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   27-MAR-2024, entry version 206.
DE   RecName: Full=Antigen peptide transporter 1;
DE            Short=APT1;
DE            EC=7.4.2.14 {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         EC=7.4.2.14; 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; 7.
DR   STRING; 10090.ENSMUSP00000128401; -.
DR   iPTMnet; P21958; -.
DR   PhosphoSitePlus; P21958; -.
DR   SwissPalm; P21958; -.
DR   EPD; P21958; -.
DR   MaxQB; P21958; -.
DR   PaxDb; 10090-ENSMUSP00000128401; -.
DR   PeptideAtlas; P21958; -.
DR   ProteomicsDB; 262932; -.
DR   Pumba; P21958; -.
DR   Antibodypedia; 4017; 384 antibodies from 40 providers.
DR   DNASU; 21354; -.
DR   Ensembl; ENSMUST00000170086.8; ENSMUSP00000128401.2; ENSMUSG00000037321.18.
DR   GeneID; 21354; -.
DR   KEGG; mmu:21354; -.
DR   UCSC; uc008cbu.2; mouse.
DR   AGR; MGI:98483; -.
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; FNQFFVG; -.
DR   OrthoDB; 5487044at2759; -.
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; 18 hits in 83 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 129 other cell types or tissues.
DR   ExpressionAtlas; P21958; baseline and differential.
DR   GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0016020; C:membrane; 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: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: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: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; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR039421; Type_1_exporter.
DR   NCBIfam; TIGR00958; 3a01208; 1.
DR   PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43394:SF15; TRANSPORTER 1, ATP BINDING CASSETTE SUBFAMILY B MEMBER; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   PIRSF; PIRSF002773; ABC_prm/ATPase_B; 1.
DR   PRINTS; PR01896; TAP1PROTEIN.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   Genevisible; P21958; MM.
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
//