PMGT2_HUMAN
ID PMGT2_HUMAN Reviewed; 580 AA.
AC Q8NAT1; B3KWC3; Q96SY3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 {ECO:0000303|PubMed:23929950};
DE Short=POMGnT2 {ECO:0000303|PubMed:23929950};
DE EC=2.4.1.312 {ECO:0000269|PubMed:23929950, ECO:0000269|PubMed:27066570};
DE AltName: Full=Extracellular O-linked N-acetylglucosamine transferase-like;
DE AltName: Full=Glycosyltransferase-like domain-containing protein 2;
GN Name=POMGNT2; Synonyms=AGO61, C3orf39, EOGTL, GTDC2;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PATHWAY.
RX PubMed=23929950; DOI=10.1126/science.1239951;
RA Yoshida-Moriguchi T., Willer T., Anderson M.E., Venzke D., Whyte T.,
RA Muntoni F., Lee H., Nelson S.F., Yu L., Campbell K.P.;
RT "SGK196 is a glycosylation-specific O-mannose kinase required for
RT dystroglycan function.";
RL Science 341:896-899(2013).
RN [6]
RP TISSUE SPECIFICITY, INVOLVEMENT IN MDDGA8, AND VARIANTS MDDGA8 HIS-158;
RP 197-TRP--THR-580 DEL AND 445-ARG--THR-580 DEL.
RX PubMed=22958903; DOI=10.1016/j.ajhg.2012.07.009;
RA Manzini M.C., Tambunan D.E., Hill R.S., Yu T.W., Maynard T.M.,
RA Heinzen E.L., Shianna K.V., Stevens C.R., Partlow J.N., Barry B.J.,
RA Rodriguez J., Gupta V.A., Al-Qudah A.K., Eyaid W.M., Friedman J.M.,
RA Salih M.A., Clark R., Moroni I., Mora M., Beggs A.H., Gabriel S.B.,
RA Walsh C.A.;
RT "Exome sequencing and functional validation in zebrafish identify GTDC2
RT mutations as a cause of Walker-Warburg syndrome.";
RL Am. J. Hum. Genet. 91:541-547(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INVOLVEMENT IN MDDGC8,
RP VARIANTS MDDGC8 THR-165 AND LEU-253, AND CHARACTERIZATION OF VARIANTS
RP MDDGC8 THR-165 AND LEU-253.
RX PubMed=27066570; DOI=10.1212/nxg.0000000000000033;
RA Endo Y., Dong M., Noguchi S., Ogawa M., Hayashi Y.K., Kuru S., Sugiyama K.,
RA Nagai S., Ozasa S., Nonaka I., Nishino I.;
RT "Milder forms of muscular dystrophy associated with POMGNT2 mutations.";
RL Neurol. Genet. 1:E33-E33(2015).
CC -!- FUNCTION: O-linked mannose beta-1,4-N-acetylglucosaminyltransferase
CC that transfers UDP-N-acetyl-D-glucosamine to the 4-position of the
CC mannose to generate N-acetyl-D-glucosamine-beta-1,4-O-D-
CC mannosylprotein. Involved in the biosynthesis of the phosphorylated O-
CC mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-
CC acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate
CC structure present in alpha-dystroglycan (DAG1), which is required for
CC binding laminin G-like domain-containing extracellular proteins with
CC high affinity. {ECO:0000269|PubMed:23929950,
CC ECO:0000269|PubMed:27066570}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + UDP-N-acetyl-
CC alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-
CC D-mannosyl)-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:37663,
CC Rhea:RHEA-COMP:13547, Rhea:RHEA-COMP:13618, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:137323,
CC ChEBI:CHEBI:137540; EC=2.4.1.312;
CC Evidence={ECO:0000269|PubMed:23929950, ECO:0000269|PubMed:27066570};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:23929950}.
CC -!- INTERACTION:
CC Q8NAT1; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-10269044, EBI-945833;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23929950, ECO:0000269|PubMed:27066570}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:23929950}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain, muscle, heart, and
CC kidney in both fetus and adult. In the brain, highest expression in the
CC cortex and cerebellum. Highly expressed in the pancreas.
CC {ECO:0000269|PubMed:22958903}.
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain
CC and eye anomalies A8 (MDDGA8) [MIM:614830]: An autosomal recessive
CC disorder characterized by congenital muscular dystrophy associated with
CC cobblestone lissencephaly and other brain anomalies, eye malformations,
CC profound intellectual disability, and death usually in the first years
CC of life. Included diseases are the more severe Walker-Warburg syndrome
CC and the slightly less severe muscle-eye-brain disease.
