P4HA1_HUMAN
ID P4HA1_HUMAN Reviewed; 534 AA.
AC P13674; C9JL12; Q15082; Q15083; Q5VSQ5;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-1;
DE Short=4-PH alpha-1;
DE EC=1.14.11.2 {ECO:0000269|PubMed:9211872};
DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1;
DE Flags: Precursor;
GN Name=P4HA1; Synonyms=P4HA;
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 1 AND 2).
RX PubMed=2543975; DOI=10.1073/pnas.86.12.4392;
RA Helaakoski T., Vuori K., Myllylae R., Kivirikko K.I., Pihlajaniemi T.;
RT "Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the
RT complete cDNA-derived amino acid sequence and evidence for alternative
RT splicing of RNA transcripts.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4392-4396(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=7961714; DOI=10.1016/s0021-9258(18)46864-0;
RA Helaakoski T., Veijola J., Vuori K., Rehn M., Chow L.T., Taillon-Miller P.,
RA Kivirikko K.I., Pihlajaniemi T.;
RT "Structure and expression of the human gene for the alpha subunit of prolyl
RT 4-hydroxylase. The two alternatively spliced types of mRNA correspond to
RT two homologous exons the sequences of which are expressed in a variety of
RT tissues.";
RL J. Biol. Chem. 269:27847-27854(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15028279; DOI=10.1016/j.ygeno.2003.09.023;
RA Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R., Au-Young J.,
RA Stuve L.L.;
RT "PCR isolation and cloning of novel splice variant mRNAs from known drug
RT target genes.";
RL Genomics 83:566-571(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, COFACTOR, AND TISSUE SPECIFICITY.
RX PubMed=9211872; DOI=10.1074/jbc.272.28.17342;
RA Annunen P., Helaakoski T., Myllyharju J., Veijola J., Pihlajaniemi T.,
RA Kivirikko K.I.;
RT "Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II)
RT and characterization of the type II enzyme tetramer. The alpha(I) and
RT alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer.";
RL J. Biol. Chem. 272:17342-17348(1997).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-113.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
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 CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-17, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 161-261, SUBUNIT, AND MUTAGENESIS
RP OF TYR-210; TYR-213 AND TYR-247.
RX PubMed=15456751; DOI=10.1074/jbc.m410007200;
RA Pekkala M., Hieta R., Bergmann U., Kivirikko K.I., Wierenga R.K.,
RA Myllyharju J.;
RT "The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is
RT a tetratricopeptide repeat domain with functional aromatic residues.";
RL J. Biol. Chem. 279:52255-52261(2004).
CC -!- FUNCTION: Catalyzes the post-translational formation of 4-
CC hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other
CC proteins. {ECO:0000269|PubMed:9211872}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate +
CC trans-4-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:18945, Rhea:RHEA-
CC COMP:11676, Rhea:RHEA-COMP:11680, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.2;
CC Evidence={ECO:0000269|PubMed:9211872};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000305|PubMed:9211872};
CC Note=Binds 1 Fe(2+) ion per subunit.;
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000305|PubMed:9211872};
CC -!- ACTIVITY REGULATION: Inhibited by poly(L-proline).
CC {ECO:0000269|PubMed:9211872}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22 uM for 2-oxoglutarate {ECO:0000269|PubMed:9211872};
CC -!- SUBUNIT: Heterotetramer of two alpha-1 chains and two beta chains
CC (P4HB)(the beta chain is the multi-functional PDI), where P4HB plays
CC the role of a structural subunit; this tetramer catalyzes the formation
CC of 4-hydroxyproline in collagen. {ECO:0000269|PubMed:15456751,
CC ECO:0000269|PubMed:9211872}.
