KLF12_HUMAN
ID KLF12_HUMAN Reviewed; 402 AA.
AC Q9Y4X4; A8K5T2; L0R3J4; Q5VZM7; Q9UHZ0;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Krueppel-like factor 12;
DE AltName: Full=Transcriptional repressor AP-2rep;
GN Name=KLF12; Synonyms=AP2REP; ORFNames=HSPC122;
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).
RX PubMed=10704285; DOI=10.1006/geno.1999.6084;
RA Roth C., Schuierer M., Gunther K., Buettner R.;
RT "Genomic structure and DNA binding properties of the human zinc finger
RT transcriptional repressor AP-2rep (KLF12).";
RL Genomics 63:384-390(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11433524; DOI=10.1002/gcc.1152;
RA Chen C., Brabham W.W., Stultz B.G., Frierson H.F. Jr., Barrett J.C.,
RA Sawyers C.L., Isaacs J.T., Dong J.T.;
RT "Defining a common region of deletion at 13q21 in human cancers.";
RL Genes Chromosomes Cancer 31:333-344(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
RX PubMed=23134681; DOI=10.1096/fj.12-220319;
RA Camacho-Vanegas O., Till J., Miranda-Lorenzo I., Ozturk B., Camacho S.C.,
RA Martignetti J.A.;
RT "Shaking the family tree: Identification of novel and biologically active
RT alternatively spliced isoforms across the KLF family of transcription
RT factors.";
RL FASEB J. 27:432-436(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Hypothalamus;
RA Jiang C., Peng Y., Gu J., Gu Y., Fu S., Wu T., Dong H., Jin W., Fu G.,
RA Han Z., Chen Z., Wang Y.;
RT "A novel gene expressed in the human hypothalamus.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [10]
RP METHYLATION AT LYS-313.
RX PubMed=18438403; DOI=10.1038/nchembio.88;
RA Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R., Jurkowska R.,
RA Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.;
RT "Protein lysine methyltransferase G9a acts on non-histone targets.";
RL Nat. Chem. Biol. 4:344-346(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, 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 [12]
RP IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [14]
RP INACTIVATION OF 9AATAD MOTIF.
RX PubMed=31375868; DOI=10.1007/s00018-019-03251-w;
RA Piskacek M., Havelka M., Jendruchova K., Knight A., Keegan L.P.;
RT "The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with
RT valines and intron reservoirs.";
RL Cell. Mol. Life Sci. 77:1793-1810(2020).
CC -!- FUNCTION: Confers strong transcriptional repression to the AP-2-alpha
CC gene. Binds to a regulatory element (A32) in the AP-2-alpha gene
CC promoter.
CC -!- INTERACTION:
CC Q9Y4X4; Q13363-2: CTBP1; NbExp=6; IntAct=EBI-750750, EBI-10171858;
CC Q9Y4X4; Q96KQ7: EHMT2; NbExp=5; IntAct=EBI-750750, EBI-744366;
CC Q9Y4X4; Q14192: FHL2; NbExp=3; IntAct=EBI-750750, EBI-701903;
CC Q9Y4X4; Q13643: FHL3; NbExp=3; IntAct=EBI-750750, EBI-741101;
CC Q9Y4X4; P42858: HTT; NbExp=3; IntAct=EBI-750750, EBI-466029;
CC Q9Y4X4; Q92993: KAT5; NbExp=3; IntAct=EBI-750750, EBI-399080;
CC Q9Y4X4; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-750750, EBI-11742507;
CC Q9Y4X4; D3DTS7: PMP22; NbExp=3; IntAct=EBI-750750, EBI-25882629;
CC Q9Y4X4; P23284: PPIB; NbExp=3; IntAct=EBI-750750, EBI-359252;
CC Q9Y4X4; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-750750, EBI-9090795;
CC Q9Y4X4; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-750750, EBI-741515;
CC Q9Y4X4; P61981: YWHAG; NbExp=3; IntAct=EBI-750750, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y4X4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4X4-2; Sequence=VSP_006876;
CC Name=3;
CC IsoId=Q9Y4X4-3; Sequence=VSP_047486, VSP_047487;
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors. In KLF12, the motif
CC is inactive. {ECO:0000269|PubMed:31375868}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AJ243274; CAB46982.1; -; mRNA.
DR EMBL; AF312872; AAK12082.1; -; Genomic_DNA.
DR EMBL; AF312866; AAK12082.1; JOINED; Genomic_DNA.
DR EMBL; AF312867; AAK12082.1; JOINED; Genomic_DNA.
DR EMBL; AF312868; AAK12082.1; JOINED; Genomic_DNA.
DR EMBL; AF312869; AAK12082.1; JOINED; Genomic_DNA.
DR EMBL; AF312870; AAK12082.1; JOINED; Genomic_DNA.
DR EMBL; AF312871; AAK12082.1; JOINED; Genomic_DNA.
DR EMBL; HF546212; CCO02798.1; -; mRNA.
DR EMBL; AF113122; AAF14863.1; -; mRNA.
DR EMBL; AF161471; AAF29086.1; -; mRNA.
DR EMBL; AK291397; BAF84086.1; -; mRNA.
DR EMBL; AL138713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL159972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471093; EAW80529.1; -; Genomic_DNA.
