TPD53_HUMAN
ID TPD53_HUMAN Reviewed; 204 AA.
AC Q16890; A8K757; A8K772; A8MUD2; A8MUJ7; A8MW70; F6V707; O43397; Q5TC99;
AC Q5TDQ0; Q9BUQ6; Q9C054;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Tumor protein D53;
DE Short=hD53;
DE AltName: Full=Tumor protein D52-like 1;
GN Name=TPD52L1;
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).
RC TISSUE=Mammary carcinoma;
RX PubMed=8812487; DOI=10.1006/geno.1996.0393;
RA Byrne J.A., Mattei M.-G., Basset P.;
RT "Definition of the tumor protein D52 (TPD52) gene family through cloning of
RT D52 homologues in human (hD53) and mouse (mD52).";
RL Genomics 35:523-532(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), SELF-ASSOCIATION, AND INTERACTION
RP WITH TPD52 AND TPD52L2.
RX PubMed=9484778; DOI=10.1038/sj.onc.1201604;
RA Byrne J.A., Nourse C.R., Basset P., Gunning P.;
RT "Identification of homo- and heteromeric interactions between members of
RT the breast carcinoma-associated D52 protein family using the yeast two-
RT hybrid system.";
RL Oncogene 16:873-881(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Cho S., Kim J., Ryu S.E.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Skeletal muscle;
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, 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-149, 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 [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-86; SER-122; SER-131; SER-149
RP AND SER-174, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND THR-146, AND
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 [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-133, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- SUBUNIT: Forms a homodimer or heterodimer with other members of the
CC family.
CC -!- INTERACTION:
CC Q16890; P55327: TPD52; NbExp=3; IntAct=EBI-717470, EBI-782581;
CC Q16890; Q16890: TPD52L1; NbExp=4; IntAct=EBI-717470, EBI-717470;
CC Q16890; Q62393: Tpd52; Xeno; NbExp=3; IntAct=EBI-717470, EBI-782591;
CC Q16890-2; Q96AL5: PBX3; NbExp=3; IntAct=EBI-18777952, EBI-741171;
CC Q16890-2; P55327-2: TPD52; NbExp=3; IntAct=EBI-18777952, EBI-12124194;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q16890-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16890-2; Sequence=VSP_036754, VSP_036755;
CC Name=3;
CC IsoId=Q16890-3; Sequence=VSP_036752, VSP_036753;
CC Name=4; Synonyms=+5hD53;
CC IsoId=Q16890-4; Sequence=VSP_036751, VSP_036752, VSP_036753;
CC Name=5;
CC IsoId=Q16890-5; Sequence=VSP_036751;
CC -!- SIMILARITY: Belongs to the TPD52 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC98475.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U44427; AAB40894.1; -; mRNA.
DR EMBL; U44428; AAB40895.1; -; mRNA.
DR EMBL; AF004427; AAC98475.1; ALT_INIT; mRNA.
DR EMBL; AF208012; AAG49634.1; -; mRNA.
DR EMBL; AK291866; BAF84555.1; -; mRNA.
DR EMBL; AK291872; BAF84561.1; -; mRNA.
DR EMBL; AK291887; BAF84576.1; -; mRNA.
DR EMBL; AL121938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48142.1; -; Genomic_DNA.
DR EMBL; BC002375; AAH02375.1; -; mRNA.
DR CCDS; CCDS34527.1; -. [Q16890-2]
DR CCDS; CCDS34528.1; -. [Q16890-3]
DR CCDS; CCDS43502.1; -. [Q16890-5]
DR CCDS; CCDS5130.1; -. [Q16890-1]
DR CCDS; CCDS75514.1; -. [Q16890-4]
DR RefSeq; NP_001003395.1; NM_001003395.2. [Q16890-5]
DR RefSeq; NP_001003396.1; NM_001003396.2. [Q16890-2]
DR RefSeq; NP_001003397.1; NM_001003397.2. [Q16890-3]
DR RefSeq; NP_003278.1; NM_003287.3. [Q16890-1]
DR RefSeq; XP_005267179.1; XM_005267122.2. [Q16890-5]
DR RefSeq; XP_016866729.1; XM_017011240.1. [Q16890-4]
DR AlphaFoldDB; Q16890; -.
DR SMR; Q16890; -.
DR BioGRID; 113017; 34.
DR IntAct; Q16890; 17.
DR MINT; Q16890; -.
DR STRING; 9606.ENSP00000434142; -.
DR iPTMnet; Q16890; -.
DR PhosphoSitePlus; Q16890; -.
DR BioMuta; TPD52L1; -.
DR DMDM; 12585368; -.
DR EPD; Q16890; -.
DR jPOST; Q16890; -.
DR MassIVE; Q16890; -.
DR MaxQB; Q16890; -.
