UCKL1_HUMAN
ID UCKL1_HUMAN Reviewed; 548 AA.
AC Q9NWZ5; B7Z8N2; Q5JWV0; Q70AQ5; Q8N524; Q9H3Z2;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Uridine-cytidine kinase-like 1;
DE EC=2.7.1.48;
GN Name=UCKL1; Synonyms=URKL1; ORFNames=F538;
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 3), INTERACTION WITH EBV EBNA3
RP (MICROBIAL INFECTION), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RC TISSUE=Heart;
RX PubMed=12199906; DOI=10.1186/1471-2121-3-23;
RA Kashuba E., Kashuba V., Sandalova T., Klein G., Szekely L.;
RT "Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human
RT uridine kinase/uracil phosphoribosyltransferase.";
RL BMC Cell Biol. 3:23-23(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP INTERACTION WITH RNF19B, AND UBIQUITINATION.
RX PubMed=16709802; DOI=10.4049/jimmunol.176.11.6454;
RA Fortier J.M., Kornbluth J.;
RT "NK lytic-associated molecule, involved in NK cytotoxic function, is an E3
RT ligase.";
RL J. Immunol. 176:6454-6463(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-56, 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).
CC -!- FUNCTION: May contribute to UTP accumulation needed for blast
CC transformation and proliferation. {ECO:0000269|PubMed:12199906}.
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 -!- 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 -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1.
CC -!- SUBUNIT: Interacts with RNF19B. {ECO:0000269|PubMed:16709802}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus/EBV
CC EBNA3. {ECO:0000269|PubMed:12199906}.
CC -!- INTERACTION:
CC Q9NWZ5; Q6ZMZ0: RNF19B; NbExp=4; IntAct=EBI-2466660, EBI-2466594;
CC Q9NWZ5; P12977: EBNA3; Xeno; NbExp=4; IntAct=EBI-2466660, EBI-993115;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12199906}. Nucleus
CC {ECO:0000269|PubMed:12199906}. Note=EBNA3 induces isoform 1
CC translocation to the nucleus, whereas it does change isoform 3
CC location.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NWZ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NWZ5-2; Sequence=VSP_021802;
CC Name=3;
CC IsoId=Q9NWZ5-3; Sequence=VSP_025641, VSP_025642;
CC Name=4;
CC IsoId=Q9NWZ5-4; Sequence=VSP_043171;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12199906}.
CC -!- PTM: Ubiquitinated by RNF19B; which induces proteasomal degradation.
CC {ECO:0000269|PubMed:16709802}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
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DR EMBL; AJ605558; CAE54074.1; -; mRNA.
DR EMBL; AK000524; BAA91230.1; -; mRNA.
DR EMBL; AK303688; BAH14018.1; -; mRNA.
DR EMBL; AK223220; BAD96940.1; -; mRNA.
DR EMBL; AL118506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033078; AAH33078.1; -; mRNA.
DR CCDS; CCDS13547.1; -. [Q9NWZ5-1]
DR CCDS; CCDS54479.1; -. [Q9NWZ5-4]
DR RefSeq; NP_001180308.1; NM_001193379.1. [Q9NWZ5-4]
DR RefSeq; NP_060329.2; NM_017859.3. [Q9NWZ5-1]
DR AlphaFoldDB; Q9NWZ5; -.
DR SMR; Q9NWZ5; -.
DR BioGRID; 120301; 84.
DR IntAct; Q9NWZ5; 17.
DR MINT; Q9NWZ5; -.
DR STRING; 9606.ENSP00000346155; -.
DR DrugBank; DB01632; 5-O-phosphono-alpha-D-ribofuranosyl diphosphate.
DR DrugBank; DB04137; Guanosine-5'-Triphosphate.
DR DrugBank; DB03419; Uracil.
DR DrugBank; DB03685; Uridine monophosphate.
DR GlyGen; Q9NWZ5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NWZ5; -.
DR PhosphoSitePlus; Q9NWZ5; -.
DR BioMuta; UCKL1; -.
DR DMDM; 84029407; -.
DR EPD; Q9NWZ5; -.
DR jPOST; Q9NWZ5; -.
DR MassIVE; Q9NWZ5; -.
DR MaxQB; Q9NWZ5; -.
DR PaxDb; Q9NWZ5; -.
DR PeptideAtlas; Q9NWZ5; -.
DR PRIDE; Q9NWZ5; -.
DR ProteomicsDB; 83002; -. [Q9NWZ5-1]
DR ProteomicsDB; 83003; -. [Q9NWZ5-2]
DR ProteomicsDB; 83004; -. [Q9NWZ5-3]
DR ProteomicsDB; 83005; -. [Q9NWZ5-4]
DR Antibodypedia; 1482; 141 antibodies from 27 providers.
DR DNASU; 54963; -.
DR Ensembl; ENST00000354216.11; ENSP00000346155.6; ENSG00000198276.16. [Q9NWZ5-1]
DR Ensembl; ENST00000358711.7; ENSP00000351546.3; ENSG00000198276.16. [Q9NWZ5-2]
DR Ensembl; ENST00000369908.9; ENSP00000358924.5; ENSG00000198276.16. [Q9NWZ5-4]
DR GeneID; 54963; -.