CC -!- INTERACTION:
CC P13674; P42858: HTT; NbExp=5; IntAct=EBI-1237386, EBI-466029;
CC P13674; P13674: P4HA1; NbExp=5; IntAct=EBI-1237386, EBI-1237386;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P13674-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13674-2; Sequence=VSP_004504;
CC Name=3;
CC IsoId=P13674-3; Sequence=VSP_004504, VSP_044578;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, liver, skeletal muscle,
CC kidney, placenta, lung and pancreas. {ECO:0000269|PubMed:9211872}.
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
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DR EMBL; M24486; AAA36534.1; -; mRNA.
DR EMBL; M24487; AAA36535.1; -; mRNA.
DR EMBL; U14620; AAA59068.1; -; Genomic_DNA.
DR EMBL; U14607; AAA59068.1; JOINED; Genomic_DNA.
DR EMBL; U14605; AAA59068.1; JOINED; Genomic_DNA.
DR EMBL; U14608; AAA59068.1; JOINED; Genomic_DNA.
DR EMBL; U14609; AAA59068.1; JOINED; Genomic_DNA.
DR EMBL; U14611; AAA59068.1; JOINED; Genomic_DNA.
DR EMBL; U14610; AAA59068.1; JOINED; Genomic_DNA.
DR EMBL; U14612; AAA59068.1; JOINED; Genomic_DNA.
DR EMBL; U14614; AAA59068.1; JOINED; Genomic_DNA.
DR EMBL; U14615; AAA59068.1; JOINED; Genomic_DNA.
DR EMBL; U14616; AAA59068.1; JOINED; Genomic_DNA.
DR EMBL; U14617; AAA59068.1; JOINED; Genomic_DNA.
DR EMBL; U14618; AAA59068.1; JOINED; Genomic_DNA.
DR EMBL; U14619; AAA59068.1; JOINED; Genomic_DNA.
DR EMBL; U14620; AAA59069.1; -; Genomic_DNA.
DR EMBL; U14607; AAA59069.1; JOINED; Genomic_DNA.
DR EMBL; U14605; AAA59069.1; JOINED; Genomic_DNA.
DR EMBL; U14608; AAA59069.1; JOINED; Genomic_DNA.
DR EMBL; U14609; AAA59069.1; JOINED; Genomic_DNA.
DR EMBL; U14611; AAA59069.1; JOINED; Genomic_DNA.
DR EMBL; U14610; AAA59069.1; JOINED; Genomic_DNA.
DR EMBL; U14612; AAA59069.1; JOINED; Genomic_DNA.
DR EMBL; U14613; AAA59069.1; JOINED; Genomic_DNA.
DR EMBL; U14615; AAA59069.1; JOINED; Genomic_DNA.
DR EMBL; U14616; AAA59069.1; JOINED; Genomic_DNA.
DR EMBL; U14617; AAA59069.1; JOINED; Genomic_DNA.
DR EMBL; U14618; AAA59069.1; JOINED; Genomic_DNA.
DR EMBL; U14619; AAA59069.1; JOINED; Genomic_DNA.
DR EMBL; CD013929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034998; AAH34998.1; -; mRNA.
DR CCDS; CCDS41537.1; -. [P13674-1]
DR CCDS; CCDS44432.1; -. [P13674-3]
DR CCDS; CCDS7320.1; -. [P13674-2]
DR PIR; A33919; DAHUA1.
DR PIR; I37173; DAHUA2.
DR RefSeq; NP_000908.2; NM_000917.3. [P13674-2]
DR RefSeq; NP_001017962.1; NM_001017962.2. [P13674-1]
DR RefSeq; NP_001136067.1; NM_001142595.1. [P13674-1]
DR RefSeq; NP_001136068.1; NM_001142596.1. [P13674-3]
DR PDB; 1TJC; X-ray; 2.30 A; A/B=161-261.
DR PDB; 2V5F; X-ray; 2.03 A; A=161-263.
DR PDB; 2YQ8; X-ray; 2.99 A; A/B=18-255.
DR PDB; 4BT8; X-ray; 2.20 A; A/B=18-255.
