ID   CXA5_HUMAN              Reviewed;         358 AA.
AC   P36382; Q5T3B6; Q5U0N6;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 213.
DE   RecName: Full=Gap junction alpha-5 protein;
DE   AltName: Full=Connexin-40;
DE            Short=Cx40;
GN   Name=GJA5;
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 [GENOMIC DNA].
RX   PubMed=7966354; DOI=10.1006/jmcc.1994.1103;
RA   Kanter H.L., Saffitz J.E., Beyer E.C.;
RT   "Molecular cloning of two human cardiac gap junction proteins, connexin40
RT   and connexin45.";
RL   J. Mol. Cell. Cardiol. 26:861-868(1994).
RN   [2]
RP   SEQUENCE REVISION.
RA   Beyer E.C., Christensen E.A.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lin H.H., Jin N., Kiang D.T.;
RT   "Nucleotide sequence of protein-coding region of human connexin 40 gene.";
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10581143; DOI=10.1053/euhj.1999.1718;
RA   Haefliger J.-A., Goy J.J., Waeber G.;
RT   "Sporadic cases of dilated cardiomyopathies associated with
RT   atrioventricular conduction defects are not linked to mutation within the
RT   connexins 40 and 43 genes.";
RL   Eur. Heart J. 20:1843-1843(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   VARIANTS ATRST1 SER-88 AND SER-96.
RX   PubMed=16790700; DOI=10.1056/nejmoa052800;
RA   Gollob M.H., Jones D.L., Krahn A.D., Danis L., Gong X.Q., Shao Q., Liu X.,
RA   Veinot J.P., Tang A.S., Stewart A.F., Tesson F., Klein G.J., Yee R.,
RA   Skanes A.C., Guiraudon G.M., Ebihara L., Bai D.;
RT   "Somatic mutations in the connexin 40 gene (GJA5) in atrial fibrillation.";
RL   N. Engl. J. Med. 354:2677-2688(2006).
RN   [9]
RP   VARIANTS ATFB11 ILE-85; ILE-221 AND MET-229.
RX   PubMed=20650941; DOI=10.1093/europace/euq274;
RA   Yang Y.Q., Liu X., Zhang X.L., Wang X.H., Tan H.W., Shi H.F., Jiang W.F.,
RA   Fang W.Y.;
RT   "Novel connexin40 missense mutations in patients with familial atrial
RT   fibrillation.";
RL   Europace 12:1421-1427(2010).
CC   -!- FUNCTION: One gap junction consists of a cluster of closely packed
CC       pairs of transmembrane channels, the connexons, through which materials
CC       of low MW diffuse from one cell to a neighboring cell.
CC   -!- SUBUNIT: A connexon is composed of a hexamer of connexins.
CC   -!- INTERACTION:
CC       P36382; O95870: ABHD16A; NbExp=3; IntAct=EBI-750433, EBI-348517;
CC       P36382; Q8WVX3-2: ARLN; NbExp=3; IntAct=EBI-750433, EBI-12003442;
CC       P36382; P62952: BLCAP; NbExp=3; IntAct=EBI-750433, EBI-3895726;
CC       P36382; P27797: CALR; NbExp=3; IntAct=EBI-750433, EBI-1049597;
CC       P36382; P36957: DLST; NbExp=3; IntAct=EBI-750433, EBI-351007;
CC       P36382; P54852: EMP3; NbExp=3; IntAct=EBI-750433, EBI-3907816;
CC       P36382; P29033: GJB2; NbExp=3; IntAct=EBI-750433, EBI-3905204;
CC       P36382; P24593: IGFBP5; NbExp=3; IntAct=EBI-750433, EBI-720480;
CC       P36382; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-750433, EBI-1055254;
CC       P36382; O15243: LEPROT; NbExp=3; IntAct=EBI-750433, EBI-15672507;
CC       P36382; O95214: LEPROTL1; NbExp=3; IntAct=EBI-750433, EBI-750776;
CC       P36382; Q6ZUX7: LHFPL2; NbExp=3; IntAct=EBI-750433, EBI-17566767;
CC       P36382; Q6N075: MFSD5; NbExp=3; IntAct=EBI-750433, EBI-3920969;