DR KEGG; hsa:54963; -.
DR MANE-Select; ENST00000354216.11; ENSP00000346155.6; NM_017859.4; NP_060329.2.
DR UCSC; uc010gkn.4; human. [Q9NWZ5-1]
DR CTD; 54963; -.
DR DisGeNET; 54963; -.
DR GeneCards; UCKL1; -.
DR HGNC; HGNC:15938; UCKL1.
DR HPA; ENSG00000198276; Low tissue specificity.
DR MIM; 610866; gene.
DR neXtProt; NX_Q9NWZ5; -.
DR OpenTargets; ENSG00000198276; -.
DR PharmGKB; PA38058; -.
DR VEuPathDB; HostDB:ENSG00000198276; -.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT01020000230412; -.
DR HOGENOM; CLU_021278_0_1_1; -.
DR InParanoid; Q9NWZ5; -.
DR OMA; RTKTMYG; -.
DR OrthoDB; 929897at2759; -.
DR PhylomeDB; Q9NWZ5; -.
DR TreeFam; TF105902; -.
DR BRENDA; 2.7.1.48; 2681.
DR PathwayCommons; Q9NWZ5; -.
DR Reactome; R-HSA-73614; Pyrimidine salvage.
DR SignaLink; Q9NWZ5; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR BioGRID-ORCS; 54963; 16 hits in 1086 CRISPR screens.
DR ChiTaRS; UCKL1; human.
DR GeneWiki; UCKL1; -.
DR GenomeRNAi; 54963; -.
DR Pharos; Q9NWZ5; Tbio.
DR PRO; PR:Q9NWZ5; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NWZ5; protein.
DR Bgee; ENSG00000198276; Expressed in right hemisphere of cerebellum and 190 other tissues.
DR ExpressionAtlas; Q9NWZ5; baseline and differential.
DR Genevisible; Q9NWZ5; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004849; F:uridine kinase activity; TAS:Reactome.
DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0043097; P:pyrimidine nucleoside salvage; TAS:Reactome.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd06223; PRTases_typeI; 1.
DR CDD; cd02023; UMPK; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR029933; UCKL1.
DR InterPro; IPR000764; Uridine_kinase-like.
DR PANTHER; PTHR10285:SF68; PTHR10285:SF68; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Host-virus interaction;
KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation.
FT CHAIN 1..548
FT /note="Uridine-cytidine kinase-like 1"
FT /id="PRO_0000164460"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YL3"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..38
FT /note="MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDR -> MSSPPAYPGI
FT RISGCRALGAEGS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043171"
FT VAR_SEQ 303..548
FT /note="RELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYS
FT KRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAV
FT CKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDH
FT DVPEDKIFLLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFG
FT TDAVPDGSDEEEVAYTG -> GCAGLGTPVPPAAPDAERPEEHAAGTGHAHHHQVRAHL
FT GTGRPRARAPAQLLAPQGQGDQSRRVHLLLQETDAAAHRARALLPALSGLRRTDPAGAG
FT LCGQVLCGEADHRCVHSARR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021802"
FT VAR_SEQ 386..395
FT /note="GKCYAGKQIT -> DHRCVHSARR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12199906"
FT /id="VSP_025641"
FT VAR_SEQ 396..548
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12199906"
FT /id="VSP_025642"
FT CONFLICT 290
FT /note="D -> N (in Ref. 1; CAE54074 and 2; BAA91230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 61141 MW; 0CD0351A802FE199 CRC64;
MAAPPARADA DPSPTSPPTA RDTPGRQAEK SETACEDRSN AESLDRLLPP VGTGRSPRKR
TTSQCKSEPP LLRTSKRTIY TAGRPPWYNE HGTQSKEAFA IGLGGGSASG KTTVARMIIE
ALDVPWVVLL SMDSFYKVLT EQQQEQAAHN NFNFDHPDAF DFDLIISTLK KLKQGKSVKV
PIYDFTTHSR KKDWKTLYGA NVIIFEGIMA FADKTLLELL DMKIFVDTDS DIRLVRRLRR
DISERGRDIE GVIKQYNKFV KPSFDQYIQP TMRLADIVVP RGSGNTVAID LIVQHVHSQL
EERELSVRAA LASAHQCHPL PRTLSVLKST PQVRGMHTII RDKETSRDEF IFYSKRLMRL
LIEHALSFLP FQDCVVQTPQ GQDYAGKCYA GKQITGVSIL RAGETMEPAL RAVCKDVRIG
TILIQTNQLT GEPELHYLRL PKDISDDHVI LMDCTVSTGA AAMMAVRVLL DHDVPEDKIF
LLSLLMAEMG VHSVAYAFPR VRIITTAVDK RVNDLFRIIP GIGNFGDRYF GTDAVPDGSD
EEEVAYTG
