ID   GATA6_MOUSE             Reviewed;         589 AA.
AC   Q61169; P97729; Q3UQJ2; Q9QZK3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 3.
DT   24-JAN-2024, entry version 187.
DE   RecName: Full=Transcription factor GATA-6;
DE   AltName: Full=GATA-binding factor 6;
GN   Name=Gata6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Heart;
RX   PubMed=8660897; DOI=10.1006/dbio.1996.0165;
RA   Morrisey E.E., Ip H.S., Lu M.M., Parmacek M.S.;
RT   "GATA-6: a zinc finger transcription factor that is expressed in multiple
RT   cell lineages derived from lateral mesoderm.";
RL   Dev. Biol. 177:309-322(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6 X DBA/2; TISSUE=Heart;
RA   Katsuoka F., Motohashi H., Yamamoto M.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 384-589 (ISOFORM 1).
RC   STRAIN=BALB/cJ; TISSUE=Heart;
RX   PubMed=8812463; DOI=10.1006/geno.1996.0472;
RA   Narita N., Heikinheimo M., Bielinska M., White R.A., Wilson D.B.;
RT   "The gene for transcription factor GATA-6 resides on mouse chromosome 18
RT   and is expressed in myocardium and vascular smooth muscle.";
RL   Genomics 36:345-348(1996).
RN   [6]
RP   ALTERNATIVE INITIATION.
RX   PubMed=10608869; DOI=10.1074/jbc.274.53.38004;
RA   Brewer A., Gove C., Davies A., McNulty C., Barrow D., Koutsourakis M.,
RA   Farzaneh F., Pizzey J., Bomford A., Patient R.;
RT   "The human and mouse GATA-6 genes utilize two promoters and two initiation
RT   codons.";
RL   J. Biol. Chem. 274:38004-38016(1999).
RN   [7]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=15329343; DOI=10.1242/dev.01344;
RA   Lee K.H., Evans S., Ruan T.Y., Lassar A.B.;
RT   "SMAD-mediated modulation of YY1 activity regulates the BMP response and
RT   cardiac-specific expression of a GATA4/5/6-dependent chick Nkx2.5
RT   enhancer.";
RL   Development 131:4709-4723(2004).
RN   [8]
RP   SUBCELLULAR LOCATION, INTERACTION WITH LMCD1, AND DOMAIN GATA-TYPE
RP   ZINC-FINGER.
RX   PubMed=16199866; DOI=10.1128/mcb.25.20.8864-8873.2005;
RA   Rath N., Wang Z., Lu M.M., Morrisey E.E.;
RT   "LMCD1/Dyxin is a novel transcriptional cofactor that restricts GATA6
RT   function by inhibiting DNA binding.";
RL   Mol. Cell. Biol. 25:8864-8873(2005).
RN   [9]
RP   FUNCTION.
RX   PubMed=19666519; DOI=10.1073/pnas.0904744106;
RA   Kodo K., Nishizawa T., Furutani M., Arai S., Yamamura E., Joo K.,
RA   Takahashi T., Matsuoka R., Yamagishi H.;
RT   "GATA6 mutations cause human cardiac outflow tract defects by disrupting
RT   semaphorin-plexin signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:13933-13938(2009).
CC   -!- FUNCTION: Transcriptional activator that regulates SEMA3C and PLXNA2
CC       (PubMed:19666519). May regulate genes that protect epithelial cells
CC       from bacterial infection (By similarity). Involved in gene regulation
CC       specifically in the gastric epithelium (By similarity). Involved in
CC       bone morphogenetic protein (BMP)-mediated cardiac-specific gene
CC       expression (PubMed:15329343). Binds to BMP response element (BMPRE) DNA
CC       sequences within cardiac activating regions (PubMed:15329343).
CC       {ECO:0000250|UniProtKB:Q92908, ECO:0000269|PubMed:15329343,
CC       ECO:0000269|PubMed:19666519}.
CC   -!- SUBUNIT: Interacts with LMCD1. {ECO:0000269|PubMed:16199866}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16199866}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q61169-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61169-2; Sequence=VSP_035779;
CC   -!- TISSUE SPECIFICITY: Expressed in myocardium, vascular smooth muscle,
CC       gut epithelium, and osteoclasts.
CC   -!- DOMAIN: The GATA-type zinc fingers mediate interaction with LMCD1.
CC       {ECO:0000269|PubMed:16199866}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-
CC       147 of isoform 1. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB37426.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAC52841.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; S82462; AAB37426.1; ALT_FRAME; mRNA.
DR   EMBL; AF179425; AAD55267.1; -; mRNA.
DR   EMBL; AK142381; BAE25049.1; -; mRNA.
DR   EMBL; CH466592; EDL22985.1; -; Genomic_DNA.
DR   EMBL; U51335; AAC52841.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS29059.1; -. [Q61169-1]
DR   RefSeq; NP_034388.2; NM_010258.3. [Q61169-1]
DR   AlphaFoldDB; Q61169; -.
DR   SMR; Q61169; -.
DR   BioGRID; 199843; 12.
DR   IntAct; Q61169; 3.
DR   MINT; Q61169; -.
DR   STRING; 10090.ENSMUSP00000041774; -.
DR   iPTMnet; Q61169; -.
DR   PhosphoSitePlus; Q61169; -.
DR   MaxQB; Q61169; -.
DR   PaxDb; 10090-ENSMUSP00000041774; -.
DR   PeptideAtlas; Q61169; -.
DR   ProteomicsDB; 271191; -. [Q61169-1]
DR   ProteomicsDB; 271192; -. [Q61169-2]
DR   Antibodypedia; 22009; 570 antibodies from 36 providers.
DR   DNASU; 14465; -.
DR   Ensembl; ENSMUST00000047762.10; ENSMUSP00000041774.8; ENSMUSG00000005836.11. [Q61169-1]
DR   GeneID; 14465; -.
DR   KEGG; mmu:14465; -.
DR   UCSC; uc008ebj.1; mouse. [Q61169-1]
DR   AGR; MGI:107516; -.
DR   CTD; 2627; -.
DR   MGI; MGI:107516; Gata6.
DR   VEuPathDB; HostDB:ENSMUSG00000005836; -.
DR   eggNOG; KOG1601; Eukaryota.
DR   GeneTree; ENSGT00940000160814; -.
DR   HOGENOM; CLU_027524_0_0_1; -.
DR   InParanoid; Q61169; -.
DR   OMA; ENSMLHC; -.
DR   OrthoDB; 685518at2759; -.
DR   PhylomeDB; Q61169; -.
DR   TreeFam; TF315391; -.
DR   Reactome; R-MMU-5683826; Surfactant metabolism.
DR   Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 14465; 4 hits in 83 CRISPR screens.
DR   PRO; PR:Q61169; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q61169; Protein.
DR   Bgee; ENSMUSG00000005836; Expressed in cardiac atrium and 233 other cell types or tissues.
DR   ExpressionAtlas; Q61169; baseline and differential.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
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; IDA:MGI.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR   GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0051525; F:NFAT protein binding; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR   GO; GO:0001223; F:transcription coactivator binding; IPI:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048645; P:animal organ formation; IMP:MGI.
DR   GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR   GO; GO:0060038; P:cardiac muscle cell proliferation; IGI:MGI.
DR   GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IMP:MGI.
DR   GO; GO:0048738; P:cardiac muscle tissue development; IGI:MGI.
DR   GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; ISO:MGI.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0071773; P:cellular response to BMP stimulus; IDA:MGI.
DR   GO; GO:0071371; P:cellular response to gonadotropin stimulus; IDA:MGI.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR   GO; GO:0060486; P:club cell differentiation; IGI:MGI.
DR   GO; GO:0035987; P:endodermal cell differentiation; IMP:MGI.
DR   GO; GO:0007493; P:endodermal cell fate determination; IDA:MGI.
DR   GO; GO:0030855; P:epithelial cell differentiation; IMP:MGI.
DR   GO; GO:0070315; P:G1 to G0 transition involved in cell differentiation; ISO:MGI.
DR   GO; GO:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:0060047; P:heart contraction; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0060575; P:intestinal epithelial cell differentiation; ISO:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0060430; P:lung saccule development; IGI:MGI.
DR   GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:MGI.
DR   GO; GO:1904003; P:negative regulation of sebum secreting cell proliferation; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0032911; P:negative regulation of transforming growth factor beta1 production; ISO:MGI.
DR   GO; GO:0032912; P:negative regulation of transforming growth factor beta2 production; ISO:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0003148; P:outflow tract septum morphogenesis; ISO:MGI.
DR   GO; GO:0031016; P:pancreas development; IMP:MGI.
DR   GO; GO:0003310; P:pancreatic A cell differentiation; IMP:MGI.
DR   GO; GO:0006644; P:phospholipid metabolic process; IGI:MGI.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:MGI.
DR   GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR   GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IGI:MGI.
DR   GO; GO:0110024; P:positive regulation of cardiac muscle myoblast proliferation; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:1901390; P:positive regulation of transforming growth factor beta activation; ISO:MGI.
DR   GO; GO:0002759; P:regulation of antimicrobial humoral response; ISO:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR   GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR   GO; GO:0043627; P:response to estrogen; IDA:MGI.
DR   GO; GO:0070848; P:response to growth factor; ISO:MGI.
DR   GO; GO:0032526; P:response to retinoic acid; ISO:MGI.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR   GO; GO:0001949; P:sebaceous gland cell differentiation; ISO:MGI.
DR   GO; GO:0003163; P:sinoatrial node development; IMP:MGI.
DR   GO; GO:0098773; P:skin epidermis development; ISO:MGI.
DR   GO; GO:0051145; P:smooth muscle cell differentiation; ISO:MGI.
DR   GO; GO:0048863; P:stem cell differentiation; IMP:MGI.
DR   GO; GO:0035239; P:tube morphogenesis; IGI:MGI.
DR   GO; GO:0003309; P:type B pancreatic cell differentiation; IMP:MGI.
DR   GO; GO:0060510; P:type II pneumocyte differentiation; IGI:MGI.
DR   CDD; cd00202; ZnF_GATA; 2.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 2.
DR   InterPro; IPR008013; GATA_N.
DR   InterPro; IPR039355; Transcription_factor_GATA.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR10071; TRANSCRIPTION FACTOR GATA FAMILY MEMBER; 1.
DR   PANTHER; PTHR10071:SF23; TRANSCRIPTION FACTOR GATA-6; 1.
DR   Pfam; PF00320; GATA; 2.
DR   Pfam; PF05349; GATA-N; 1.
DR   PRINTS; PR00619; GATAZNFINGER.
DR   SMART; SM00401; ZnF_GATA; 2.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
DR   Genevisible; Q61169; MM.
PE   1: Evidence at protein level;
KW   Activator; Alternative initiation; DNA-binding; Isopeptide bond;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..589
FT                   /note="Transcription factor GATA-6"
FT                   /id="PRO_0000083424"
FT   ZN_FING         384..408
FT                   /note="GATA-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT   ZN_FING         438..462
FT                   /note="GATA-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT   REGION          17..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         266
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92908"
FT   CROSSLNK        423
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q92908"
FT   CROSSLNK        467
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q92908"
FT   CROSSLNK        478
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q92908"
FT   VAR_SEQ         1..146
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8660897, ECO:0000303|Ref.2"
FT                   /id="VSP_035779"
FT   CONFLICT        297
FT                   /note="S -> T (in Ref. 1; AAB37426)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="G -> A (in Ref. 5; AAC52841)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        536
FT                   /note="G -> R (in Ref. 5; AAC52841)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        538
FT                   /note="Missing (in Ref. 5; AAC52841)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        546
FT                   /note="N -> K (in Ref. 5; AAC52841)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        589
FT                   /note="A -> V (in Ref. 1; AAB37426 and 2; AAD55267)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   589 AA;  59307 MW;  1A55474DA65EC6ED CRC64;
     MALTDGGWCL PKRFGAAAAD AGDSGPFPAR EPSSPLSPIS SSSSSCSRGG DRGPCGASNC
     RTPQLDAEAV AGPPGRSLLL SPYASHPFAA AHGAAAPGVA GPGSALSTWE DLLLFTDLDQ
     AATASKLLWS SRGAKLSPFA AEQPEEMYQT LAALSSQGPA AYDGAPGGFV HSAAAAAAAA
     AAASSPVYVP TTRVGSMLSG LPYLQGAGSG PSNHAGGAGA HPGWSQASAD SPPYGGGGAA
     GGGAAGPGGA GSATAHASAR FPYSPSPPMA NGAARDPGGY VAAGGTGAGS VSGGGGSLAA
     MGGREHQYSS LSAARPLNGT YHHHHHHHPT YSPYMAAPLT PAWPAGPFET PVLHSLQGRA
     GAPLPVPRGP STDLLEDLSE SRECVNCGSI QTPLWRRDGT GHYLCNACGL YSKMNGLSRP
     LIKPQKRVPS SRRLGLSCAN CHTTTTTLWR RNAEGEPVCN ACGLYMKLHG VPRPLAMKKE
     GIQTRKRKPK NINKSKACSG NSSGSVPMTP TSSSSNSDDC TKNTSPSTQA TTSGVGASVM
     SAVGENANPE NSDLKYSGQD GLYIGVSLSS PAEVTSSVRQ DSWCALALA
//