CC       P36382; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-750433, EBI-12070086;
CC       P36382; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-750433, EBI-1055945;
CC       P36382; Q6P499: NIPAL3; NbExp=3; IntAct=EBI-750433, EBI-10252783;
CC       P36382; Q16617: NKG7; NbExp=3; IntAct=EBI-750433, EBI-3919611;
CC       P36382; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-750433, EBI-12092917;
CC       P36382; O60831: PRAF2; NbExp=3; IntAct=EBI-750433, EBI-2506064;
CC       P36382; Q9NS64: RPRM; NbExp=3; IntAct=EBI-750433, EBI-1052363;
CC       P36382; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-750433, EBI-12808018;
CC       P36382; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-750433, EBI-8644112;
CC       P36382; Q5T1Q4: SLC35F1; NbExp=3; IntAct=EBI-750433, EBI-13365456;
CC       P36382; Q8IVJ1: SLC41A1; NbExp=3; IntAct=EBI-750433, EBI-12266234;
CC       P36382; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-750433, EBI-10290130;
CC       P36382; Q6ZP29-3: SLC66A1; NbExp=3; IntAct=EBI-750433, EBI-12889586;
CC       P36382; P55061: TMBIM6; NbExp=3; IntAct=EBI-750433, EBI-1045825;
CC       P36382; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-750433, EBI-12845616;
CC       P36382; Q9NSU2-1: TREX1; NbExp=3; IntAct=EBI-750433, EBI-16746122;
CC       P36382; Q86Y07: VRK2; NbExp=3; IntAct=EBI-750433, EBI-1207615;
CC       P36382; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-750433, EBI-751210;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell
CC       junction, gap junction.
CC   -!- DISEASE: Atrial standstill 1 (ATRST1) [MIM:108770]: A rare arrhythmia
CC       characterized by the absence of electrical and mechanical activity in
CC       the atria. Electrocardiographically, it is characterized by
CC       bradycardia, the absence of P waves, and a junctional narrow complex
CC       escape rhythm. {ECO:0000269|PubMed:16790700}. Note=The disease may be
CC       caused by variants affecting distinct genetic loci, including the gene
CC       represented in this entry. A rare GJA5 genotype has been detected in
CC       combination with a mutation in SCN5A in a large family with atrial
CC       standstill.
CC   -!- DISEASE: Atrial fibrillation, familial, 11 (ATFB11) [MIM:614049]: A
CC       familial form of atrial fibrillation, a common sustained cardiac rhythm
CC       disturbance. Atrial fibrillation is characterized by disorganized
CC       atrial electrical activity and ineffective atrial contraction promoting
CC       blood stasis in the atria and reduces ventricular filling. It can
CC       result in palpitations, syncope, thromboembolic stroke, and congestive
CC       heart failure. {ECO:0000269|PubMed:20650941}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U03486; AAA60457.2; -; Genomic_DNA.
DR   EMBL; L34954; AAA91833.1; -; Genomic_DNA.
DR   EMBL; AF151979; AAD37801.1; -; Genomic_DNA.
DR   EMBL; BT019415; AAV38222.1; -; mRNA.
DR   EMBL; BT019416; AAV38223.1; -; mRNA.
DR   EMBL; AL365260; CAI14124.1; -; Genomic_DNA.
DR   EMBL; AL365260; CAI14125.1; -; Genomic_DNA.
DR   EMBL; BC013313; AAH13313.1; -; mRNA.
DR   CCDS; CCDS929.1; -.
DR   PIR; I38429; I38429.
DR   RefSeq; NP_005257.2; NM_005266.7.
DR   RefSeq; NP_859054.1; NM_181703.4.
DR   AlphaFoldDB; P36382; -.
DR   SMR; P36382; -.
