DMTF1_HUMAN
ID DMTF1_HUMAN Reviewed; 760 AA.
AC Q9Y222; B2RBE1; B4DJS5; Q05C48; Q59G79; Q6IS13; Q969T2; Q9H2Z2; Q9H2Z3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Cyclin-D-binding Myb-like transcription factor 1;
DE Short=hDMTF1;
DE AltName: Full=Cyclin-D-interacting Myb-like protein 1;
DE Short=hDMP1;
GN Name=DMTF1; Synonyms=DMP1;
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), AND TISSUE SPECIFICITY.
RX PubMed=10095122; DOI=10.1016/s0378-1119(98)00591-5;
RA Bodner S.M., Naeve C.W., Rakestraw K.M., Jones B.G., Valentine V.A.,
RA Valentine M.B., Luthardt F.W., Willman C.L., Raimondi S.C., Downing J.R.,
RA Roussel M.F., Sherr C.J., Look A.T.;
RT "Cloning and chromosomal localization of the gene encoding human cyclin D-
RT binding Myb-like protein (hDMP1).";
RL Gene 229:223-228(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Chronic myeloid leukemia cell;
RX PubMed=12917399; DOI=10.1074/jbc.m307067200;
RA Tschan M.P., Fischer K.M., Fung V.S., Pirnia F., Borner M.M., Fey M.F.,
RA Tobler A., Torbett B.E.;
RT "Alternative splicing of the human cyclin D-binding Myb-like protein
RT (hDMP1) yields a truncated protein isoform that alters macrophage
RT differentiation patterns.";
RL J. Biol. Chem. 278:42750-42760(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 5).
RC TISSUE=Cerebellum, Placenta, and Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(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 1).
RC TISSUE=Muscle, 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 [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17936562; DOI=10.1016/j.ccr.2007.08.034;
RA Mallakin A., Sugiyama T., Taneja P., Matise L.A., Frazier D.P.,
RA Choudhary M., Hawkins G.A., D'Agostino R.B. Jr., Willingham M.C., Inoue K.;
RT "Mutually exclusive inactivation of DMP1 and ARF/p53 in lung cancer.";
RL Cancer Cell 12:381-394(2007).
CC -!- FUNCTION: Transcriptional activator which activates the CDKN2A/ARF
CC locus in response to Ras-Raf signaling, thereby promoting p53/TP53-
CC dependent growth arrest (By similarity). Binds to the consensus
CC sequence 5'-CCCG[GT]ATGT-3' (By similarity). Isoform 1 may cooperate
CC with MYB to activate transcription of the ANPEP gene. Isoform 2 may
CC antagonize transcriptional activation by isoform 1. {ECO:0000250,
CC ECO:0000269|PubMed:12917399}.
CC -!- SUBUNIT: Interacts with the D-type cyclins CCND1, CCND2 and CCND3.
CC Interaction with D-type cyclins may modulate transcriptional activation
CC by this protein. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y222; O00629: KPNA4; NbExp=3; IntAct=EBI-2814971, EBI-396343;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:17936562}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q9Y222-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q9Y222-2; Sequence=VSP_032091, VSP_032092;
CC Name=3; Synonyms=Gamma;
CC IsoId=Q9Y222-3; Sequence=VSP_032090, VSP_032093;
CC Name=4;
CC IsoId=Q9Y222-4; Sequence=VSP_032089, VSP_032090, VSP_032093;
CC Name=5;
CC IsoId=Q9Y222-5; Sequence=VSP_041063;
CC -!- TISSUE SPECIFICITY: Expressed at relatively low levels in colonic
CC mucosa, ovary, peripheral leukocytes, prostate and small intestine, and
CC at higher levels in spleen, testis and thymus. Expressed in multiple
CC regions of the brain and CNS including amygdala, caudate, corpus
CC callosum, hippocampus, substantia nigra and subthalamic nucleus.
CC Isoform 1 is the predominant isoform in monocytes, macrophages and
CC neutrophils, isoform 2 is most strongly expressed in peripheral blood
CC leukocytes and quiescent CD34 positive cells, and isoform 3 is
CC expressed at low levels in all hematopoietic cell types. Expression is
CC frequently reduced in non-small-cell lung carcinomas (NSCLC) due to
CC hemizygous gene deletion, strongly suggesting that this locus is
CC haploinsufficient for tumor suppression. Loss of this locus frequently
CC occurs in tumors which retain wild-type CDKN2A/ARF and p53/TP53 loci.
CC Hemizygous gene deletion has also been observed in leukemic blasts from
CC patients with abnormalities of the long arm of chromosome 7.
CC {ECO:0000269|PubMed:10095122, ECO:0000269|PubMed:12917399,
CC ECO:0000269|PubMed:17936562}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 expression is down-regulated during
CC myeloid differentiation, while the expression of isoform 1 and isoform
CC 3 remain constant.
CC -!- PTM: Phosphorylated by the cyclin-D2/CDK4, cyclin-D3/CDK4 and cyclin-
CC D2/CDK6 complexes and to a lesser extent by the cyclin-D1/CDK4 complex.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DMTF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92467.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DMTF1ID40340ch7q21.html";
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DR EMBL; AF084530; AAC33480.1; -; mRNA.
