NFAC3_HUMAN
ID NFAC3_HUMAN Reviewed; 1075 AA.
AC Q12968; O75211; Q14516; Q99840; Q99841; Q99842;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Nuclear factor of activated T-cells, cytoplasmic 3;
DE Short=NF-ATc3;
DE Short=NFATc3;
DE AltName: Full=NFATx;
DE AltName: Full=T-cell transcription factor NFAT4 {ECO:0000303|PubMed:7749981};
DE Short=NF-AT4 {ECO:0000303|PubMed:7749981};
DE Short=NF-AT4c {ECO:0000303|PubMed:7749981};
GN Name=NFATC3; Synonyms=NFAT4 {ECO:0000303|PubMed:7749981};
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] (ISOFORMS 2; 5 AND 6).
RC TISSUE=Skeletal muscle, and T-cell;
RX PubMed=7749981; DOI=10.1016/1074-7613(95)90027-6;
RA Hoey T., Sun Y.-L., Williamson K., Xu X.;
RT "Isolation of two new members of the NF-AT gene family and functional
RT characterization of the NF-AT proteins.";
RL Immunity 2:461-472(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=T-cell;
RX PubMed=7739550; DOI=10.1128/mcb.15.5.2697;
RA Masuda E.S., Naito Y., Tokumitsu H., Campbell D., Saito F., Hannum C.,
RA Arai K., Arai N.;
RT "NFATx, a novel member of the nuclear factor of activated T cells family
RT that is expressed predominantly in the thymus.";
RL Mol. Cell. Biol. 15:2697-2706(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Fibroblast, and T-cell;
RX PubMed=9759864;
RA Imamura R., Masuda E.S., Naito Y., Imai S., Fujino T., Takano T., Arai K.,
RA Arai N.;
RT "Carboxy-terminal 15 amino acids sequence of NFATx1 is possibly created by
RT tissue-specific splicing and is essential for transactivation activity in T
RT cells.";
RL J. Immunol. 161:3455-3463(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 4).
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [6]
RP PROTEIN SEQUENCE OF 2-15; 468-488; 505-519 AND 579-594, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP MUTAGENESIS.
RX PubMed=9630228; DOI=10.1016/s0092-8674(00)81445-2;
RA Zhu J., Shibasaki F., Price R., Guillemot J.-C., Yano T., Doetsch V.,
RA Wagner G., Ferrara P., McKeon F.;
RT "Intramolecular masking of nuclear import signal on NF-AT4 by casein kinase
RT I and MEKK1.";
RL Cell 93:851-861(1998).
RN [8]
RP REVIEW.
RX PubMed=10089876; DOI=10.1016/s0092-8674(00)80571-1;
RA Crabtree G.R.;
RT "Generic signals and specific outcomes: signaling through Ca2+,
RT calcineurin, and NF-AT.";
RL Cell 96:611-614(1999).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18815128; DOI=10.1074/jbc.m806684200;
RA Li G.D., Zhang X., Li R., Wang Y.D., Wang Y.L., Han K.J., Qian X.P.,
RA Yang C.G., Liu P., Wei Q., Chen W.F., Zhang J., Zhang Y.;
RT "CHP2 activates the calcineurin/nuclear factor of activated T cells
RT signaling pathway and enhances the oncogenic potential of HEK293 cells.";
RL J. Biol. Chem. 283:32660-32668(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372; SER-1063 AND SER-1066,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Acts as a regulator of transcriptional activation. Plays a
CC role in the inducible expression of cytokine genes in T-cells,
CC especially in the induction of the IL-2 (PubMed:18815128). Along with
CC NFATC4, involved in embryonic heart development (By similarity).
CC {ECO:0000250|UniProtKB:P97305, ECO:0000269|PubMed:18815128}.
CC -!- SUBUNIT: Member of the multicomponent NFATC transcription complex that
CC consists of at least two components, a pre-existing cytoplasmic
CC component NFATC2 and an inducible nuclear component NFATC1. Other
CC members such as NFATC4, or members of the activating protein-1 family,
CC MAF, GATA4 and Cbp/p300 can also bind the complex. NFATC proteins bind
CC to DNA as monomers. Interacts with TRIM17; this interaction prevents
CC NFATC3 nuclear localization (By similarity).
CC {ECO:0000250|UniProtKB:P97305}.
CC -!- INTERACTION:
CC Q12968; P04049: RAF1; NbExp=2; IntAct=EBI-5278441, EBI-365996;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18815128}. Nucleus
CC {ECO:0000269|PubMed:18815128}. Note=Cytoplasmic for the phosphorylated
CC form and nuclear after activation that is controlled by calcineurin-
CC mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to
CC be one mechanism by which cells distinguish between sustained and
CC transient calcium signals. The subcellular localization of NFATC plays
CC a key role in the regulation of gene transcription.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=X1;
CC IsoId=Q12968-1; Sequence=Displayed;
CC Name=2; Synonyms=X2, C;
CC IsoId=Q12968-2; Sequence=VSP_005600;
CC Name=3; Synonyms=X3;
CC IsoId=Q12968-3; Sequence=VSP_005601;
CC Name=4; Synonyms=X4;
CC IsoId=Q12968-4; Sequence=VSP_005602;
CC Name=5; Synonyms=A;
CC IsoId=Q12968-5; Sequence=VSP_005598;
CC Name=6; Synonyms=B;
CC IsoId=Q12968-6; Sequence=VSP_005599;
CC -!- TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in thymus and
CC is also found in peripheral blood leukocytes and kidney. Isoform 2 is
CC predominantly expressed in skeletal muscle and is also found in thymus,
CC kidney, testis, spleen, prostate, ovary, small intestine, heart,
CC placenta and pancreas. Isoform 3 is expressed in thymus and kidney.
CC Isoform 4 is expressed in thymus and skeletal muscle.
CC -!- DOMAIN: Rel Similarity Domain (RSD) allows DNA-binding and cooperative
CC interactions with AP1 factors.
CC -!- PTM: Phosphorylated by NFATC-kinase; dephosphorylated by calcineurin.
CC {ECO:0000250}.
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DR EMBL; L41067; AAA79174.1; -; mRNA.
DR EMBL; U14510; AAA86308.1; -; mRNA.
DR EMBL; U85428; AAB46595.1; -; mRNA.
DR EMBL; U85429; AAB46596.1; -; mRNA.
DR EMBL; U85430; AAB46597.1; -; mRNA.
DR EMBL; AC130462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001050; AAH01050.1; -; mRNA.
DR CCDS; CCDS10860.1; -. [Q12968-1]
DR CCDS; CCDS10861.1; -. [Q12968-3]
DR CCDS; CCDS10862.1; -. [Q12968-2]
DR PIR; A57377; A57377.
DR RefSeq; NP_004546.1; NM_004555.3. [Q12968-2]
DR RefSeq; NP_775186.1; NM_173163.2. [Q12968-3]
DR RefSeq; NP_775188.1; NM_173165.2. [Q12968-1]
DR PDB; 2XRW; X-ray; 1.33 A; B=141-154.
DR PDB; 2XS0; X-ray; 2.60 A; B=141-154.
DR PDBsum; 2XRW; -.
DR PDBsum; 2XS0; -.
DR AlphaFoldDB; Q12968; -.
DR SMR; Q12968; -.
DR BioGRID; 110848; 30.
DR ELM; Q12968; -.
DR IntAct; Q12968; 14.
DR MINT; Q12968; -.
DR STRING; 9606.ENSP00000300659; -.
DR GlyGen; Q12968; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12968; -.
DR PhosphoSitePlus; Q12968; -.
DR BioMuta; NFATC3; -.
DR DMDM; 9087155; -.
DR EPD; Q12968; -.
DR jPOST; Q12968; -.
DR MassIVE; Q12968; -.
DR MaxQB; Q12968; -.
DR PaxDb; Q12968; -.
DR PeptideAtlas; Q12968; -.
DR PRIDE; Q12968; -.
DR ProteomicsDB; 59061; -. [Q12968-1]
DR ProteomicsDB; 59062; -. [Q12968-2]
DR ProteomicsDB; 59063; -. [Q12968-3]
DR ProteomicsDB; 59064; -. [Q12968-4]
DR ProteomicsDB; 59065; -. [Q12968-5]
DR ProteomicsDB; 59066; -. [Q12968-6]
DR Antibodypedia; 3861; 329 antibodies from 38 providers.
DR DNASU; 4775; -.
DR Ensembl; ENST00000329524.8; ENSP00000331324.4; ENSG00000072736.19. [Q12968-2]
DR Ensembl; ENST00000346183.8; ENSP00000300659.5; ENSG00000072736.19. [Q12968-1]
DR Ensembl; ENST00000349223.9; ENSP00000264008.6; ENSG00000072736.19. [Q12968-3]
DR GeneID; 4775; -.
DR KEGG; hsa:4775; -.
DR MANE-Select; ENST00000346183.8; ENSP00000300659.5; NM_173165.3; NP_775188.1.
DR UCSC; uc002evm.3; human. [Q12968-1]
DR CTD; 4775; -.
DR DisGeNET; 4775; -.
DR GeneCards; NFATC3; -.
DR HGNC; HGNC:7777; NFATC3.
DR HPA; ENSG00000072736; Tissue enhanced (lymphoid).
DR MIM; 602698; gene.
DR neXtProt; NX_Q12968; -.
DR OpenTargets; ENSG00000072736; -.
DR PharmGKB; PA247; -.
DR VEuPathDB; HostDB:ENSG00000072736; -.
DR eggNOG; ENOG502QWQ4; Eukaryota.
DR GeneTree; ENSGT00940000156131; -.
DR InParanoid; Q12968; -.
DR OMA; QGHKSYE; -.
DR PhylomeDB; Q12968; -.
DR TreeFam; TF326480; -.
DR PathwayCommons; Q12968; -.
DR Reactome; R-HSA-2025928; Calcineurin activates NFAT.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-HSA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR SignaLink; Q12968; -.
DR SIGNOR; Q12968; -.
DR BioGRID-ORCS; 4775; 12 hits in 1102 CRISPR screens.
DR ChiTaRS; NFATC3; human.
DR GeneWiki; NFATC3; -.
DR GenomeRNAi; 4775; -.
DR Pharos; Q12968; Tbio.
DR PRO; PR:Q12968; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q12968; protein.
DR Bgee; ENSG00000072736; Expressed in oocyte and 203 other tissues.
DR ExpressionAtlas; Q12968; baseline and differential.
DR Genevisible; Q12968; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IGI:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IGI:BHF-UCL.
DR GO; GO:1905064; P:negative regulation of vascular associated smooth muscle cell differentiation; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 1.
DR IDEAL; IID00466; -.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR008366; NFAT.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR032397; RHD_dimer.
DR InterPro; IPR011539; RHD_DNA_bind_dom.
DR InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR PANTHER; PTHR12533; PTHR12533; 1.
DR Pfam; PF16179; RHD_dimer; 1.
DR Pfam; PF00554; RHD_DNA_bind; 1.
DR PRINTS; PR01789; NUCFACTORATC.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50254; REL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Cytoplasm;
KW Developmental protein; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..1075
FT /note="Nuclear factor of activated T-cells, cytoplasmic 3"
FT /id="PRO_0000205180"
FT REPEAT 207..223
FT /note="1"
FT REPEAT 236..252
FT /note="2"
FT REPEAT 292..308
FT /note="3"
FT DOMAIN 415..596
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT DNA_BIND 444..451
FT REGION 18..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..114
FT /note="Calcineurin-binding"
FT REGION 205..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..308
FT /note="3 X SP repeats"
FT REGION 711..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 273..275
FT /note="Nuclear localization signal"
FT MOTIF 686..688
FT /note="Nuclear localization signal"
FT MOTIF 1032..1041
FT /note="Nuclear export signal"
FT COMPBIAS 229..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97305"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1063
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1066
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 700..1075
FT /note="VLMKQEHREEIDLSSVPSLPVPHPAQTQRPSSDSGCSHDSVLSGQRSLICSI
FT PQTYASMVTSSHLPQLQCRDESVSKEQHMIPSPIVHQPFQVTPTPPVGSSYQPMQTNVV
FT YNGPTCLPINAASSQEFDSVLFQQDATLSGLVNLGCQPLSSIPFHSSNSGSTGHLLAHT
FT PHSVHTLPHLQSMGYHCSNTGQRSLSSPVADQITGQPSSQLQPITYGPSHSGSATTASP
FT AASHPLASSPLSGPPSPQLQPMPYQSPSSGTASSPSPATRMHSGQHSTQAQSTGQGGLS
FT APSSLICHSLCDPASFPPDGATVSIKPEPEDREPNFATIGLQDITLDDVNEIIGRDMSQ
FT ISVSQGAGVSRQAPLPSPESLDLGRSDGL -> GTRSHDGLL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:7749981"
FT /id="VSP_005598"
FT VAR_SEQ 717..1075
FT /note="SLPVPHPAQTQRPSSDSGCSHDSVLSGQRSLICSIPQTYASMVTSSHLPQLQ
FT CRDESVSKEQHMIPSPIVHQPFQVTPTPPVGSSYQPMQTNVVYNGPTCLPINAASSQEF
FT DSVLFQQDATLSGLVNLGCQPLSSIPFHSSNSGSTGHLLAHTPHSVHTLPHLQSMGYHC
FT SNTGQRSLSSPVADQITGQPSSQLQPITYGPSHSGSATTASPAASHPLASSPLSGPPSP
FT QLQPMPYQSPSSGTASSPSPATRMHSGQHSTQAQSTGQGGLSAPSSLICHSLCDPASFP
FT PDGATVSIKPEPEDREPNFATIGLQDITLDDVNEIIGRDMSQISVSQGAGVSRQAPLPS
FT PESLDLGRSDGL -> TLPQTSRQTLLGSQPPSASPPTV (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:7749981"
FT /id="VSP_005599"
FT VAR_SEQ 1036..1075
FT /note="VNEIIGRDMSQISVSQGAGVSRQAPLPSPESLDLGRSDGL -> DQFISDLE
FT HQPSGSAEKWPNHSVLSCPAPFWRI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7749981,
FT ECO:0000303|PubMed:9759864"
FT /id="VSP_005600"
FT VAR_SEQ 1036..1075
FT /note="VNEIIGRDMSQISVSQGAGVSRQAPLPSPESLDLGRSDGL -> DLFTSNNF
FT DLLQLRPTFWPVPAGRYLRNLE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9759864"
FT /id="VSP_005601"
FT VAR_SEQ 1036..1075
FT /note="VNEIIGRDMSQISVSQGAGVSRQAPLPSPESLDLGRSDGL -> GKFISDMF
FT LK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9759864"
FT /id="VSP_005602"
FT VARIANT 75
FT /note="S -> L (in dbSNP:rs2230092)"
FT /id="VAR_051784"
FT VARIANT 94
FT /note="E -> A (in dbSNP:rs3743736)"
FT /id="VAR_051785"
FT VARIANT 100
FT /note="L -> S (in dbSNP:rs2230093)"
FT /id="VAR_051786"
FT VARIANT 136
FT /note="P -> L (in dbSNP:rs2230094)"
FT /id="VAR_051787"
FT VARIANT 382
FT /note="P -> S (in dbSNP:rs2230095)"
FT /id="VAR_051788"
FT CONFLICT 702
FT /note="M -> L (in Ref. 3; AAB46595/AAB46596/AAB46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="L -> W (in Ref. 3; AAB46595/AAB46596/AAB46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="A -> G (in Ref. 3; AAB46595/AAB46596/AAB46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="A -> V (in Ref. 3; AAB46595/AAB46596/AAB46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 935
FT /note="A -> G (in Ref. 3; AAB46595/AAB46596/AAB46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 947
FT /note="L -> F (in Ref. 3; AAB46595/AAB46596/AAB46597)"
FT /evidence="ECO:0000305"
FT CONFLICT 960
FT /note="A -> G (in Ref. 3; AAB46595/AAB46596/AAB46597)"
FT /evidence="ECO:0000305"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2XRW"
SQ SEQUENCE 1075 AA; 115594 MW; 0B25D61A2B56D898 CRC64;
MTTANCGAHD ELDFKLVFGE DGAPAPPPPG SRPADLEPDD CASIYIFNVD PPPSTLTTPL
CLPHHGLPSH SSVLSPSFQL QSHKNYEGTC EIPESKYSPL GGPKPFECPS IQITSISPNC
HQELDAHEDD LQINDPEREF LERPSRDHLY LPLEPSYRES SLSPSPASSI SSRSWFSDAS
SCESLSHIYD DVDSELNEAA ARFTLGSPLT SPGGSPGGCP GEETWHQQYG LGHSLSPRQS
PCHSPRSSVT DENWLSPRPA SGPSSRPTSP CGKRRHSSAE VCYAGSLSPH HSPVPSPGHS
PRGSVTEDTW LNASVHGGSG LGPAVFPFQY CVETDIPLKT RKTSEDQAAI LPGKLELCSD
DQGSLSPARE TSIDDGLGSQ YPLKKDSCGD QFLSVPSPFT WSKPKPGHTP IFRTSSLPPL
DWPLPAHFGQ CELKIEVQPK THHRAHYETE GSRGAVKAST GGHPVVKLLG YNEKPINLQM
FIGTADDRYL RPHAFYQVHR ITGKTVATAS QEIIIASTKV LEIPLLPENN MSASIDCAGI
LKLRNSDIEL RKGETDIGRK NTRVRLVFRV HIPQPSGKVL SLQIASIPVE CSQRSAQELP
HIEKYSINSC SVNGGHEMVV TGSNFLPESK IIFLEKGQDG RPQWEVEGKI IREKCQGAHI
VLEVPPYHNP AVTAAVQVHF YLCNGKRKKS QSQRFTYTPV LMKQEHREEI DLSSVPSLPV
PHPAQTQRPS SDSGCSHDSV LSGQRSLICS IPQTYASMVT SSHLPQLQCR DESVSKEQHM
IPSPIVHQPF QVTPTPPVGS SYQPMQTNVV YNGPTCLPIN AASSQEFDSV LFQQDATLSG
LVNLGCQPLS SIPFHSSNSG STGHLLAHTP HSVHTLPHLQ SMGYHCSNTG QRSLSSPVAD
QITGQPSSQL QPITYGPSHS GSATTASPAA SHPLASSPLS GPPSPQLQPM PYQSPSSGTA
SSPSPATRMH SGQHSTQAQS TGQGGLSAPS SLICHSLCDP ASFPPDGATV SIKPEPEDRE
PNFATIGLQD ITLDDVNEII GRDMSQISVS QGAGVSRQAP LPSPESLDLG RSDGL