DR   BioGRID; 108969; 37.
DR   FunCoup; P36382; 31.
DR   IntAct; P36382; 34.
DR   NDEx; IQUERY-CP-GJA5; 3 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000484552; -.
DR   TCDB; 1.A.24.1.15; the gap junction-forming connexin (connexin) family.
DR   iPTMnet; P36382; -.
DR   PhosphoSitePlus; P36382; -.
DR   BioMuta; GJA5; -.
DR   DMDM; 8928556; -.
DR   MassIVE; P36382; -.
DR   PaxDb; 9606-ENSP00000484552; -.
DR   PeptideAtlas; P36382; -.
DR   ProteomicsDB; 55180; -.
DR   Antibodypedia; 72405; 294 antibodies from 34 providers.
DR   DNASU; 2702; -.
DR   Ensembl; ENST00000579774.3; ENSP00000463851.1; ENSG00000265107.4.
DR   Ensembl; ENST00000621517.1; ENSP00000484552.1; ENSG00000265107.4.
DR   Ensembl; ENST00000863529.1; ENSP00000533588.1; ENSG00000265107.4.
DR   Ensembl; ENST00000922170.1; ENSP00000592229.1; ENSG00000265107.4.
DR   Ensembl; ENST00000955979.1; ENSP00000626038.1; ENSG00000265107.4.
DR   Ensembl; ENST00000955980.1; ENSP00000626039.1; ENSG00000265107.4.
DR   Ensembl; ENST00000955981.1; ENSP00000626040.1; ENSG00000265107.4.
DR   GeneID; 2702; -.
DR   KEGG; hsa:2702; -.
DR   MANE-Select; ENST00000579774.3; ENSP00000463851.1; NM_181703.4; NP_859054.1.
DR   UCSC; uc057kfi.1; human.
DR   AGR; HGNC:4279; -.
DR   ClinPGx; PA28690; -.
DR   CTD; 2702; -.
DR   DisGeNET; 2702; -.
DR   GeneCards; GJA5; -.
DR   GeneReviews; GJA5; -.
DR   HGNC; HGNC:4279; GJA5.
DR   HPA; ENSG00000265107; Tissue enhanced (placenta).
DR   MalaCards; GJA5; -.
DR   MIM; 108770; phenotype.
DR   MIM; 121013; gene.
DR   MIM; 614049; phenotype.
DR   OpenTargets; ENSG00000265107; -.
DR   Orphanet; 334; Hereditary atrial fibrillation.
DR   Orphanet; 3303; Tetralogy of Fallot.
DR   VEuPathDB; HostDB:ENSG00000265107; -.
DR   eggNOG; ENOG502QW11; Eukaryota.
DR   GeneTree; ENSGT01150000286930; -.
DR   HOGENOM; CLU_037388_0_0_1; -.
DR   InParanoid; P36382; -.
DR   OMA; FIHIHYG; -.
DR   OrthoDB; 9946832at2759; -.
DR   PAN-GO; P36382; 5 GO annotations based on evolutionary models.
DR   PhylomeDB; P36382; -.
DR   PathwayCommons; P36382; -.
DR   Reactome; R-HSA-190861; Gap junction assembly.
DR   SignaLink; P36382; -.
DR   SIGNOR; P36382; -.
DR   Agora; ENSG00000265107; -.
DR   BioGRID-ORCS; 2702; 11 hits in 1140 CRISPR screens.
DR   ChiTaRS; GJA5; human.
DR   GeneWiki; GJA5; -.
DR   GenomeRNAi; 2702; -.
DR   Pharos; P36382; Tbio.
DR   PRO; PR:P36382; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P36382; protein.
DR   Bgee; ENSG00000265107; Expressed in placenta and 125 other cell types or tissues.
DR   ExpressionAtlas; P36382; baseline and differential.
DR   GO; GO:0005922; C:connexin complex; IDA:BHF-UCL.
DR   GO; GO:0005921; C:gap junction; IDA:BHF-UCL.
DR   GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0071253; F:connexin binding; IEA:Ensembl.
DR   GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR   GO; GO:0086076; F:gap junction channel activity involved in atrial cardiac muscle cell-AV node cell electrical coupling; IMP:BHF-UCL.
DR   GO; GO:0086077; F:gap junction channel activity involved in AV node cell-bundle of His cell electrical coupling; IDA:BHF-UCL.
DR   GO; GO:0086078; F:gap junction channel activity involved in bundle of His cell-Purkinje myocyte electrical coupling; IMP:BHF-UCL.
DR   GO; GO:0086075; F:gap junction channel activity involved in cardiac conduction electrical coupling; IDA:BHF-UCL.
DR   GO; GO:0086079; F:gap junction channel activity involved in Purkinje myocyte-ventricular cardiac muscle cell electrical coupling; NAS:BHF-UCL.
DR   GO; GO:0086020; F:gap junction channel activity involved in SA node cell-atrial cardiac muscle cell electrical coupling; NAS:BHF-UCL.
DR   GO; GO:0055077; F:gap junction hemi-channel activity; IDA:BHF-UCL.
DR   GO; GO:0001525; P:angiogenesis; IEP:UniProtKB.
DR   GO; GO:0048844; P:artery morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0086044; P:atrial cardiac muscle cell to AV node cell communication by electrical coupling; IMP:BHF-UCL.
DR   GO; GO:0003283; P:atrial septum development; IMP:BHF-UCL.
DR   GO; GO:0086053; P:AV node cell to bundle of His cell communication by electrical coupling; IMP:BHF-UCL.
DR   GO; GO:0086054; P:bundle of His cell to Purkinje myocyte communication by electrical coupling; IMP:BHF-UCL.
DR   GO; GO:0003161; P:cardiac conduction system development; ISS:BHF-UCL.
DR   GO; GO:0010643; P:cell communication by chemical coupling; IEA:Ensembl.
DR   GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; IDA:BHF-UCL.
DR   GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR   GO; GO:0003158; P:endothelium development; IEA:Ensembl.
DR   GO; GO:0016264; P:gap junction assembly; IDA:BHF-UCL.
DR   GO; GO:0007507; P:heart development; IBA:GO_Central.
DR   GO; GO:0003174; P:mitral valve development; IMP:BHF-UCL.
DR   GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0003105; P:negative regulation of glomerular filtration; IEA:Ensembl.
DR   GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0010652; P:positive regulation of cell communication by chemical coupling; IEA:Ensembl.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
DR   GO; GO:0006813; P:potassium ion transport; IEA:Ensembl.
DR   GO; GO:0003193; P:pulmonary valve formation; IMP:BHF-UCL.
DR   GO; GO:0086055; P:Purkinje myocyte to ventricular cardiac muscle cell communication by electrical coupling; NAS:BHF-UCL.
DR   GO; GO:0098910; P:regulation of atrial cardiac muscle cell action potential; IMP:BHF-UCL.
DR   GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IMP:BHF-UCL.
DR   GO; GO:0098904; P:regulation of AV node cell action potential; IMP:BHF-UCL.
DR   GO; GO:0098905; P:regulation of bundle of His cell action potential; IMP:BHF-UCL.
DR   GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
DR   GO; GO:0010649; P:regulation of cell communication by electrical coupling; IEA:Ensembl.
DR   GO; GO:0098906; P:regulation of Purkinje myocyte action potential; IMP:BHF-UCL.
DR   GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; ISS:BHF-UCL.
DR   GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISS:BHF-UCL.
DR   GO; GO:0086021; P:SA node cell to atrial cardiac muscle cell communication by electrical coupling; NAS:BHF-UCL.
DR   GO; GO:0042311; P:vasodilation; IEA:Ensembl.
DR   GO; GO:1990029; P:vasomotion; IEA:Ensembl.
DR   GO; GO:0003281; P:ventricular septum development; IMP:BHF-UCL.
