UCK1_HUMAN
ID UCK1_HUMAN Reviewed; 277 AA.
AC Q9HA47; Q5JT09; Q5JT10; Q5JT12; Q5JT13; Q6IA74; Q96BJ0;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Uridine-cytidine kinase 1;
DE Short=UCK 1;
DE EC=2.7.1.48 {ECO:0000269|PubMed:11306702};
DE AltName: Full=Cytidine monophosphokinase 1;
DE AltName: Full=Uridine monophosphokinase 1;
GN Name=UCK1; Synonyms=URK1;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=11306702; DOI=10.1124/mol.59.5.1181;
RA Van Rompay A.R., Norda A., Linden K., Johansson M., Karlsson A.;
RT "Phosphorylation of uridine and cytidine nucleoside analogs by two human
RT uridine-cytidine kinases.";
RL Mol. Pharmacol. 59:1181-1186(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ho Y.S., Johnson R.K.;
RT "Human uridine kinase from prostate cancer cell line (LNCaP).";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Xin Y.R., Yu L., Zhao S.Y.;
RT "Cloning of a new human cDNA similar to Mus musculus uridine kinase mRNA.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Hippocampus, and Mammary gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Colon;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251 AND SER-253, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, AND IDENTIFICATION BY
RP 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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-243 IN COMPLEX WITH ADP.
RG Northeast structural genomics consortium (NESG);
RT "Structure of human uridine-cytidine kinase 1.";
RL Submitted (JAN-2007) to the PDB data bank.
CC -!- FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate
CC and cytidine monophosphate (PubMed:11306702). Does not phosphorylate
CC deoxyribonucleosides or purine ribonucleosides (PubMed:11306702). Can
CC use ATP or GTP as a phosphate donor (PubMed:11306702). Can also
CC phosphorylate cytidine and uridine nucleoside analogs such as 6-
CC azauridine, 5-fluorouridine, 4-thiouridine, 5-bromouridine, N(4)-
CC acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine,
CC 5-methylcytidine, and N(4)-anisoylcytidine (PubMed:11306702).
CC {ECO:0000269|PubMed:11306702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000269|PubMed:11306702};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000269|PubMed:11306702};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3. {ECO:0000269|PubMed:11306702}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1. {ECO:0000269|PubMed:11306702}.
CC -!- INTERACTION:
CC Q9HA47-2; P22607: FGFR3; NbExp=3; IntAct=EBI-16434682, EBI-348399;
CC Q9HA47-2; P06396: GSN; NbExp=3; IntAct=EBI-16434682, EBI-351506;
CC Q9HA47-2; A0A0S2Z5Y6: UCK1; NbExp=3; IntAct=EBI-16434682, EBI-16434671;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9HA47-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HA47-2; Sequence=VSP_041269;
CC Name=3;
CC IsoId=Q9HA47-3; Sequence=VSP_045174;
CC Name=4;
CC IsoId=Q9HA47-4; Sequence=VSP_056748;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11306702}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
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DR EMBL; AF237290; AAK28324.1; -; mRNA.
DR EMBL; AF254133; AAK49122.1; -; mRNA.
DR EMBL; AF125106; AAL75943.1; -; mRNA.
DR EMBL; AK022317; BAB14010.1; -; mRNA.
DR EMBL; AK295471; BAG58400.1; -; mRNA.
DR EMBL; CR457281; CAG33562.1; -; mRNA.
DR EMBL; AL358781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87983.1; -; Genomic_DNA.
DR EMBL; BC015547; AAH15547.1; -; mRNA.
DR EMBL; BC091495; AAH91495.1; -; mRNA.
DR CCDS; CCDS48046.1; -. [Q9HA47-2]
DR CCDS; CCDS59151.1; -. [Q9HA47-3]
DR CCDS; CCDS59152.1; -. [Q9HA47-4]
DR CCDS; CCDS6944.1; -. [Q9HA47-1]
DR RefSeq; NP_001129426.1; NM_001135954.2. [Q9HA47-2]
DR RefSeq; NP_001248379.1; NM_001261450.2. [Q9HA47-3]
DR RefSeq; NP_001248380.1; NM_001261451.2. [Q9HA47-4]
DR RefSeq; NP_001305448.1; NM_001318519.1.
DR RefSeq; NP_113620.1; NM_031432.3. [Q9HA47-1]
DR PDB; 2JEO; X-ray; 2.50 A; A=22-243.
DR PDB; 2UVQ; X-ray; 3.00 A; A=22-243.
DR PDBsum; 2JEO; -.
DR PDBsum; 2UVQ; -.
DR AlphaFoldDB; Q9HA47; -.
DR SMR; Q9HA47; -.
DR BioGRID; 123681; 16.
DR IntAct; Q9HA47; 10.
DR STRING; 9606.ENSP00000361285; -.
DR ChEMBL; CHEMBL5682; -.
DR DrugCentral; Q9HA47; -.
DR GlyGen; Q9HA47; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HA47; -.
DR MetOSite; Q9HA47; -.
DR PhosphoSitePlus; Q9HA47; -.
DR BioMuta; UCK1; -.
DR DMDM; 20455360; -.
DR EPD; Q9HA47; -.
DR jPOST; Q9HA47; -.
DR MassIVE; Q9HA47; -.
DR MaxQB; Q9HA47; -.
DR PaxDb; Q9HA47; -.
DR PeptideAtlas; Q9HA47; -.
DR PRIDE; Q9HA47; -.
DR ProteomicsDB; 63191; -.
DR ProteomicsDB; 63192; -.
