UAP1_HUMAN
ID UAP1_HUMAN Reviewed; 522 AA.
AC Q16222; B2R6R8; Q5VTA9; Q5VTB0; Q5VTB1; Q96GM2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=UDP-N-acetylhexosamine pyrophosphorylase;
DE AltName: Full=Antigen X;
DE Short=AGX;
DE AltName: Full=Sperm-associated antigen 2;
DE Includes:
DE RecName: Full=UDP-N-acetylgalactosamine pyrophosphorylase;
DE EC=2.7.7.83;
DE AltName: Full=AGX-1;
DE Includes:
DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase;
DE EC=2.7.7.23;
DE AltName: Full=AGX-2;
GN Name=UAP1; Synonyms=SPAG2;
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] (ISOFORMS AGX1; AGX2 AND 3).
RC TISSUE=Testis;
RX PubMed=8025165; DOI=10.1095/biolreprod50.5.1087;
RA Diekman A.B., Goldberg E.;
RT "Characterization of a human antigen with sera from infertile patients.";
RL Biol. Reprod. 50:1087-1093(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AGX1).
RC TISSUE=Testis;
RX PubMed=9603950; DOI=10.1074/jbc.273.23.14392;
RA Mio T., Yabe T., Arisawa M., Yamada-Okabe H.;
RT "The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases: gene cloning,
RT protein expression, and catalytic mechanism.";
RL J. Biol. Chem. 273:14392-14397(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM AGX1).
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] (ISOFORMS AGX1; AGX2 AND 3).
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(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 AGX1).
RC TISSUE=Muscle;
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 PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING, CATALYTIC ACTIVITY, AND
RP CHARACTERIZATION.
RC TISSUE=Mammary cancer;
RX PubMed=9765219; DOI=10.1074/jbc.273.42.27055;
RA Wang-Gillam A., Pastuszak I., Elbein A.D.;
RT "A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase
RT specificity from UDP-GalNAc to UDP-GlcNAc.";
RL J. Biol. Chem. 273:27055-27057(1998).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
RX PubMed=11707391; DOI=10.1093/emboj/20.22.6191;
RA Peneff C., Ferrari P., Charrier V., Taburet Y., Monnier C., Zamboni V.,
RA Winter J., Harnois M., Fassy F., Bourne Y.;
RT "Crystal structures of two human pyrophosphorylase isoforms in complexes
RT with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme
RT oligomeric assembly and active site architecture.";
RL EMBO J. 20:6191-6202(2001).
CC -!- FUNCTION: Converts UTP and GlcNAc-1-P into UDP-GlcNAc, and UTP and
CC GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher
CC activity towards GalNAc-1-P, while isoform AGX2 has 8 times more
CC activity towards GlcNAc-1-P.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-galactosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-galactosamine;
CC Xref=Rhea:RHEA:34363, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:61970, ChEBI:CHEBI:67138; EC=2.7.7.83;
CC Evidence={ECO:0000269|PubMed:9765219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC Evidence={ECO:0000269|PubMed:9765219};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
CC -!- SUBUNIT: Monomer and homodimer. Isoform AGX1 is a homodimer. Isoform
CC AGX2 is a monomer. {ECO:0000269|PubMed:11707391}.
CC -!- INTERACTION:
CC Q16222; Q16222: UAP1; NbExp=3; IntAct=EBI-10237564, EBI-10237564;
CC Q16222-2; Q16222-2: UAP1; NbExp=3; IntAct=EBI-12293309, EBI-12293309;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In spermatozoa, localized to the
CC principal piece of the tail, the neck region of the head and to a
CC lesser extent, the midpiece of the tail.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=AGX2; Synonyms=AGX-2;
CC IsoId=Q16222-1; Sequence=Displayed;
CC Name=AGX1; Synonyms=AGX-1;
CC IsoId=Q16222-2; Sequence=VSP_004483;
CC Name=3;
CC IsoId=Q16222-3; Sequence=VSP_014523;
CC -!- TISSUE SPECIFICITY: Widely expressed. Isoform AGX1 is more abundant in
CC testis than isoform AGX2, while isoform AGX2 is more abundant than
CC isoform AGX1 in somatic tissue. Expressed at low level in placenta,
CC muscle and liver.
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR EMBL; S73498; AAB31210.2; -; mRNA.
