ID   DOA_HUMAN               Reviewed;         250 AA.
AC   P06340; Q58HU0; Q58HU1; Q5STC7; Q9TQC6; Q9TQC7; Q9TQC8; Q9TQC9; Q9TQD0;
AC   Q9TQD1; Q9TQD2; Q9TQD3;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   04-NOV-2026, entry version 198.
DE   RecName: Full=HLA class II histocompatibility antigen, DO alpha chain;
DE   AltName: Full=MHC DN-alpha;
DE   AltName: Full=MHC DZ alpha;
DE   AltName: Full=MHC class II antigen DOA;
DE   Flags: Precursor;
GN   Name=HLA-DOA; Synonyms=HLA-DNA, HLA-DZA;
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 [GENOMIC DNA] (ALLELE DOA*01:01).
RX   PubMed=3000765; DOI=10.1002/j.1460-2075.1985.tb03919.x;
RA   Trowsdale J., Kelly A.;
RT   "The human HLA class II alpha chain gene DZ alpha is distinct from genes in
RT   the DP, DQ and DR subregions.";
RL   EMBO J. 4:2231-2237(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DOA*01:01).
RX   PubMed=2499532; DOI=10.1007/bf00375872;
RA   Jonsson A.-K., Rask L.;
RT   "Human class II DNA and DOB genes display low sequence variability.";
RL   Immunogenetics 29:411-413(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DOA*01:01).
RX   PubMed=2370084; DOI=10.1007/bf02115015;
RA   Young J.A., Trowsdale J.;
RT   "The HLA-DNA (DZA) gene is correctly expressed as a 1.1 kb mature mRNA
RT   transcript.";
RL   Immunogenetics 31:386-388(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DOA*01:01; DOA*01:02 AND DOA*01:03).
RX   PubMed=16101837; DOI=10.1111/j.1399-0039.2005.00446.x;
RA   Moon S.-M., Gu H., Ryu H.-J., Kim J.-J., Kim H.-T., Han B.G., Kimm K.,
RA   Lee J.-K., Oh B.;
RT   "Identification of four novel HLA-DOA alleles, DOA*010106, DOA*0102,
RT   DOA*0103, and DOA*0104N, by sequence-based typing.";
RL   Tissue Antigens 66:242-245(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DOA*01:01).
RC   TISSUE=Lung;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DOA*01:01).
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DOA*01:01).
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DOA*01:01).
RC   TISSUE=Lymph;
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   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-250 (ALLELE DOA*01:01).
RX   PubMed=10323340; DOI=10.1034/j.1399-0039.1999.530406.x;
RA   Naruse T.K., Kawata H., Anzai T., Takashige N., Kagiya M., Nose Y.,
RA   Nabeya N., Isshiki G., Tatsumi N., Inoko H.;
RT   "Limited polymorphism in the HLA-DOA gene.";
RL   Tissue Antigens 53:359-365(1999).
RN   [10]
RP   REVIEW.
RX   PubMed=10837054; DOI=10.1146/annurev.immunol.18.1.113;
RA   Alfonso C., Karlsson L.;
RT   "Nonclassical MHC class II molecules.";
RL   Annu. Rev. Immunol. 18:113-142(2000).
CC   -!- FUNCTION: Important modulator in the HLA class II restricted antigen
CC       presentation pathway by interaction with the HLA-DM molecule in B-
CC       cells. Modifies peptide exchange activity of HLA-DM.
CC   -!- SUBUNIT: Heterodimer of an alpha chain (DOA) and a beta chain (DOB).
CC       Forms a heterotetrameric complex with an HLA-DM molecule during
CC       intracellular transport in endosomal/lysosomal compartments in B-cells.
CC   -!- INTERACTION:
CC       P06340; Q04864: REL; NbExp=3; IntAct=EBI-10194851, EBI-307352;
CC   -!- SUBCELLULAR LOCATION: Endosome membrane; Single-pass type I membrane
CC       protein. Lysosome membrane; Single-pass type I membrane protein.
CC       Note=Complexes with HLA-DM molecule during intracellular transport and
CC       in endosomal/lysosomal compartments. Heterotetramerization is necessary
CC       to exit the ER.
CC   -!- POLYMORPHISM: The following alleles of DOA are known: DOA*01:01,
CC       DOA*01:02 and DOA*01:03. The sequence shown is that of DOA*01:01.
CC   -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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DR   EMBL; X02882; CAA26635.1; -; Genomic_DNA.
DR   EMBL; M26039; AAA59716.1; -; mRNA.
DR   EMBL; M31525; AAA60075.1; -; mRNA.
