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Gap junction alpha-1 protein (Connexin-43) (Cx43) (Gap junction 43 kDa heart protein)

 CXA1_RAT                Reviewed;         382 AA.
P08050; Q53ZE1;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
27-SEP-2017, entry version 178.
RecName: Full=Gap junction alpha-1 protein;
AltName: Full=Connexin-43;
Short=Cx43;
AltName: Full=Gap junction 43 kDa heart protein;
Name=Gja1; Synonyms=Cxn-43;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2826492; DOI=10.1083/jcb.105.6.2621;
Beyer E.C., Paul D.L., Goodenough D.A.;
"Connexin43: a protein from rat heart homologous to a gap junction
protein from liver.";
J. Cell Biol. 105:2621-2629(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Uterus;
PubMed=1852114;
Lang L.M., Beyer E.C., Schwartz A.L., Gitlin J.D.;
"Molecular cloning of a rat uterine gap junction protein and analysis
of gene expression during gestation.";
Am. J. Physiol. 260:E787-E793(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
Ma L.X., Peng Y.W.;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-33.
TISSUE=Heart;
PubMed=2987225;
Nicholson B.J., Gros D.B., Kent S.B.H., Hood L.E., Revel J.-P.;
"The Mr 28,000 gap junction proteins from rat heart and liver are
different but related.";
J. Biol. Chem. 260:6514-6517(1985).
[6]
PROTEIN SEQUENCE OF 2-16.
TISSUE=Brain;
PubMed=1652440; DOI=10.1111/j.1432-1033.1991.tb21075.x;
Dupont E., el Aoumari A., Fromaget C., Briand J.-C., Gros D.;
"Affinity purification of a rat-brain junctional protein, connexin
43.";
Eur. J. Biochem. 200:263-270(1991).
[7]
DISULFIDE BONDS.
PubMed=1651718; DOI=10.1016/0006-291X(91)91037-D;
John S.A., Revel J.-P.;
"Connexon integrity is maintained by non-covalent bonds:
intramolecular disulfide bonds link the extracellular domains in rat
connexin-43.";
Biochem. Biophys. Res. Commun. 178:1312-1318(1991).
[8]
TOPOLOGY.
PubMed=1371548; DOI=10.1016/0022-2836(92)90253-G;
Yeager M., Gilula N.B.;
"Membrane topology and quaternary structure of cardiac gap junction
ion channels.";
J. Mol. Biol. 223:929-948(1992).
[9]
PHOSPHORYLATION AT SER-365; SER-368; SER-369 AND SER-373.
PubMed=12417300; DOI=10.1016/S0014-5793(02)03441-5;
Yogo K., Ogawa T., Akiyama M., Ishida N., Takeya T.;
"Identification and functional analysis of novel phosphorylation sites
in Cx43 in rat primary granulosa cells.";
FEBS Lett. 531:132-136(2002).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NOV.
PubMed=15181016; DOI=10.1074/jbc.M404073200;
Gellhaus A., Dong X., Propson S., Maass K., Klein-Hitpass L.,
Kibschull M., Traub O., Willecke K., Perbal B., Lye S.J.,
Winterhager E.;
"Connexin43 interacts with NOV: a possible mechanism for negative
regulation of cell growth in choriocarcinoma cells.";
J. Biol. Chem. 279:36931-36942(2004).
[11]
SUBCELLULAR LOCATION, AND INTERACTION WITH NOV.
PubMed=15213231; DOI=10.1074/jbc.M403952200;
Fu C.T., Bechberger J.F., Ozog M.A., Perbal B., Naus C.C.;
"CCN3 (NOV) interacts with connexin43 in C6 glioma cells: possible
mechanism of connexin-mediated growth suppression.";
J. Biol. Chem. 279:36943-36950(2004).
[12]
INTERACTION WITH UBQLN4.
PubMed=20127391; DOI=10.1007/s10858-010-9397-9;
Kieken F., Spagnol G., Su V., Lau A.F., Sorgen P.L.;
"NMR structure note: UBA domain of CIP75.";
J. Biomol. NMR 46:245-250(2010).
[13]
INDUCTION.
PubMed=22549838; DOI=10.1038/ncomms1812;
Negoro H., Kanematsu A., Doi M., Suadicani S.O., Matsuo M.,
Imamura M., Okinami T., Nishikawa N., Oura T., Matsui S., Seo K.,
Tainaka M., Urabe S., Kiyokage E., Todo T., Okamura H., Tabata Y.,
Ogawa O.;
"Involvement of urinary bladder Connexin43 and the circadian clock in
coordination of diurnal micturition rhythm.";
Nat. Commun. 3:809-809(2012).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-257; SER-306;
SER-314; SER-325; THR-326; SER-328 AND SER-330, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[15]
PHOSPHORYLATION AT SER-368, AND MUTAGENESIS OF SER-368.
