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   24-JAN-2024, entry version 181.
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   -!- 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="https://atlasgeneticsoncology.org/gene/40340/DMTF1";
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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.
DR   RefSeq; XP_011515039.1; XM_011516737.1. [Q9Y222-1]
DR   RefSeq; XP_016868354.1; XM_017012865.1.
DR   PDB; 2LLK; NMR; -; A=220-274.
DR   PDBsum; 2LLK; -.
DR   AlphaFoldDB; Q9Y222; -.
DR   SMR; Q9Y222; -.
DR   BioGRID; 115309; 6.
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; 9606-ENSP00000378193; -.
DR   PeptideAtlas; 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; 275 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   AGR; HGNC:14603; -.
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; HESQKNT; -.
DR   OrthoDB; 4837009at2759; -.
DR   PhylomeDB; Q9Y222; -.
DR   TreeFam; TF333537; -.
DR   PathwayCommons; Q9Y222; -.
DR   SignaLink; Q9Y222; -.
DR   SIGNOR; Q9Y222; -.
DR   BioGRID-ORCS; 9988; 18 hits in 1180 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 206 other cell types or tissues.
DR   ExpressionAtlas; Q9Y222; baseline and differential.
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:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00167; SANT; 3.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   InterPro; IPR046775; DMTF1_N.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   PANTHER; PTHR46380; CYCLIN-D-BINDING MYB-LIKE TRANSCRIPTION FACTOR 1; 1.
DR   PANTHER; PTHR46380:SF2; CYCLIN-D-BINDING MYB-LIKE TRANSCRIPTION FACTOR 1; 1.
DR   Pfam; PF20588; DMTF1_N; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 2.
DR   SMART; SM00717; SANT; 3.
DR   SUPFAM; SSF46689; Homeodomain-like; 3.
DR   PROSITE; PS51294; HTH_MYB; 1.
DR   PROSITE; PS50090; MYB_LIKE; 2.
DR   Genevisible; Q9Y222; HS.
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
//