DR   FunFam; 1.20.1440.80:FF:000001; Gap junction alpha-1; 1.
DR   Gene3D; 1.20.1440.80; Gap junction channel protein cysteine-rich domain; 1.
DR   InterPro; IPR000500; Connexin.
DR   InterPro; IPR002264; Connexin40.
DR   InterPro; IPR034634; Connexin_C.
DR   InterPro; IPR019570; Connexin_CCC.
DR   InterPro; IPR017990; Connexin_CS.
DR   InterPro; IPR013092; Connexin_N.
DR   InterPro; IPR038359; Connexin_N_sf.
DR   InterPro; IPR031862; Cx40_C.
DR   PANTHER; PTHR11984; CONNEXIN; 1.
DR   PANTHER; PTHR11984:SF13; GAP JUNCTION ALPHA-5 PROTEIN; 1.
DR   Pfam; PF00029; Connexin; 1.
DR   Pfam; PF16791; Connexin40_C; 1.
DR   PRINTS; PR00206; CONNEXIN.
DR   PRINTS; PR01135; CONNEXINA5.
DR   SMART; SM00037; CNX; 1.
DR   SMART; SM01089; Connexin_CCC; 1.
DR   SUPFAM; SSF118220; Connexin43; 1.
DR   PROSITE; PS00407; CONNEXINS_1; 1.
DR   PROSITE; PS00408; CONNEXINS_2; 1.
PE   1: Evidence at protein level;
KW   Atrial fibrillation; Cardiomyopathy; Cell junction; Cell membrane;
KW   Disease variant; Gap junction; Membrane; Phosphoprotein;
KW   Proteomics identification; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..358
FT                   /note="Gap junction alpha-5 protein"
FT                   /id="PRO_0000057819"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..76
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..164
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        186..205
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        227..358
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          319..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..345
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P28234"
FT   MOD_RES         357
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P28234"
FT   VARIANT         85
FT                   /note="V -> I (in ATFB11; dbSNP:rs387906613)"
FT                   /evidence="ECO:0000269|PubMed:20650941"
FT                   /id="VAR_066249"
FT   VARIANT         88
FT                   /note="P -> S (in ATRST1; somatic; dbSNP:rs121434558)"
FT                   /evidence="ECO:0000269|PubMed:16790700"
FT                   /id="VAR_035013"
FT   VARIANT         96
FT                   /note="A -> S (in ATRST1; dbSNP:rs121434557)"
FT                   /evidence="ECO:0000269|PubMed:16790700"
FT                   /id="VAR_035014"
FT   VARIANT         221
FT                   /note="L -> I (in ATFB11; dbSNP:rs387906614)"
FT                   /evidence="ECO:0000269|PubMed:20650941"
FT                   /id="VAR_066250"
FT   VARIANT         229
FT                   /note="L -> M (in ATFB11; dbSNP:rs387906615)"
FT                   /evidence="ECO:0000269|PubMed:20650941"
FT                   /id="VAR_066251"
SQ   SEQUENCE   358 AA;  40380 MW;  DE9DD863C130229A CRC64;
     MGDWSFLGNF LEEVHKHSTV VGKVWLTVLF IFRMLVLGTA AESSWGDEQA DFRCDTIQPG
     CQNVCYDQAF PISHIRYWVL QIIFVSTPSL VYMGHAMHTV RMQEKRKLRE AERAKEVRGS
     GSYEYPVAEK AELSCWEEGN GRIALQGTLL NTYVCSILIR TTMEVGFIVG QYFIYGIFLT
     TLHVCRRSPC PHPVNCYVSR PTEKNVFIVF MLAVAALSLL LSLAELYHLG WKKIRQRFVK
     PRQHMAKCQL SGPSVGIVQS CTPPPDFNQC LENGPGGKFF NPFSNNMASQ QNTDNLVTEQ
     VRGQEQTPGE GFIQVRYGQK PEVPNGVSPG HRLPHGYHSD KRRLSKASSK ARSDDLSV
//