PubMed=24500718; DOI=10.1074/jbc.M113.533265;
Cone A.C., Cavin G., Ambrosi C., Hakozaki H., Wu-Zhang A.X.,
Kunkel M.T., Newton A.C., Sosinsky G.E.;
"Protein kinase Cdelta-mediated phosphorylation of Connexin43 gap
junction channels causes movement within gap junctions followed by
vesicle internalization and protein degradation.";
J. Biol. Chem. 289:8781-8798(2014).
[16]
STRUCTURE BY NMR OF 255-381, AND INTERACTION WITH TJP1 AND SRC.
PubMed=15492000; DOI=10.1074/jbc.M409552200;
Sorgen P.L., Duffy H.S., Sahoo P., Coombs W., Delmar M., Spray D.C.;
"Structural changes in the carboxyl terminus of the gap junction
protein connexin43 indicates signaling between binding domains for c-
Src and zonula occludens-1.";
J. Biol. Chem. 279:54695-54701(2004).
[17]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 374-382 IN COMPLEX WITH TJP1,
SUBCELLULAR LOCATION, AND INTERACTION WITH TJP1.
PubMed=18636092; DOI=10.1038/emboj.2008.138;
Chen J., Pan L., Wei Z., Zhao Y., Zhang M.;
"Domain-swapped dimerization of ZO-1 PDZ2 generates specific and
regulatory connexin43-binding sites.";
EMBO J. 27:2113-2123(2008).
-!- FUNCTION: Gap junction protein that acts as a regulator of bladder
capacity. A gap junction consists of a cluster of closely packed
pairs of transmembrane channels, the connexons, through which
materials of low MW diffuse from one cell to a neighboring cell.
Negative regulator of bladder functional capacity: acts by
enhancing intercellular electrical and chemical transmission, thus
sensitizing bladder muscles to cholinergic neural stimuli and
causing them to contract (By similarity). May play a role in cell
growth inhibition through the regulation of NOV expression and
localization (PubMed:15181016). Plays an essential role in gap
junction communication in the ventricles (By similarity).
{ECO:0000250|UniProtKB:P23242, ECO:0000269|PubMed:15181016}.
-!- SUBUNIT: A connexon is composed of a hexamer of connexins.
Interacts with SGSM3 (By similarity). Interacts with RIC1/CIP150
(By similarity). Interacts with CNST and CSNK1D (By similarity).
Interacts (via C-terminus) with TJP1. Interacts (via C-terminus)
with SRC (via SH3 domain). Interacts (not ubiquitinated) with
UBQLN4 (via UBA domain). Interacts with NOV (PubMed:15181016,
PubMed:15213231). Interacts with TMEM65 (By similarity).
{ECO:0000250|UniProtKB:P17302, ECO:0000250|UniProtKB:P23242,
ECO:0000269|PubMed:15181016, ECO:0000269|PubMed:15213231,
ECO:0000269|PubMed:15492000, ECO:0000269|PubMed:18636092,
ECO:0000269|PubMed:20127391}.
-!- INTERACTION:
Q63664:Kcnj8; NbExp=4; IntAct=EBI-476947, EBI-6991142;
Q8VCZ6:Sgsm3 (xeno); NbExp=4; IntAct=EBI-476947, EBI-525155;
Q9NRR5:UBQLN4 (xeno); NbExp=2; IntAct=EBI-476947, EBI-711226;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18636092};
Multi-pass membrane protein {ECO:0000255}. Cell junction, gap
junction {ECO:0000269|PubMed:15213231,
ECO:0000269|PubMed:18636092}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:P23242}. Note=Localizes at the intercalated
disk (ICD) in cardiomyocytes and the proper localization at ICD is
dependent on TMEM65. {ECO:0000250|UniProtKB:P23242}.
-!- INDUCTION: In bladder smooth muscle cells, exhibits night/day
variations with low levels during the sleep phase, at circadian
time (CT) 4-8 (at protein level). Expression starts to increase
around CT12 and forms a plateau during the active phase (CT16-24)
(at protein level). {ECO:0000269|PubMed:22549838}.
-!- PTM: Contains at least one intramolecular disulfide bond.