DR EMBL; AB011004; BAA31202.1; -; mRNA.
DR EMBL; AK312685; BAG35565.1; -; mRNA.
DR EMBL; AL596325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90710.1; -; Genomic_DNA.
DR EMBL; BC009377; AAH09377.1; -; mRNA.
DR CCDS; CCDS1240.1; -. [Q16222-2]
DR CCDS; CCDS81393.1; -. [Q16222-1]
DR CCDS; CCDS81394.1; -. [Q16222-3]
DR RefSeq; NP_001311042.1; NM_001324113.1. [Q16222-2]
DR RefSeq; NP_001311043.1; NM_001324114.1. [Q16222-2]
DR RefSeq; NP_001311044.1; NM_001324115.1. [Q16222-2]
DR RefSeq; NP_001311045.1; NM_001324116.1. [Q16222-1]
DR RefSeq; NP_001311046.1; NM_001324117.1. [Q16222-3]
DR RefSeq; NP_003106.3; NM_003115.4. [Q16222-2]
DR RefSeq; XP_011508215.1; XM_011509913.2. [Q16222-1]
DR RefSeq; XP_011508216.1; XM_011509914.2. [Q16222-1]
DR PDB; 1JV1; X-ray; 1.90 A; A/B=1-522.
DR PDB; 1JV3; X-ray; 2.20 A; A/B=1-522.
DR PDB; 1JVD; X-ray; 2.40 A; A/B=1-522.
DR PDB; 1JVG; X-ray; 2.30 A; A/B=1-522.
DR PDB; 6Z2F; X-ray; 1.70 A; A/B=1-522.
DR PDBsum; 1JV1; -.
DR PDBsum; 1JV3; -.
DR PDBsum; 1JVD; -.
DR PDBsum; 1JVG; -.
DR PDBsum; 6Z2F; -.
DR AlphaFoldDB; Q16222; -.
DR SMR; Q16222; -.
DR BioGRID; 112557; 31.
DR IntAct; Q16222; 10.
DR STRING; 9606.ENSP00000356903; -.
DR DrugBank; DB02196; Uridine-Diphosphate-N-Acetylgalactosamine.
DR DrugBank; DB03397; Uridine-Diphosphate-N-Acetylglucosamine.
DR GlyGen; Q16222; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16222; -.
DR MetOSite; Q16222; -.
DR PhosphoSitePlus; Q16222; -.
DR BioMuta; UAP1; -.
DR DMDM; 68846235; -.
DR REPRODUCTION-2DPAGE; IPI00217816; -.
DR EPD; Q16222; -.
DR jPOST; Q16222; -.
DR MassIVE; Q16222; -.
DR MaxQB; Q16222; -.
DR PaxDb; Q16222; -.
DR PeptideAtlas; Q16222; -.
DR PRIDE; Q16222; -.
DR ProteomicsDB; 60840; -. [Q16222-1]
DR ProteomicsDB; 60841; -. [Q16222-2]
DR ProteomicsDB; 60842; -. [Q16222-3]
DR Antibodypedia; 1654; 256 antibodies from 30 providers.
DR DNASU; 6675; -.
DR Ensembl; ENST00000271469.7; ENSP00000271469.3; ENSG00000117143.13. [Q16222-1]
DR Ensembl; ENST00000367924.1; ENSP00000356901.1; ENSG00000117143.13. [Q16222-3]
DR Ensembl; ENST00000367925.5; ENSP00000356902.1; ENSG00000117143.13. [Q16222-1]
DR Ensembl; ENST00000367926.8; ENSP00000356903.4; ENSG00000117143.13. [Q16222-2]
DR GeneID; 6675; -.
DR KEGG; hsa:6675; -.
DR MANE-Select; ENST00000367925.6; ENSP00000356902.1; NM_001324116.5; NP_001311045.1.
DR UCSC; uc001gce.5; human. [Q16222-1]
DR CTD; 6675; -.
DR DisGeNET; 6675; -.
DR GeneCards; UAP1; -.
DR HGNC; HGNC:12457; UAP1.
DR HPA; ENSG00000117143; Low tissue specificity.
DR MIM; 602862; gene.
DR neXtProt; NX_Q16222; -.
DR OpenTargets; ENSG00000117143; -.
DR PharmGKB; PA37107; -.
DR VEuPathDB; HostDB:ENSG00000117143; -.
