PDXD1_HUMAN
ID PDXD1_HUMAN Reviewed; 788 AA.
AC Q6P996; B4DR55; B4DSL3; E7EMH5; E7EPL4; H3BNZ1; O00236; Q4F6X7; Q6PID7;
AC Q86YF1; Q8N4Q9; Q8TBS5;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Pyridoxal-dependent decarboxylase domain-containing protein 1;
DE EC=4.1.1.-;
GN Name=PDXDC1; Synonyms=KIAA0251;
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] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP LEU-301.
RC TISSUE=Brain, and Teratocarcinoma;
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 GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Cervix, Lung, Placenta, and Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-371 (ISOFORM 1).
RA Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Wen S., Lin L., Yang S.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-691, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757, AND IDENTIFICATION BY
RP 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-652 AND SER-718, AND
RP IDENTIFICATION BY 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710, 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 THR-414; SER-710; SER-718;
RP SER-722; SER-779 AND SER-786, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-786, 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).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6P996-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P996-2; Sequence=VSP_027341, VSP_027342, VSP_027343;
CC Name=3;
CC IsoId=Q6P996-3; Sequence=VSP_055731, VSP_055733;
CC Name=4;
CC IsoId=Q6P996-4; Sequence=VSP_055732, VSP_055734;
CC Name=5;
CC IsoId=Q6P996-5; Sequence=VSP_055734;
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33748.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAZ14099.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA19780.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D87438; BAA19780.1; ALT_INIT; mRNA.
DR EMBL; AK299799; BAG61675.1; -; mRNA.
DR EMBL; AK299111; BAG61167.1; -; mRNA.
DR EMBL; AC138932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025366; AAH25366.2; -; mRNA.
DR EMBL; BC033748; AAH33748.1; ALT_FRAME; mRNA.
DR EMBL; BC036520; AAH36520.1; -; mRNA.
DR EMBL; BC042104; AAH42104.2; -; mRNA.
DR EMBL; BC060871; AAH60871.1; -; mRNA.
DR EMBL; DQ111782; AAZ14099.1; ALT_FRAME; mRNA.
DR CCDS; CCDS32393.1; -. [Q6P996-1]
DR CCDS; CCDS66954.1; -. [Q6P996-5]
DR CCDS; CCDS66955.1; -. [Q6P996-4]
DR CCDS; CCDS66957.1; -. [Q6P996-3]
DR CCDS; CCDS73831.1; -. [Q6P996-2]
DR RefSeq; NP_001272373.1; NM_001285444.1. [Q6P996-5]
DR RefSeq; NP_001272374.1; NM_001285445.1. [Q6P996-4]
DR RefSeq; NP_001272376.1; NM_001285447.1.
DR RefSeq; NP_001272377.1; NM_001285448.1. [Q6P996-3]
DR RefSeq; NP_001272379.1; NM_001285450.1. [Q6P996-2]
DR RefSeq; NP_055842.2; NM_015027.3. [Q6P996-1]
DR RefSeq; XP_006725288.1; XM_006725225.1.
DR RefSeq; XP_006725291.1; XM_006725228.2.
DR RefSeq; XP_006726660.1; XM_006726597.1.
DR RefSeq; XP_006726663.1; XM_006726600.2.
DR AlphaFoldDB; Q6P996; -.
DR SMR; Q6P996; -.
DR BioGRID; 116681; 204.
DR IntAct; Q6P996; 46.
DR MINT; Q6P996; -.
DR STRING; 9606.ENSP00000379691; -.
DR GlyGen; Q6P996; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q6P996; -.
DR MetOSite; Q6P996; -.
DR PhosphoSitePlus; Q6P996; -.
DR BioMuta; PDXDC1; -.
DR DMDM; 156633546; -.
DR EPD; Q6P996; -.
DR jPOST; Q6P996; -.
DR MassIVE; Q6P996; -.
DR MaxQB; Q6P996; -.
DR PaxDb; Q6P996; -.
DR PeptideAtlas; Q6P996; -.
DR PRIDE; Q6P996; -.
DR ProteomicsDB; 16941; -.
DR ProteomicsDB; 17384; -.
DR ProteomicsDB; 41339; -.
DR ProteomicsDB; 67028; -. [Q6P996-1]
DR ProteomicsDB; 67029; -. [Q6P996-2]
DR Antibodypedia; 24937; 213 antibodies from 26 providers.
DR DNASU; 23042; -.
DR Ensembl; ENST00000396410.9; ENSP00000379691.4; ENSG00000179889.20. [Q6P996-1]
DR Ensembl; ENST00000450288.3; ENSP00000391147.3; ENSG00000179889.20. [Q6P996-3]
DR Ensembl; ENST00000455313.6; ENSP00000406703.2; ENSG00000179889.20. [Q6P996-2]
DR Ensembl; ENST00000569715.5; ENSP00000455070.1; ENSG00000179889.20. [Q6P996-5]
DR Ensembl; ENST00000613798.4; ENSP00000481784.1; ENSG00000275498.5. [Q6P996-2]
DR Ensembl; ENST00000614833.4; ENSP00000480418.1; ENSG00000275498.5. [Q6P996-3]
DR Ensembl; ENST00000618389.4; ENSP00000484595.1; ENSG00000275498.5. [Q6P996-1]
DR Ensembl; ENST00000619589.4; ENSP00000478686.1; ENSG00000275498.5. [Q6P996-5]
DR Ensembl; ENST00000627450.2; ENSP00000486662.1; ENSG00000179889.20. [Q6P996-4]
DR Ensembl; ENST00000631842.1; ENSP00000488664.1; ENSG00000275498.5. [Q6P996-4]
DR GeneID; 23042; -.