CC {ECO:0000269|PubMed:22958903}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C8 (MDDGC8)
CC [MIM:618135]: An autosomal recessive muscular disease with onset in
CC childhood, characterized by limb-girdle muscular dystrophy and
CC intellectual disability without brain malformation. Disease severity is
CC highly variable and some patients may be clinically asymptomatic.
CC {ECO:0000269|PubMed:27066570}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 61 family.
CC {ECO:0000305}.
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DR EMBL; AK027472; BAB55137.1; -; mRNA.
DR EMBL; AK092147; BAC03816.1; -; mRNA.
DR EMBL; AK124737; BAG54085.1; -; mRNA.
DR EMBL; AC092042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64690.1; -; Genomic_DNA.
DR EMBL; BC060861; AAH60861.1; -; mRNA.
DR CCDS; CCDS2709.1; -.
DR RefSeq; NP_116195.2; NM_032806.5.
DR RefSeq; XP_005265572.1; XM_005265515.2.
DR RefSeq; XP_011532465.1; XM_011534163.2.
DR RefSeq; XP_011532466.1; XM_011534164.1.
DR RefSeq; XP_016862842.1; XM_017007353.1.
DR PDB; 6XFI; X-ray; 2.00 A; A=52-580.
DR PDBsum; 6XFI; -.
DR AlphaFoldDB; Q8NAT1; -.
DR SMR; Q8NAT1; -.
DR BioGRID; 124332; 123.
DR IntAct; Q8NAT1; 13.
DR MINT; Q8NAT1; -.
DR STRING; 9606.ENSP00000344125; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR GlyGen; Q8NAT1; 2 sites.
DR iPTMnet; Q8NAT1; -.
DR PhosphoSitePlus; Q8NAT1; -.
DR BioMuta; POMGNT2; -.
DR DMDM; 74729999; -.
DR EPD; Q8NAT1; -.
DR jPOST; Q8NAT1; -.
DR MassIVE; Q8NAT1; -.
DR MaxQB; Q8NAT1; -.
DR PaxDb; Q8NAT1; -.
DR PeptideAtlas; Q8NAT1; -.
DR PRIDE; Q8NAT1; -.
DR ProteomicsDB; 72695; -.
DR Antibodypedia; 29340; 158 antibodies from 26 providers.
DR DNASU; 84892; -.
DR Ensembl; ENST00000344697.3; ENSP00000344125.2; ENSG00000144647.7.
DR Ensembl; ENST00000441964.1; ENSP00000408992.1; ENSG00000144647.7.
DR Ensembl; ENST00000686643.1; ENSP00000509123.1; ENSG00000144647.7.
DR Ensembl; ENST00000687440.1; ENSP00000509610.1; ENSG00000144647.7.
DR Ensembl; ENST00000689987.1; ENSP00000510646.1; ENSG00000144647.7.
DR Ensembl; ENST00000692017.1; ENSP00000510571.1; ENSG00000144647.7.
DR Ensembl; ENST00000693717.1; ENSP00000510801.1; ENSG00000144647.7.
DR GeneID; 84892; -.
DR KEGG; hsa:84892; -.
DR MANE-Select; ENST00000344697.3; ENSP00000344125.2; NM_032806.6; NP_116195.2.
DR UCSC; uc003cmr.3; human.
DR CTD; 84892; -.
DR DisGeNET; 84892; -.
DR GeneCards; POMGNT2; -.
DR HGNC; HGNC:25902; POMGNT2.
DR HPA; ENSG00000144647; Low tissue specificity.
DR MalaCards; POMGNT2; -.
DR MIM; 614828; gene.
DR MIM; 614830; phenotype.
DR MIM; 618135; phenotype.
DR neXtProt; NX_Q8NAT1; -.
DR OpenTargets; ENSG00000144647; -.
DR Orphanet; 899; Walker-Warburg syndrome.
DR PharmGKB; PA142672374; -.
DR VEuPathDB; HostDB:ENSG00000144647; -.
DR eggNOG; KOG4698; Eukaryota.
DR GeneTree; ENSGT00940000160695; -.
DR HOGENOM; CLU_020169_0_0_1; -.
DR InParanoid; Q8NAT1; -.
DR OMA; EFQMRVV; -.
DR OrthoDB; 820160at2759; -.
DR PhylomeDB; Q8NAT1; -.
DR TreeFam; TF332712; -.
DR BioCyc; MetaCyc:ENSG00000144647-MON; -.
DR BRENDA; 2.4.1.312; 2681.