DR PDB; 4BT9; X-ray; 1.90 A; A/B=18-255.
DR PDB; 4BTA; X-ray; 2.95 A; A/B=18-261.
DR PDB; 4BTB; X-ray; 1.90 A; A=18-255.
DR PDBsum; 1TJC; -.
DR PDBsum; 2V5F; -.
DR PDBsum; 2YQ8; -.
DR PDBsum; 4BT8; -.
DR PDBsum; 4BT9; -.
DR PDBsum; 4BTA; -.
DR PDBsum; 4BTB; -.
DR AlphaFoldDB; P13674; -.
DR SMR; P13674; -.
DR BioGRID; 111072; 242.
DR CORUM; P13674; -.
DR DIP; DIP-38180N; -.
DR IntAct; P13674; 70.
DR MINT; P13674; -.
DR STRING; 9606.ENSP00000263556; -.
DR BindingDB; P13674; -.
DR ChEMBL; CHEMBL1250350; -.
DR DrugBank; DB00126; Ascorbic acid.
DR DrugBank; DB01275; Hydralazine.
DR DrugBank; DB00172; Proline.
DR DrugBank; DB00139; Succinic acid.
DR DrugCentral; P13674; -.
DR GlyConnect; 1640; 9 N-Linked glycans (1 site).
DR GlyGen; P13674; 3 sites, 8 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P13674; -.
DR MetOSite; P13674; -.
DR PhosphoSitePlus; P13674; -.
DR SwissPalm; P13674; -.
DR BioMuta; P4HA1; -.
DR DMDM; 2507090; -.
DR EPD; P13674; -.
DR jPOST; P13674; -.
DR MassIVE; P13674; -.
DR MaxQB; P13674; -.
DR PaxDb; P13674; -.
DR PeptideAtlas; P13674; -.
DR PRIDE; P13674; -.
DR ProteomicsDB; 10641; -.
DR ProteomicsDB; 52957; -. [P13674-1]
DR ProteomicsDB; 52958; -. [P13674-2]
DR Antibodypedia; 2000; 264 antibodies from 33 providers.
DR DNASU; 5033; -.
DR Ensembl; ENST00000263556.3; ENSP00000263556.3; ENSG00000122884.13. [P13674-2]
DR Ensembl; ENST00000307116.6; ENSP00000307318.2; ENSG00000122884.13. [P13674-1]
DR Ensembl; ENST00000373008.6; ENSP00000362099.1; ENSG00000122884.13. [P13674-2]
DR Ensembl; ENST00000394890.7; ENSP00000378353.2; ENSG00000122884.13. [P13674-1]
DR Ensembl; ENST00000440381.5; ENSP00000414464.1; ENSG00000122884.13. [P13674-3]
DR GeneID; 5033; -.
DR KEGG; hsa:5033; -.
DR MANE-Select; ENST00000394890.7; ENSP00000378353.2; NM_001017962.3; NP_001017962.1.
DR UCSC; uc001jtg.4; human. [P13674-1]
DR CTD; 5033; -.
DR DisGeNET; 5033; -.
DR GeneCards; P4HA1; -.
DR HGNC; HGNC:8546; P4HA1.
DR HPA; ENSG00000122884; Low tissue specificity.
DR MIM; 176710; gene.
DR neXtProt; NX_P13674; -.
DR OpenTargets; ENSG00000122884; -.
DR PharmGKB; PA32874; -.
DR VEuPathDB; HostDB:ENSG00000122884; -.
DR eggNOG; KOG1591; Eukaryota.
DR GeneTree; ENSGT00940000156635; -.
DR HOGENOM; CLU_024155_1_1_1; -.
DR InParanoid; P13674; -.
DR OMA; NTRAKNN; -.
DR PhylomeDB; P13674; -.
DR TreeFam; TF313393; -.
DR BioCyc; MetaCyc:HS04613-MON; -.