DR EMBL; BC019680; AAH19680.1; -; mRNA.
DR CCDS; CCDS9449.1; -. [Q9Y4X4-1]
DR RefSeq; NP_009180.3; NM_007249.4. [Q9Y4X4-1]
DR RefSeq; XP_005266308.1; XM_005266251.3. [Q9Y4X4-1]
DR RefSeq; XP_011533211.1; XM_011534909.2. [Q9Y4X4-1]
DR AlphaFoldDB; Q9Y4X4; -.
DR SMR; Q9Y4X4; -.
DR BioGRID; 116434; 184.
DR IntAct; Q9Y4X4; 185.
DR STRING; 9606.ENSP00000366897; -.
DR iPTMnet; Q9Y4X4; -.
DR PhosphoSitePlus; Q9Y4X4; -.
DR BioMuta; KLF12; -.
DR DMDM; 91771555; -.
DR EPD; Q9Y4X4; -.
DR jPOST; Q9Y4X4; -.
DR MassIVE; Q9Y4X4; -.
DR MaxQB; Q9Y4X4; -.
DR PaxDb; Q9Y4X4; -.
DR PeptideAtlas; Q9Y4X4; -.
DR PRIDE; Q9Y4X4; -.
DR ProteomicsDB; 86262; -. [Q9Y4X4-1]
DR ProteomicsDB; 86263; -. [Q9Y4X4-2]
DR Antibodypedia; 24434; 287 antibodies from 29 providers.
DR DNASU; 11278; -.
DR Ensembl; ENST00000377669.7; ENSP00000366897.2; ENSG00000118922.18. [Q9Y4X4-1]
DR GeneID; 11278; -.
DR KEGG; hsa:11278; -.
DR UCSC; uc058xlm.1; human. [Q9Y4X4-1]
DR CTD; 11278; -.
DR DisGeNET; 11278; -.
DR GeneCards; KLF12; -.
DR HGNC; HGNC:6346; KLF12.
DR HPA; ENSG00000118922; Low tissue specificity.
DR MIM; 607531; gene.
DR neXtProt; NX_Q9Y4X4; -.
DR OpenTargets; ENSG00000118922; -.
DR PharmGKB; PA30132; -.
DR VEuPathDB; HostDB:ENSG00000118922; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158108; -.
DR InParanoid; Q9Y4X4; -.
DR OMA; NIPMKRK; -.
DR OrthoDB; 845652at2759; -.
DR PhylomeDB; Q9Y4X4; -.
DR TreeFam; TF350556; -.
DR PathwayCommons; Q9Y4X4; -.
DR SignaLink; Q9Y4X4; -.
DR BioGRID-ORCS; 11278; 9 hits in 1091 CRISPR screens.
DR ChiTaRS; KLF12; human.
DR GeneWiki; KLF12; -.
DR GenomeRNAi; 11278; -.
DR Pharos; Q9Y4X4; Tbio.
DR PRO; PR:Q9Y4X4; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9Y4X4; protein.
DR Bgee; ENSG00000118922; Expressed in corpus epididymis and 196 other tissues.
DR Genevisible; Q9Y4X4; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR030447; KLF12.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23235:SF56; PTHR23235:SF56; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..402
FT /note="Krueppel-like factor 12"
FT /id="PRO_0000047182"
FT ZN_FING 317..341
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 347..371
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 377..399
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 79..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 80..88
FT /note="9aaTAD; inactive"
FT /evidence="ECO:0000269|PubMed:31375868"
FT COMPBIAS 278..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 313
FT /note="N6-methylated lysine; by EHMT2"
FT /evidence="ECO:0000269|PubMed:18438403"
FT VAR_SEQ 270..402
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11042152, ECO:0000303|Ref.4"
FT /id="VSP_006876"
FT VAR_SEQ 290..309
FT /note="CSISPFSIESTRRQRRSESP -> WRETLQVYLGRLHLEVRSFR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:23134681"
FT /id="VSP_047486"
FT VAR_SEQ 310..402
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:23134681"
FT /id="VSP_047487"
FT CONFLICT 246
FT /note="P -> L (in Ref. 1; CAB46982 and 2; AAK12082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 44240 MW; 9557E776878BAA8D CRC64;
MNIHMKRKTI KNINTFENRM LMLDGMPAVR VKTELLESEQ GSPNVHNYPD MEAVPLLLNN
VKGEPPEDSL SVDHFQTQTE PVDLSINKAR TSPTAVSSSP VSMTASASSP SSTSTSSSSS
SRLASSPTVI TSVSSASSSS TVLTPGPLVA SASGVGGQQF LHIIHPVPPS SPMNLQSNKL
SHVHRIPVVV QSVPVVYTAV RSPGNVNNTI VVPLLEDGRG HGKAQMDPRG LSPRQSKSDS
DDDDLPNVTL DSVNETGSTA LSIARAVQEV HPSPVSRVRG NRMNNQKFPC SISPFSIEST
RRQRRSESPD SRKRRIHRCD FEGCNKVYTK SSHLKAHRRT HTGEKPYKCT WEGCTWKFAR
SDELTRHYRK HTGVKPFKCA DCDRSFSRSD HLALHRRRHM LV