DR   EMBL; AY947479; AAX49509.1; -; mRNA.
DR   EMBL; AY947480; AAX49510.1; -; mRNA.
DR   EMBL; AY947481; AAX49511.1; -; mRNA.
DR   EMBL; AK290714; BAF83403.1; -; mRNA.
DR   EMBL; AK313551; BAG36327.1; -; mRNA.
DR   EMBL; Z81310; CAB03594.1; -; Genomic_DNA.
DR   EMBL; AL662845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL645931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL805913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX005422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR759829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR936909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR759795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03668.1; -; Genomic_DNA.
DR   EMBL; BC013183; AAH13183.1; -; mRNA.
DR   EMBL; AB005991; BAA81787.1; -; Genomic_DNA.
DR   EMBL; AB005992; BAA81788.1; -; Genomic_DNA.
DR   EMBL; AB005993; BAA81789.1; -; Genomic_DNA.
DR   EMBL; AB005994; BAA81790.1; -; Genomic_DNA.
DR   EMBL; AB005995; BAA81791.1; -; Genomic_DNA.
DR   EMBL; AB005996; BAA81792.1; -; Genomic_DNA.
DR   EMBL; AB005997; BAA81793.1; -; Genomic_DNA.
DR   EMBL; AB005998; BAA81794.1; -; Genomic_DNA.
DR   CCDS; CCDS4763.1; -.
DR   PIR; A02216; HLHUDZ.
DR   RefSeq; NP_002110.1; NM_002119.4.
DR   PDB; 4I0P; X-ray; 3.20 A; C/G=27-207.
DR   SMR; P06340; -.
DR   BioGRID; 109356; 4.
DR   DIP; DIP-60116N; -.
DR   IntAct; P06340; 6.
DR   STRING; 9606.ENSP00000229829; -.
DR   NDEx; IQUERY-CP-HLA-DOA; 3 NDEx IQuery Curated Pathways.
DR   GlyCosmos; P06340; 2 sites, No reported glycans.
DR   GlyGen; P06340; 2 sites.
DR   iPTMnet; P06340; -.
DR   PhosphoSitePlus; P06340; -.
DR   BioMuta; HLA-DOA; -.
DR   DMDM; 122210; -.
DR   PaxDb; 9606-ENSP00000229829; -.
DR   PeptideAtlas; P06340; -.
DR   ProteomicsDB; 51896; -.
DR   MassIVE; P06340; -.
DR   DNASU; 3111; -.
DR   Ensembl; ENST00000229829.7; ENSP00000229829.3; ENSG00000204252.15.
DR   Ensembl; ENST00000383226.4; ENSP00000372713.4; ENSG00000206292.13.
DR   Ensembl; ENST00000426070.2; ENSP00000401504.2; ENSG00000231558.11.
DR   Ensembl; ENST00000426685.2; ENSP00000397945.2; ENSG00000232957.11.
DR   Ensembl; ENST00000434335.2; ENSP00000416448.2; ENSG00000232962.11.
DR   Ensembl; ENST00000438987.2; ENSP00000395737.2; ENSG00000230141.11.
DR   Ensembl; ENST00000452598.2; ENSP00000398819.2; ENSG00000235744.11.
DR   GeneID; 3111; -.
DR   KEGG; hsa:3111; -.
DR   MANE-Select; ENST00000229829.7; ENSP00000229829.3; NM_002119.4; NP_002110.1.
DR   CTD; 3111; -.
DR   DisGeNET; 3111; -.
DR   VEuPathDB; HostDB:ENSG00000204252; -.
DR   GeneCards; HLA-DOA; -.
DR   HGNC; HGNC:4936; HLA-DOA.
DR   AGR; HGNC:4936; -.
DR   HPA; ENSG00000204252; Tissue enhanced (lymphoid).
DR   MIM; 142930; gene.
DR   OpenTargets; ENSG00000204252; -.
DR   ClinPGx; PA35060; -.
DR   eggNOG; ENOG502RXYJ; Eukaryota.
DR   GeneTree; ENSGT00940000162112; -.
DR   HOGENOM; CLU_069380_0_0_1; -.
DR   InParanoid; P06340; -.
DR   OMA; AENQRFC; -.
DR   OrthoDB; 8925804at2759; -.
DR   PhylomeDB; P06340; -.
DR   Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR   Reactome; R-HSA-9979719; Processing of antigen in germinal center B cells.
DR   SignaLink; P06340; -.
DR   SIGNOR; P06340; -.
DR   EvolutionaryTrace; P06340; -.
DR   Agora; ENSG00000204252; Agora Nominated Target for Alzheimer's Disease.