DR BRENDA; 1.14.11.2; 2681.
DR PathwayCommons; P13674; -.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR SignaLink; P13674; -.
DR BioGRID-ORCS; 5033; 22 hits in 1082 CRISPR screens.
DR ChiTaRS; P4HA1; human.
DR EvolutionaryTrace; P13674; -.
DR GeneWiki; P4HA1; -.
DR GenomeRNAi; 5033; -.
DR Pharos; P13674; Tchem.
DR PRO; PR:P13674; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P13674; protein.
DR Bgee; ENSG00000122884; Expressed in cartilage tissue and 205 other tissues.
DR ExpressionAtlas; P13674; baseline and differential.
DR Genevisible; P13674; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0016222; C:procollagen-proline 4-dioxygenase complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR013547; Pro_4_hyd_alph_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10869; PTHR10869; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF08336; P4Ha_N; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Dioxygenase; Endoplasmic reticulum;
KW Glycoprotein; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Signal; TPR repeat; Vitamin C.
FT SIGNAL 1..17
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 18..534
FT /note="Prolyl 4-hydroxylase subunit alpha-1"
FT /id="PRO_0000022723"
FT REPEAT 205..238
FT /note="TPR"
FT DOMAIN 411..519
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 429
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 431
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 500
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 510
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT VAR_SEQ 361..380
FT /note="RRATISNPITGDLETVHYRI -> SRATVHDPETGKLTTAQYRV (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15028279,
FT ECO:0000303|PubMed:2543975"
FT /id="VSP_004504"
FT VAR_SEQ 417..434
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15028279"
FT /id="VSP_044578"
FT MUTAGEN 210
FT /note="Y->A: Strongly reduced affinity for peptide
FT substrate."
FT /evidence="ECO:0000269|PubMed:15456751"
FT MUTAGEN 213
FT /note="Y->A: Strongly reduced affinity for peptide
FT substrate."
FT /evidence="ECO:0000269|PubMed:15456751"
FT MUTAGEN 247
FT /note="Y->A: Strongly reduced affinity for peptide
FT substrate."
FT /evidence="ECO:0000269|PubMed:15456751"
FT CONFLICT 119..122
FT /note="QYFP -> PVLS (in Ref. 1; AAA36534/AAA36535)"
FT /evidence="ECO:0000305"
FT HELIX 21..71
FT /evidence="ECO:0007829|PDB:4BTB"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:4BT9"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:4BTB"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:4BTB"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:4BTB"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:4BTB"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:4BTB"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:4BTB"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:4BTB"
FT HELIX 180..195
FT /evidence="ECO:0007829|PDB:4BTB"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:4BTB"
FT HELIX 221..234
FT /evidence="ECO:0007829|PDB:4BTB"
FT HELIX 239..252
FT /evidence="ECO:0007829|PDB:4BTB"
SQ SEQUENCE 534 AA; 61049 MW; EBAFA8CCF09A1DDB CRC64;
MIWYILIIGI LLPQSLAHPG FFTSIGQMTD LIHTEKDLVT SLKDYIKAEE DKLEQIKKWA
EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN LVLKDMSDGF ISNLTIQRQY
FPNDEDQVGA AKALLRLQDT YNLDTDTISK GNLPGVKHKS FLTAEDCFEL GKVAYTEADY
YHTELWMEQA LRQLDEGEIS TIDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR
ANGNLKYFEY IMAKEKDVNK SASDDQSDQK TTPKKKGVAV DYLPERQKYE MLCRGEGIKM
TPRRQKKLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE IVKDLAKPRL
RRATISNPIT GDLETVHYRI SKSAWLSGYE NPVVSRINMR IQDLTGLDVS TAEELQVANY
GVGGQYEPHF DFARKDEPDA FKELGTGNRI ATWLFYMSDV SAGGATVFPE VGASVWPKKG
TAVFWYNLFA SGEGDYSTRH AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE
