 and TAP2 (TAP1-TAP2). A component of the
CC peptide loading complex (PLC), interacts via TAPBP with MHCI
CC heterodimer; this interaction mediates peptide-MHCI assembly. Interacts
CC with PSMB5 and PSMB8. {ECO:0000250|UniProtKB:Q03518}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q03518}; Multi-pass membrane protein
CC {ECO:0000255}. Note=The transmembrane segments seem to form a pore in
CC the membrane.
CC -!- DOMAIN: The peptide-binding site is shared between the cytoplasmic
CC loops of TAP1 and TAP2. {ECO:0000250|UniProtKB:Q03518}.
CC -!- DOMAIN: The nucleotide-binding domain (NBD) mediates ATP hydrolysis
CC coupled to peptide translocation. Two ATP molecules are accommodated at
CC distinct nucleotide binding sites (NBS) at TAP1-TAP2 dimer interface.
CC Each NBS is formed by Walker A (GxxGxGKST) and Q-loop motifs from NBD
CC of one subunit, while the NBD from the second subunit completes the
CC active site by contributing the C loop motif (LSGGQ). Each ATP molecule
CC is coordinated via the beta- and gamma-phosphates to a Mg2+ ion, which
CC is necessary for ATP hydrolysis. {ECO:0000250|UniProtKB:P36370}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC MHC peptide exporter (TC 3.A.1.209) subfamily. {ECO:0000305}.
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DR EMBL; U60018; AAB41962.1; -; mRNA.
DR EMBL; U60019; AAB41963.1; -; mRNA.
DR EMBL; AK162731; BAE37041.1; -; mRNA.
DR EMBL; AF027865; AAB81534.1; -; Genomic_DNA.
DR EMBL; CH466660; EDL10260.1; -; Genomic_DNA.
DR EMBL; M55637; AAA39570.1; -; mRNA.
DR EMBL; X59615; CAA42178.1; -; mRNA.
DR CCDS; CCDS28643.1; -.
DR PIR; A37779; A37779.
DR PIR; JC2020; JC2020.
DR RefSeq; NP_038711.2; NM_013683.2.
DR AlphaFoldDB; P21958; -.
DR SMR; P21958; -.
DR BioGRID; 203966; 6.
DR STRING; 10090.ENSMUSP00000128401; -.
DR iPTMnet; P21958; -.
DR PhosphoSitePlus; P21958; -.
DR SwissPalm; P21958; -.
DR EPD; P21958; -.
DR MaxQB; P21958; -.
DR PaxDb; P21958; -.
DR PeptideAtlas; P21958; -.
DR PRIDE; P21958; -.
DR ProteomicsDB; 262932; -.
DR Antibodypedia; 4017; 339 antibodies from 40 providers.
DR DNASU; 21354; -.
DR Ensembl; ENSMUST00000170086; ENSMUSP00000128401; ENSMUSG00000037321.
DR GeneID; 21354; -.
DR KEGG; mmu:21354; -.
DR UCSC; uc008cbu.2; mouse.
DR CTD; 6890; -.
DR MGI; MGI:98483; Tap1.
DR VEuPathDB; HostDB:ENSMUSG00000037321; -.
DR eggNOG; KOG0058; Eukaryota.
DR GeneTree; ENSGT00940000159023; -.
DR HOGENOM; CLU_000604_84_3_1; -.
DR InParanoid; P21958; -.
DR OMA; LGIMLWG; -.
DR OrthoDB; 684058at2759; -.
DR PhylomeDB; P21958; -.
DR TreeFam; TF105197; -.
DR BRENDA; 7.4.2.14; 3474.
DR Reactome; R-MMU-1236974; ER-Phagosome pathway.
DR Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR BioGRID-ORCS; 21354; 16 hits in 78 CRISPR screens.
DR ChiTaRS; Tap1; mouse.
DR PRO; PR:P21958; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P21958; protein.
DR Bgee; ENSMUSG00000037321; Expressed in peripheral lymph node and 126 other tissues.
DR ExpressionAtlas; P21958; baseline and differential.
DR Genevisible; P21958; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0042824; C:MHC class I peptide loading complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0042825; C:TAP complex; ISO:MGI.
DR GO; GO:0015433; F:ABC-type peptide antigen transporter activity; EXP:Reactome.