DR PaxDb; Q16890; -.
DR PeptideAtlas; Q16890; -.
DR PRIDE; Q16890; -.
DR ProteomicsDB; 28063; -.
DR ProteomicsDB; 61125; -. [Q16890-1]
DR ProteomicsDB; 61126; -. [Q16890-2]
DR ProteomicsDB; 61127; -. [Q16890-3]
DR ProteomicsDB; 61128; -. [Q16890-4]
DR TopDownProteomics; Q16890-3; -. [Q16890-3]
DR Antibodypedia; 32681; 257 antibodies from 35 providers.
DR DNASU; 7164; -.
DR Ensembl; ENST00000368388.6; ENSP00000357373.2; ENSG00000111907.21. [Q16890-3]
DR Ensembl; ENST00000368402.9; ENSP00000357387.5; ENSG00000111907.21. [Q16890-2]
DR Ensembl; ENST00000392482.6; ENSP00000376273.2; ENSG00000111907.21. [Q16890-4]
DR Ensembl; ENST00000524679.1; ENSP00000432787.1; ENSG00000111907.21. [Q16890-4]
DR Ensembl; ENST00000532429.5; ENSP00000435447.1; ENSG00000111907.21. [Q16890-5]
DR Ensembl; ENST00000534000.6; ENSP00000434142.1; ENSG00000111907.21. [Q16890-1]
DR Ensembl; ENST00000534199.5; ENSP00000432590.1; ENSG00000111907.21. [Q16890-4]
DR GeneID; 7164; -.
DR KEGG; hsa:7164; -.
DR MANE-Select; ENST00000534000.6; ENSP00000434142.1; NM_003287.4; NP_003278.1.
DR UCSC; uc003pzu.2; human. [Q16890-1]
DR CTD; 7164; -.
DR DisGeNET; 7164; -.
DR GeneCards; TPD52L1; -.
DR HGNC; HGNC:12006; TPD52L1.
DR HPA; ENSG00000111907; Tissue enhanced (adrenal gland, salivary gland).
DR MIM; 604069; gene.
DR neXtProt; NX_Q16890; -.
DR OpenTargets; ENSG00000111907; -.
DR PharmGKB; PA36687; -.
DR VEuPathDB; HostDB:ENSG00000111907; -.
DR eggNOG; KOG4010; Eukaryota.
DR GeneTree; ENSGT00940000159202; -.
DR HOGENOM; CLU_080743_0_0_1; -.
DR InParanoid; Q16890; -.
DR PhylomeDB; Q16890; -.
DR TreeFam; TF317562; -.
DR PathwayCommons; Q16890; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; Q16890; -.
DR BioGRID-ORCS; 7164; 11 hits in 1086 CRISPR screens.
DR ChiTaRS; TPD52L1; human.
DR GeneWiki; TPD52L1; -.
DR GenomeRNAi; 7164; -.
DR Pharos; Q16890; Tbio.
DR PRO; PR:Q16890; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q16890; protein.
DR Bgee; ENSG00000111907; Expressed in parotid gland and 194 other tissues.
DR ExpressionAtlas; Q16890; baseline and differential.
DR Genevisible; Q16890; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR InterPro; IPR007327; TPD52.
DR PANTHER; PTHR19307; PTHR19307; 1.
DR Pfam; PF04201; TPD52; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..204
FT /note="Tumor protein D53"
FT /id="PRO_0000185741"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..73
FT /evidence="ECO:0000255"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 133
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:9484778"
FT /id="VSP_036751"
FT VAR_SEQ 129..131
FT /note="SYS -> RRK (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9484778, ECO:0000303|Ref.3"
FT /id="VSP_036752"
FT VAR_SEQ 132..204
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9484778, ECO:0000303|Ref.3"
FT /id="VSP_036753"
FT VAR_SEQ 143..144
FT /note="NS -> RK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036754"
FT VAR_SEQ 145..204
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036755"
FT VARIANT 62
FT /note="R -> K (in dbSNP:rs6905231)"
FT /id="VAR_034568"
FT CONFLICT 74
FT /note="N -> T (in Ref. 4; BAF84576)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="G -> E (in Ref. 4; BAF84561)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 204 AA; 22449 MW; 6B3C336D5C0653C9 CRC64;
MEAQAQGLLE TEPLQGTDED AVASADFSSM LSEEEKEELK AELVQLEDEI TTLRQVLSAK
ERHLVEIKQK LGMNLMNELK QNFSKSWHDM QTTTAYKKTH ETLSHAGQKA TAAFSNVGTA
ISKKFGDMSY SIRHSISMPA MRNSPTFKSF EERVETTVTS LKTKVGGTNP NGGSFEEVLS
STAHASAQSL AGGSRRTKEE ELQC