DR EMBL; AF202144; AAG35613.1; -; mRNA.
DR EMBL; AF202145; AAG35614.1; -; mRNA.
DR EMBL; AK296211; BAG58937.1; -; mRNA.
DR EMBL; AK126664; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK314622; BAG37188.1; -; mRNA.
DR EMBL; AB209230; BAD92467.1; ALT_SEQ; mRNA.
DR EMBL; AC005076; AAD43181.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76963.1; -; Genomic_DNA.
DR EMBL; BC007418; AAH07418.2; -; mRNA.
DR EMBL; BC007447; AAH07447.2; -; mRNA.
DR EMBL; BC029370; AAH29370.1; ALT_TERM; mRNA.
DR EMBL; BC070064; AAH70064.1; -; mRNA.
DR CCDS; CCDS47633.1; -. [Q9Y222-5]
DR CCDS; CCDS5601.1; -. [Q9Y222-1]
DR RefSeq; NP_001135798.1; NM_001142326.1. [Q9Y222-5]
DR RefSeq; NP_001135799.1; NM_001142327.1. [Q9Y222-1]
DR RefSeq; NP_066968.3; NM_021145.3. [Q9Y222-1]
DR RefSeq; XP_011515037.1; XM_011516735.2. [Q9Y222-1]
DR RefSeq; XP_011515039.1; XM_011516737.1. [Q9Y222-1]
DR RefSeq; XP_016868354.1; XM_017012865.1. [Q9Y222-1]
DR PDB; 2LLK; NMR; -; A=220-274.
DR PDBsum; 2LLK; -.
DR AlphaFoldDB; Q9Y222; -.
DR SMR; Q9Y222; -.
DR BioGRID; 115309; 5.
DR IntAct; Q9Y222; 5.
DR MINT; Q9Y222; -.
DR STRING; 9606.ENSP00000378193; -.
DR iPTMnet; Q9Y222; -.
DR PhosphoSitePlus; Q9Y222; -.
DR BioMuta; DMTF1; -.
DR DMDM; 74762040; -.
DR EPD; Q9Y222; -.
DR jPOST; Q9Y222; -.
DR MassIVE; Q9Y222; -.
DR MaxQB; Q9Y222; -.
DR PaxDb; Q9Y222; -.
DR PeptideAtlas; Q9Y222; -.
DR PRIDE; Q9Y222; -.
DR ProteomicsDB; 85599; -. [Q9Y222-1]
DR ProteomicsDB; 85600; -. [Q9Y222-2]
DR ProteomicsDB; 85601; -. [Q9Y222-3]
DR ProteomicsDB; 85602; -. [Q9Y222-4]
DR ProteomicsDB; 85603; -. [Q9Y222-5]
DR Antibodypedia; 15263; 255 antibodies from 26 providers.
DR DNASU; 9988; -.
DR Ensembl; ENST00000331242.12; ENSP00000332171.7; ENSG00000135164.19. [Q9Y222-1]
DR Ensembl; ENST00000394703.9; ENSP00000378193.5; ENSG00000135164.19. [Q9Y222-1]
DR Ensembl; ENST00000412139.6; ENSP00000407941.2; ENSG00000135164.19. [Q9Y222-2]
DR Ensembl; ENST00000425406.5; ENSP00000411908.1; ENSG00000135164.19. [Q9Y222-4]
DR Ensembl; ENST00000432937.6; ENSP00000412532.2; ENSG00000135164.19. [Q9Y222-5]
DR Ensembl; ENST00000447863.5; ENSP00000389774.1; ENSG00000135164.19. [Q9Y222-3]
DR Ensembl; ENST00000579677.5; ENSP00000464596.1; ENSG00000135164.19. [Q9Y222-2]
DR Ensembl; ENST00000584619.5; ENSP00000464092.1; ENSG00000135164.19. [Q9Y222-2]
DR GeneID; 9988; -.
DR KEGG; hsa:9988; -.
DR MANE-Select; ENST00000331242.12; ENSP00000332171.7; NM_001142327.2; NP_001135799.1.
DR UCSC; uc003uih.3; human. [Q9Y222-1]
DR CTD; 9988; -.
DR DisGeNET; 9988; -.
DR GeneCards; DMTF1; -.
DR HGNC; HGNC:14603; DMTF1.
DR HPA; ENSG00000135164; Low tissue specificity.
DR MIM; 608491; gene.
DR neXtProt; NX_Q9Y222; -.
DR OpenTargets; ENSG00000135164; -.
DR PharmGKB; PA27389; -.
DR VEuPathDB; HostDB:ENSG00000135164; -.
DR eggNOG; KOG0051; Eukaryota.
DR GeneTree; ENSGT00940000156016; -.
DR HOGENOM; CLU_089341_0_0_1; -.
DR InParanoid; Q9Y222; -.
DR OMA; WEDLAWG; -.
DR OrthoDB; 1474117at2759; -.
DR PhylomeDB; Q9Y222; -.
DR TreeFam; TF333537; -.