DR GO; GO:0015440; F:ABC-type peptide transporter activity; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042288; F:MHC class I protein binding; IPI:MGI.
DR GO; GO:0023029; F:MHC class Ib protein binding; ISO:MGI.
DR GO; GO:0000166; F:nucleotide binding; ISO:MGI.
DR GO; GO:0042605; F:peptide antigen binding; ISO:MGI.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0046978; F:TAP1 binding; ISO:MGI.
DR GO; GO:0046979; F:TAP2 binding; ISO:MGI.
DR GO; GO:0046980; F:tapasin binding; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; ISO:MGI.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; IEA:InterPro.
DR GO; GO:0046967; P:cytosol to endoplasmic reticulum transport; ISO:MGI.
DR GO; GO:0006952; P:defense response; IMP:MGI.
DR GO; GO:0015833; P:peptide transport; ISO:MGI.
DR GO; GO:0042270; P:protection from natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR013305; ABC_Tap-like.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013306; Tap1/ABCB2.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR PANTHER; PTHR24221:SF249; PTHR24221:SF249; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR TIGRFAMs; TIGR00958; 3a01208; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; ATP-binding; Endoplasmic reticulum; Immunity; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Peptide transport;
KW Protein transport; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..724
FT /note="Antigen peptide transporter 1"
FT /id="PRO_0000093327"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 33..36
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..59
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 60..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 90..109
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 131..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 184..203
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 225..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 296..304
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 326..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 416..419
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 441..724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 163..446
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 479..718
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 351..396
FT /note="Part of the peptide-binding site"
FT /evidence="ECO:0000250|UniProtKB:Q03518"
FT REGION 429..463
FT /note="Part of the peptide-binding site"
FT /evidence="ECO:0000250|UniProtKB:Q03518"
FT BINDING 514..522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P36370,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q03518"
FT BINDING 617..623
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P36370"
FT BINDING 677
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P36370"
FT SITE 16
FT /note="Inter-subunit salt bridge with TAPBP"
FT /evidence="ECO:0000250|UniProtKB:Q03518"
FT CONFLICT 277
FT /note="G -> D (in Ref. 1; AAB41962, 5; AAA39570 and 6;
FT CAA42178)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="S -> Q (in Ref. 6; CAA42178)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="A -> T (in Ref. 1; AAB41962, 5; AAA39570 and 6;
FT CAA42178)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="F -> L (in Ref. 6; CAA42178)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="C -> R (in Ref. 1; AAB41962, 5; AAA39570 and 6;
FT CAA42178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 724 AA; 78864 MW; A08E40F9F5FBAE9D CRC64;
MAAHVWLAAA LLLLVDWLLL RPMLPGIFSL LVPEVPLLRV WVVGLSRWAI LGLGVRGVLG
VTAGAHGWLA ALQPLVAALS LALPGLALFR ELAAWGTLRE GDSAGLLYWN SRPDAFAISY
VAALPAAALW HKLGSLWAPS GNRDAGDMLC RMLGFLGPKK RRLYLVLVLL ILSCLGEMAI
PFFTGRITDW ILQDKTVPSF TRNIWLMSIL TIASTALEFA SDGIYNITMG HMHGRVHREV
FRAVLRQETG FFLKNPAGSI TSRVTEDTAN VCESISGTLS LLLWYLGRAL CLLVFMFWGS
PYLTLVTLIN LPLLFLLPKK LGKVHQSLAV KVQESLAKST QVALEALSAM PTVRSFANEE
GEAQKFRQKL EEMKTLNKKE ALAYVAEVWT TSVSGMLLKV GILYLGGQLV IRGAVSSGNL
VSFVLYQLQF TQAVQVLLSL YPSMQKAVGS SEKIFEYLDR TPCSPLSGSL APSNMKGLVE
FQDVSFAYPN QPKVQVLQGL TFTLHPGTVT ALVGPNGSGK STVAALLQNL YQPTGGQLLL
DGQCLVQYDH HYLHTQVAAV GQEPLLFGRS FRENIAYGLN RTPTMEEITA VAVESGAHDF
ISGFPQGYDT EVGETGNQLS GGQRQAVALA RALIRKPLLL ILDDATSALD AGNQLRVQRL
LYESPKRASR TVLLITQQLS LAEQAHHILF LREGSVGEQG THLQLMKRGG CYRAMVEALA
APAD