DR   GeneWiki; HLA-DOA; -.
DR   GenomeRNAi; 3111; -.
DR   PRO; PR:P06340; -.
DR   Bgee; ENSG00000204252; Expressed in lymph node and 103 other cell types or tissues.
DR   ExpressionAtlas; P06340; baseline and differential.
DR   CDD; cd21004; IgC1_MHC_II_alpha_HLA_DO; 1.
DR   FunFam; 2.60.40.10:FF:000280; HLA class II histocompatibility antigen, DR alpha chain; 1.
DR   FunFam; 3.10.320.10:FF:000002; HLA class II histocompatibility antigen, DR alpha chain; 1.
DR   Gene3D; 3.10.320.10; Class II Histocompatibility Antigen, M Beta Chain, Chain B, domain 1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR003597; Ig_C1-set.
DR   InterPro; IPR050160; MHC/Immunoglobulin.
DR   InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR   InterPro; IPR014745; MHC_II_a/b_N.
DR   InterPro; IPR001003; MHC_II_a_N.
DR   PANTHER; PTHR19944:SF44; HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DO ALPHA CHAIN; 1.
DR   PANTHER; PTHR19944; MHC CLASS II-RELATED; 1.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF00993; MHC_II_alpha; 1.
DR   SMART; SM00407; IGc1; 1.
DR   SMART; SM00920; MHC_II_alpha; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF54452; MHC antigen-recognition domain; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00290; IG_MHC; 1.
DR   GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR   GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR   GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR   GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
DR   GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB.
DR   GO; GO:0042605; F:peptide antigen binding; IBA:GO_Central.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IBA:GO_Central.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IDA:UniProtKB.
DR   GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central.
DR   GO; GO:0050778; P:positive regulation of immune response; IBA:GO_Central.
DR   GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR   Proteomes; UP000005640; Chromosome 6.
DR   PathwayCommons; P06340; -.
DR   Pharos; P06340; Tbio.
DR   Antibodypedia; 28851; 170 antibodies from 28 providers.
DR   RNAct; P06340; protein.
DR   BioGRID-ORCS; 3111; 17 hits in 1140 CRISPR screens.
DR   AlphaFoldDB; P06340; -.
DR   FunCoup; P06340; 461.
DR   PAN-GO; P06340; 9 GO annotations based on evolutionary models.
PE   1: Evidence at protein level;
KW   3D-structure; Adaptive immunity; Disulfide bond; Endosome; Glycoprotein;
KW   Immunity; Lysosome; Membrane; MHC II; Proteomics identification;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..250
FT                   /note="HLA class II histocompatibility antigen, DO alpha
FT                   chain"
FT                   /id="PRO_0000018962"
FT   TOPO_DOM        26..217
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241..250
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          113..205
FT                   /note="Ig-like C1-type"
FT   REGION          26..110
FT                   /note="Alpha-1"
FT   REGION          111..204
FT                   /note="Alpha-2"
FT   REGION          205..217
FT                   /note="Connecting peptide"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        133..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VARIANT         99
FT                   /note="L -> V (in allele DOA*01:03; dbSNP:rs41542323)"
FT                   /id="VAR_058126"
FT   VARIANT         105
FT                   /note="R -> C (in allele DOA*01:02; dbSNP:rs11575906)"
FT                   /id="VAR_058127"
FT   STRAND          29..40
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   STRAND          45..52
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   STRAND          55..61
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   TURN            62..65
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   HELIX           72..74
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   HELIX           87..94
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   HELIX           96..102
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   STRAND          114..121
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   STRAND          129..141
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   STRAND          144..149
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   STRAND          171..179
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   STRAND          187..192
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   STRAND          196..198
FT                   /evidence="ECO:0007829|PDB:4I0P"
FT   STRAND          200..204
FT                   /evidence="ECO:0007829|PDB:4I0P"
SQ   SEQUENCE   250 AA;  27599 MW;  FA9482197A02AC85 CRC64;
     MALRAGLVLG FHTLMTLLSP QEAGATKADH MGSYGPAFYQ SYGASGQFTH EFDEEQLFSV
     DLKKSEAVWR LPEFGDFARF DPQGGLAGIA AIKAHLDILV ERSNRSRAIN VPPRVTVLPK
     SRVELGQPNI LICIVDNIFP PVINITWLRN GQTVTEGVAQ TSFYSQPDHL FRKFHYLPFV
     PSAEDVYDCQ VEHWGLDAPL LRHWELQVPI PPPDAMETLV CALGLAIGLV GFLVGTVLII
     MGTYVSSVPR
//