DR PathwayCommons; Q9Y222; -.
DR SignaLink; Q9Y222; -.
DR SIGNOR; Q9Y222; -.
DR BioGRID-ORCS; 9988; 18 hits in 1100 CRISPR screens.
DR ChiTaRS; DMTF1; human.
DR GeneWiki; DMTF1; -.
DR GenomeRNAi; 9988; -.
DR Pharos; Q9Y222; Tbio.
DR PRO; PR:Q9Y222; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y222; protein.
DR Bgee; ENSG00000135164; Expressed in right lobe of thyroid gland and 204 other tissues.
DR ExpressionAtlas; Q9Y222; baseline and differential.
DR Genevisible; Q9Y222; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd00167; SANT; 3.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF00249; Myb_DNA-binding; 2.
DR SMART; SM00717; SANT; 3.
DR SUPFAM; SSF46689; SSF46689; 3.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cell cycle; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Tumor suppressor.
FT CHAIN 1..760
FT /note="Cyclin-D-binding Myb-like transcription factor 1"
FT /id="PRO_0000323729"
FT DOMAIN 225..263
FT /note="Myb-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DOMAIN 268..333
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 339..388
FT /note="Myb-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DNA_BIND 306..329
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..237
FT /note="Interaction with CCND2"
FT /evidence="ECO:0000250"
FT REGION 87..458
FT /note="Required for DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 87..170
FT /note="Required for transcriptional activation"
FT /evidence="ECO:0000250"
FT REGION 176..760
FT /note="Interaction with CCND1, CCND2 and CCND3"
FT /evidence="ECO:0000250"
FT REGION 414..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..760
FT /note="Required for transcriptional activation"
FT /evidence="ECO:0000250"
FT REGION 738..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..88
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041063"
FT VAR_SEQ 37..78
FT /note="EADEIDSEDSIEPPHKRLCLSSEDDQSIDDSTPCISVVALPL -> V (in
FT isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_032089"
FT VAR_SEQ 238..285
FT /note="LRIKHGNDWATIGAALGRSASSVKDRCRLMKDTCNTGKWTEEEEKRLA ->
FT KKAIAACFFFTHRQLWTPKKGHTFKLWLSKYCCPQLPNQSNGKKKNEE (in
FT isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12917399, ECO:0000303|Ref.4"
FT /id="VSP_032090"
FT VAR_SEQ 238..273
FT /note="LRIKHGNDWATIGAALGRSASSVKDRCRLMKDTCNT -> QLWTPKKGHTFK
FT LWLSKYCCPQLPNQSNGKKKNEE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12917399,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_032091"
FT VAR_SEQ 274..760
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12917399,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_032092"
FT VAR_SEQ 286..760
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12917399, ECO:0000303|Ref.4"
FT /id="VSP_032093"
FT VARIANT 479
FT /note="V -> I (in dbSNP:rs1558049)"
FT /id="VAR_039577"
FT CONFLICT 345
FT /note="I -> T (in Ref. 3; BAG58937)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="I -> V (in Ref. 7; AAH70064)"
FT /evidence="ECO:0000305"
FT HELIX 229..242
FT /evidence="ECO:0007829|PDB:2LLK"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:2LLK"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:2LLK"
SQ SEQUENCE 760 AA; 84471 MW; 57B3AE332F21A333 CRC64;
MSTVEEDSDT VTVETVNSVT LTQDTEGNLI LHCPQNEADE IDSEDSIEPP HKRLCLSSED
DQSIDDSTPC ISVVALPLSE NDQSFEVTMT ATTEVADDEV TEGTVTQIQI LQNEQLDEIS
PLGNEEVSAV SQAWFTTKED KDSLTNKGHK WKQGMWSKEE IDILMNNIER YLKARGIKDA
TEIIFEMSKD ERKDFYRTIA WGLNRPLFAV YRRVLRMYDD RNHVGKYTPE EIEKLKELRI
KHGNDWATIG AALGRSASSV KDRCRLMKDT CNTGKWTEEE EKRLAEVVHE LTSTEPGDIV
TQGVSWAAVA ERVGTRSEKQ CRSKWLNYLN WKQSGGTEWT KEDEINLILR IAELDVADEN
DINWDLLAEG WSSVRSPQWL RSKWWTIKRQ IANHKDVSFP VLIKGLKQLH ENQKNNPTLL
ENKSGSGVPN SNTNSSVQHV QIRVARLEDN TAISSSPMAA LQIPVQITHV SSADSPATVD
SETITLNSGT LQTFEILPSF HLQPTGTPGT YLLQTSSSQG LPLTLTASPT VTLTAAAPAS
PEQIIVHALS PEHLLNTSDN VTVQCHTPRV IIQTVATEDI TSSISQAELT VDSDIQSSDF
PEPPDALEAD TFPDEIHHPK MTVEPSFNDA HVSKFSDQNS TELMNSVMVR TEEEISDTDL
KQEESPSDLA SAYVTEGLES PTIEEQVDQT IDDETILIVP SPHGFIQASD VIDTESVLPL
TTLTDPILQH HQEESNIIGS SLGSPVSEDS KDVEDLVNCH