DR eggNOG; KOG2388; Eukaryota.
DR GeneTree; ENSGT00940000153464; -.
DR HOGENOM; CLU_025603_1_0_1; -.
DR InParanoid; Q16222; -.
DR OMA; QPDVLKF; -.
DR OrthoDB; 888726at2759; -.
DR PhylomeDB; Q16222; -.
DR TreeFam; TF300611; -.
DR BRENDA; 2.7.7.23; 2681.
DR BRENDA; 2.7.7.83; 2681.
DR PathwayCommons; Q16222; -.
DR Reactome; R-HSA-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR SABIO-RK; Q16222; -.
DR SignaLink; Q16222; -.
DR UniPathway; UPA00113; UER00533.
DR BioGRID-ORCS; 6675; 106 hits in 1088 CRISPR screens.
DR ChiTaRS; UAP1; human.
DR EvolutionaryTrace; Q16222; -.
DR GeneWiki; UAP1; -.
DR GenomeRNAi; 6675; -.
DR Pharos; Q16222; Tbio.
DR PRO; PR:Q16222; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q16222; protein.
DR Bgee; ENSG00000117143; Expressed in synovial joint and 208 other tissues.
DR ExpressionAtlas; Q16222; baseline and differential.
DR Genevisible; Q16222; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0052630; F:UDP-N-acetylgalactosamine diphosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
DR DisProt; DP00363; -.
DR DisProt; DP01098; -. [Q16222-2]
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR039741; UDP-sugar_pyrophosphorylase.
DR InterPro; IPR002618; UDPGP_fam.
DR PANTHER; PTHR11952; PTHR11952; 1.
DR Pfam; PF01704; UDPGP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..522
FT /note="UDP-N-acetylhexosamine pyrophosphorylase"
FT /id="PRO_0000185767"
FT MOTIF 108..111
FT /note="Substrate binding"
FT MOTIF 303..304
FT /note="Substrate binding"
FT BINDING 108..111
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 122
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 196
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 222
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11707391"
FT BINDING 253
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 377
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11707391"
FT VAR_SEQ 454..470
FT /note="Missing (in isoform AGX1)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8025165,
FT ECO:0000303|PubMed:9603950"
FT /id="VSP_004483"
FT VAR_SEQ 454
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8025165"
FT /id="VSP_014523"
FT VARIANT 418
FT /note="P -> H (in dbSNP:rs1128539)"
FT /id="VAR_014935"
FT CONFLICT 61
FT /note="H -> Y (in Ref. 6; AAH09377)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="G -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="S -> Q (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1JV1"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1JV1"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:1JV1"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1JV1"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 135..154
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:6Z2F"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:1JV1"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 325..334
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 382..388
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 418..435
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:6Z2F"
FT TURN 485..487
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:6Z2F"
FT HELIX 495..498
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 505..510
FT /evidence="ECO:0007829|PDB:6Z2F"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:6Z2F"
SQ SEQUENCE 522 AA; 58769 MW; 8A69B36D852B9472 CRC64;
MNINDLKLTL SKAGQEHLLR FWNELEEAQQ VELYAELQAM NFEELNFFFQ KAIEGFNQSS
HQKNVDARME PVPREVLGSA TRDQDQLQAW ESEGLFQISQ NKVAVLLLAG GQGTRLGVAY
PKGMYDVGLP SRKTLFQIQA ERILKLQQVA EKYYGNKCII PWYIMTSGRT MESTKEFFTK
HKYFGLKKEN VIFFQQGMLP AMSFDGKIIL EEKNKVSMAP DGNGGLYRAL AAQNIVEDME
QRGIWSIHVY CVDNILVKVA DPRFIGFCIQ KGADCGAKVV EKTNPTEPVG VVCRVDGVYQ
VVEYSEISLA TAQKRSSDGR LLFNAGNIAN HFFTVPFLRD VVNVYEPQLQ HHVAQKKIPY
VDTQGQLIKP DKPNGIKMEK FVFDIFQFAK KFVVYEVLRE DEFSPLKNAD SQNGKDNPTT
ARHALMSLHH CWVLNAGGHF IDENGSRLPA IPRSATNGKS ETITADVNHN LKDANDVPIQ
CEISPLISYA GEGLESYVAD KEFHAPLIID ENGVHELVKN GI