DR ProteomicsDB; 81375; -. [Q9HA47-1]
DR ProteomicsDB; 81376; -. [Q9HA47-2]
DR Antibodypedia; 31627; 334 antibodies from 22 providers.
DR DNASU; 83549; -.
DR Ensembl; ENST00000372208.7; ENSP00000361282.3; ENSG00000130717.13. [Q9HA47-2]
DR Ensembl; ENST00000372210.7; ENSP00000361284.3; ENSG00000130717.13. [Q9HA47-3]
DR Ensembl; ENST00000372211.7; ENSP00000361285.3; ENSG00000130717.13. [Q9HA47-4]
DR Ensembl; ENST00000372215.5; ENSP00000361289.4; ENSG00000130717.13. [Q9HA47-1]
DR GeneID; 83549; -.
DR KEGG; hsa:83549; -.
DR MANE-Select; ENST00000372215.5; ENSP00000361289.4; NM_031432.5; NP_113620.1.
DR UCSC; uc004cay.4; human. [Q9HA47-1]
DR CTD; 83549; -.
DR DisGeNET; 83549; -.
DR GeneCards; UCK1; -.
DR HGNC; HGNC:14859; UCK1.
DR HPA; ENSG00000130717; Low tissue specificity.
DR MIM; 609328; gene.
DR neXtProt; NX_Q9HA47; -.
DR OpenTargets; ENSG00000130717; -.
DR PharmGKB; PA134861770; -.
DR VEuPathDB; HostDB:ENSG00000130717; -.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT01020000230412; -.
DR HOGENOM; CLU_021278_1_4_1; -.
DR InParanoid; Q9HA47; -.
DR OMA; TTLKPMH; -.
DR OrthoDB; 929897at2759; -.
DR PhylomeDB; Q9HA47; -.
DR TreeFam; TF316686; -.
DR BioCyc; MetaCyc:HS05429-MON; -.
DR BRENDA; 2.7.1.48; 2681.
DR PathwayCommons; Q9HA47; -.
DR Reactome; R-HSA-73614; Pyrimidine salvage.
DR SABIO-RK; Q9HA47; -.
DR SignaLink; Q9HA47; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR BioGRID-ORCS; 83549; 15 hits in 1078 CRISPR screens.
DR ChiTaRS; UCK1; human.
DR EvolutionaryTrace; Q9HA47; -.
DR GenomeRNAi; 83549; -.
DR Pharos; Q9HA47; Tbio.
DR PRO; PR:Q9HA47; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9HA47; protein.
DR Bgee; ENSG00000130717; Expressed in pancreatic ductal cell and 168 other tissues.
DR ExpressionAtlas; Q9HA47; baseline and differential.
DR Genevisible; Q9HA47; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043771; F:cytidine kinase activity; IDA:UniProtKB.
DR GO; GO:0004849; F:uridine kinase activity; IDA:UniProtKB.
DR GO; GO:0044211; P:CTP salvage; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0044206; P:UMP salvage; IDA:UniProtKB.
DR CDD; cd02023; UMPK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR029920; UCK-1.
DR InterPro; IPR000764; Uridine_kinase-like.
DR PANTHER; PTHR10285:SF66; PTHR10285:SF66; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..277
FT /note="Uridine-cytidine kinase 1"
FT /id="PRO_0000164453"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|Ref.12"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|Ref.12"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 28..36
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045174"
FT VAR_SEQ 28..36
FT /note="VSGGTASGK -> DERFQAGIPLLCLQ (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_056748"
FT VAR_SEQ 170..277
FT /note="VLRDVRRGRDLEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAIN
FT LIVQHIQDILNGDICKWHRGGSNGRSYKRTFSEPGDHPGMLTSGKRSHLESSSRPH ->
FT DKEVCRCDHPARSGQYGCHQPDRAAHPGHSEW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041269"
FT CONFLICT 8..17
FT /note="DCESPAPEAD -> GARARAGAN (in Ref. 3; AAL75943)"
FT /evidence="ECO:0000305"
FT CONFLICT 56..57
FT /note="QR -> HG (in Ref. 3; AAL75943)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="R -> H (in Ref. 5; CAG33562)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="S -> T (in Ref. 3; AAL75943)"
FT /evidence="ECO:0000305"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:2JEO"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:2JEO"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:2JEO"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:2JEO"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:2JEO"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:2JEO"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:2JEO"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2JEO"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:2JEO"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2JEO"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:2JEO"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2JEO"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:2JEO"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:2JEO"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:2JEO"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:2JEO"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:2JEO"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:2JEO"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:2JEO"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:2JEO"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:2JEO"
FT HELIX 217..232
FT /evidence="ECO:0007829|PDB:2JEO"
FT CONFLICT Q9HA47-2:180
FT /note="A -> T (in Ref. 8; AAH15547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 31435 MW; AFD9ED92780CD502 CRC64;
MASAGGEDCE SPAPEADRPH QRPFLIGVSG GTASGKSTVC EKIMELLGQN EVEQRQRKVV
ILSQDRFYKV LTAEQKAKAL KGQYNFDHPD AFDNDLMHRT LKNIVEGKTV EVPTYDFVTH
SRLPETTVVY PADVVLFEGI LVFYSQEIRD MFHLRLFVDT DSDVRLSRRV LRDVRRGRDL
EQILTQYTTF VKPAFEEFCL PTKKYADVII PRGVDNMVAI NLIVQHIQDI LNGDICKWHR
GGSNGRSYKR TFSEPGDHPG MLTSGKRSHL ESSSRPH