DR PathwayCommons; Q8NAT1; -.
DR Reactome; R-HSA-5173105; O-linked glycosylation.
DR SignaLink; Q8NAT1; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 84892; 10 hits in 1058 CRISPR screens.
DR ChiTaRS; POMGNT2; human.
DR GenomeRNAi; 84892; -.
DR Pharos; Q8NAT1; Tbio.
DR PRO; PR:Q8NAT1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8NAT1; protein.
DR Bgee; ENSG00000144647; Expressed in lateral nuclear group of thalamus and 175 other tissues.
DR ExpressionAtlas; Q8NAT1; baseline and differential.
DR Genevisible; Q8NAT1; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0097363; F:protein O-GlcNAc transferase activity; IDA:MGI.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007657; Glycosyltransferase_61.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR20961; PTHR20961; 1.
DR Pfam; PF04577; Glyco_transf_61; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Congenital muscular dystrophy; Disease variant;
KW Dystroglycanopathy; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Limb-girdle muscular dystrophy; Lissencephaly;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..580
FT /note="Protein O-linked-mannose beta-1,4-N-
FT acetylglucosaminyltransferase 2"
FT /id="PRO_0000249014"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..580
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 488..580
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 158
FT /note="R -> H (in MDDGA8; dbSNP:rs387907300)"
FT /evidence="ECO:0000269|PubMed:22958903"
FT /id="VAR_068967"
FT VARIANT 165
FT /note="M -> T (in MDDGC8; no effect on protein expression;
FT unchanged localization to the endoplasmic reticulum;
FT decreased protein O-GlcNAc transferase catalytic activity)"
FT /evidence="ECO:0000269|PubMed:27066570"
FT /id="VAR_081560"
FT VARIANT 197..580
FT /note="Missing (in MDDGA8)"
FT /evidence="ECO:0000269|PubMed:22958903"
FT /id="VAR_081561"
FT VARIANT 253
FT /note="P -> L (in MDDGC8; no effect on protein expression;
FT unchanged localization to the endoplasmic reticulum;
FT decreased protein O-GlcNAc transferase catalytic activity;
FT dbSNP:rs374042455)"
FT /evidence="ECO:0000269|PubMed:27066570"
FT /id="VAR_081562"
FT VARIANT 445..580
FT /note="Missing (in MDDGA8)"
FT /evidence="ECO:0000269|PubMed:22958903"
FT /id="VAR_081563"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 78..87
FT /evidence="ECO:0007829|PDB:6XFI"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 261..274
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 303..314
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:6XFI"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:6XFI"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 421..427
FT /evidence="ECO:0007829|PDB:6XFI"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 440..446
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 454..463
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 486..495
FT /evidence="ECO:0007829|PDB:6XFI"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 499..507
FT /evidence="ECO:0007829|PDB:6XFI"
FT HELIX 510..514
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 520..528
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 537..546
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 555..564
FT /evidence="ECO:0007829|PDB:6XFI"
FT TURN 565..567
FT /evidence="ECO:0007829|PDB:6XFI"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:6XFI"
SQ SEQUENCE 580 AA; 66615 MW; 57D7FD168373FD9D CRC64;
MHLSAVFNAL LVSVLAAVLW KHVRLREHAA TLEEELALSR QATEPAPALR IDYPKALQIL
MEGGTHMVCT GRTHTDRICR FKWLCYSNEA EEFIFFHGNT SVMLPNLGSR RFQPALLDLS
TVEDHNTQYF NFVELPAAAL RFMPKPVFVP DVALIANRFN PDNLMHVFHD DLLPLFYTLR
QFPGLAHEAR LFFMEGWGEG AHFDLYKLLS PKQPLLRAQL KTLGRLLCFS HAFVGLSKIT
TWYQYGFVQP QGPKANILVS GNEIRQFARF MTEKLNVSHT GVPLGEEYIL VFSRTQNRLI
LNEAELLLAL AQEFQMKTVT VSLEDHTFAD VVRLVSNASM LVSMHGAQLV TTLFLPRGAT
VVELFPYAVN PDHYTPYKTL AMLPGMDLQY VAWRNMMPEN TVTHPERPWD QGGITHLDRA
EQARILQSRE VPRHLCCRNP EWLFRIYQDT KVDIPSLIQT IRRVVKGRPG PRKQKWTVGL
YPGKVREARC QASVHGASEA RLTVSWQIPW NLKYLKVREV KYEVWLQEQG ENTYVPYILA
LQNHTFTENI KPFTTYLVWV RCIFNKILLG PFADVLVCNT