DR KEGG; hsa:23042; -.
DR MANE-Select; ENST00000396410.9; ENSP00000379691.4; NM_015027.4; NP_055842.2.
DR UCSC; uc002dcz.5; human. [Q6P996-1]
DR CTD; 23042; -.
DR DisGeNET; 23042; -.
DR GeneCards; PDXDC1; -.
DR HGNC; HGNC:28995; PDXDC1.
DR HPA; ENSG00000179889; Low tissue specificity.
DR MIM; 614244; gene.
DR neXtProt; NX_Q6P996; -.
DR OpenTargets; ENSG00000179889; -.
DR PharmGKB; PA162399182; -.
DR VEuPathDB; HostDB:ENSG00000179889; -.
DR eggNOG; KOG0630; Eukaryota.
DR GeneTree; ENSGT00390000009628; -.
DR HOGENOM; CLU_014327_0_0_1; -.
DR InParanoid; Q6P996; -.
DR OMA; RYCPLEL; -.
DR OrthoDB; 804210at2759; -.
DR PhylomeDB; Q6P996; -.
DR TreeFam; TF313101; -.
DR PathwayCommons; Q6P996; -.
DR SignaLink; Q6P996; -.
DR SIGNOR; Q6P996; -.
DR BioGRID-ORCS; 102724985; 1 hit in 3 CRISPR screens.
DR BioGRID-ORCS; 23042; 18 hits in 1077 CRISPR screens.
DR ChiTaRS; PDXDC1; human.
DR Pharos; Q6P996; Tbio.
DR PRO; PR:Q6P996; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6P996; protein.
DR Bgee; ENSG00000179889; Expressed in rectum and 114 other tissues.
DR ExpressionAtlas; Q6P996; baseline and differential.
DR Genevisible; Q6P996; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Decarboxylase; Lyase; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..788
FT /note="Pyridoxal-dependent decarboxylase domain-containing
FT protein 1"
FT /id="PRO_0000297677"
FT REGION 28..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 414
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 687
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99K01"
FT MOD_RES 691
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99K01"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055731"
FT VAR_SEQ 32
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055732"
FT VAR_SEQ 54..129
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055733"
FT VAR_SEQ 54..80
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055734"
FT VAR_SEQ 194..216
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027341"
FT VAR_SEQ 432..452
FT /note="LGEQLKQLVPASGLTVMDLEA -> VRMAVTPLSFQVPVHHHPTCW (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027342"
FT VAR_SEQ 453..788
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027343"
FT VARIANT 301
FT /note="P -> L (in dbSNP:rs4985162)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_059252"
FT CONFLICT 37
FT /note="E -> G (in Ref. 2; BAG61167)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="G -> V (in Ref. 5; AAZ14099)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="I -> M (in Ref. 2; BAG61167 and 5; AAZ14099)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="T -> A (in Ref. 5; AAZ14099)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="L -> F (in Ref. 5; AAZ14099)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="K -> E (in Ref. 4; AAH60871)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="T -> A (in Ref. 2; BAG61675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 788 AA; 86707 MW; 2BAFEDC0A1C13AD3 CRC64;
MDASLEKIAD PTLAEMGKNL KEAVKMLEDS QRRTEEENGK KLISGDIPGP LQGSGQDMVS
ILQLVQNLMH GDEDEEPQSP RIQNIGEQGH MALLGHSLGA YISTLDKEKL RKLTTRILSD
TTLWLCRIFR YENGCAYFHE EEREGLAKIC RLAIHSRYED FVVDGFNVLY NKKPVIYLSA
AARPGLGQYL CNQLGLPFPC LCRVPCNTVF GSQHQMDVAF LEKLIKDDIE RGRLPLLLVA
NAGTAAVGHT DKIGRLKELC EQYGIWLHVE GVNLATLALG YVSSSVLAAA KCDSMTMTPG
PWLGLPAVPA VTLYKHDDPA LTLVAGLTSN KPTDKLRALP LWLSLQYLGL DGFVERIKHA
CQLSQRLQES LKKVNYIKIL VEDELSSPVV VFRFFQELPG SDPVFKAVPV PNMTPSGVGR
ERHSCDALNR WLGEQLKQLV PASGLTVMDL EAEGTCLRFS PLMTAAVLGT RGEDVDQLVA
CIESKLPVLC CTLQLREEFK QEVEATAGLL YVDDPNWSGI GVVRYEHAND DKSSLKSDPE
GENIHAGLLK KLNELESDLT FKIGPEYKSM KSCLYVGMAS DNVDAAELVE TIAATAREIE
ENSRLLENMT EVVRKGIQEA QVELQKASEE RLLEEGVLRQ IPVVGSVLNW FSPVQALQKG
RTFNLTAGSL ESTEPIYVYK AQGAGVTLPP TPSGSRTKQR LPGQKPFKRS LRGSDALSET
SSVSHIEDLE KVERLSSGPE QITLEASSTE GHPGAPSPQH TDQTEAFQKG VPHPEDDHSQ
VEGPESLR