-!- PTM: Phosphorylation at Ser-325, Ser-328 and Ser-330 by CK1
modulates gap junction assembly. Phosphorylated at Ser-368 by
PRKCG; phosphorylation induces disassembly of gap junction plaques
and inhibition of gap junction activity (By similarity).
Phosphorylation at Ser-368 by PRKCD triggers its internalization
into small vesicles leading to proteasome-mediated degradation
(PubMed:24500718). {ECO:0000250|UniProtKB:P17302,
ECO:0000250|UniProtKB:Q6TYA7, ECO:0000269|PubMed:24500718}.
-!- PTM: Sumoylated with SUMO1, SUMO2 and SUMO3, which may regulate
the level of functional Cx43 gap junctions at the plasma membrane.
May be desumoylated by SENP1 or SENP2 (By similarity).
{ECO:0000250}.
-!- PTM: S-nitrosylation at Cys-271 is enriched at the muscle
endothelial gap junction in arteries, it augments channel
permeability and may regulate of smooth muscle cell to endothelial
cell communication.
-!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
subfamily. {ECO:0000305}.
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EMBL; X06656; CAA29855.1; -; mRNA.
EMBL; AY324140; AAP88589.1; -; mRNA.
EMBL; BC081842; AAH81842.1; -; mRNA.
PIR; A24047; A24047.
PIR; S00532; S00532.
RefSeq; NP_036699.1; NM_012567.2.
UniGene; Rn.10346; -.
PDB; 1R5S; NMR; -; A=255-382.
PDB; 2N8T; NMR; -; B=276-289.
PDB; 3CYY; X-ray; 2.40 A; C/D=374-382.
PDBsum; 1R5S; -.
PDBsum; 2N8T; -.
PDBsum; 3CYY; -.
DisProt; DP00278; -.
ProteinModelPortal; P08050; -.
SMR; P08050; -.
BioGrid; 246562; 119.
CORUM; P08050; -.
DIP; DIP-34793N; -.
IntAct; P08050; 12.
MINT; MINT-1791096; -.
STRING; 10116.ENSRNOP00000001054; -.
TCDB; 1.A.24.1.1; the gap junction-forming connexin (connexin) family.
iPTMnet; P08050; -.
PhosphoSitePlus; P08050; -.
PaxDb; P08050; -.
PRIDE; P08050; -.
Ensembl; ENSRNOT00000001054; ENSRNOP00000001054; ENSRNOG00000000805.
GeneID; 24392; -.
KEGG; rno:24392; -.
UCSC; RGD:2690; rat.
CTD; 2697; -.
RGD; 2690; Gja1.
eggNOG; ENOG410IF97; Eukaryota.
eggNOG; ENOG4110JTW; LUCA.
GeneTree; ENSGT00840000129674; -.
HOGENOM; HOG000231127; -.
HOVERGEN; HBG009576; -.
InParanoid; P08050; -.
KO; K07372; -.
OMA; GANVDMH; -.
OrthoDB; EOG091G0FKH; -.
PhylomeDB; P08050; -.
TreeFam; TF329606; -.
Reactome; R-RNO-190704; Oligomerization of connexins into connexons.
Reactome; R-RNO-190827; Transport of connexins along the secretory pathway.
Reactome; R-RNO-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
Reactome; R-RNO-190861; Gap junction assembly.
Reactome; R-RNO-190873; Gap junction degradation.
Reactome; R-RNO-191647; c-src mediated regulation of Cx43 function and closure of gap junctions.
Reactome; R-RNO-196025; Formation of annular gap junctions.
Reactome; R-RNO-215126; Transport of connexins along the secretory pathway.
EvolutionaryTrace; P08050; -.
PRO; PR:P08050; -.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000000805; -.
Genevisible; P08050; RN.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005922; C:connexin complex; IDA:CAFA.
GO; GO:0043292; C:contractile fiber; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005769; C:early endosome; IDA:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005768; C:endosome; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005916; C:fascia adherens; IDA:RGD.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0005921; C:gap junction; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
GO; GO:0005882; C:intermediate filament; IEA:Ensembl.
GO; GO:0005770; C:late endosome; IDA:RGD.
GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
GO; GO:0005764; C:lysosome; IDA:RGD.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
GO; GO:0005771; C:multivesicular body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
GO; GO:0071253; F:connexin binding; IPI:RGD.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0005243; F:gap junction channel activity; IDA:CAFA.
GO; GO:1903763; F:gap junction channel activity involved in cell communication by electrical coupling; IEA:Ensembl.
GO; GO:0015075; F:ion transmembrane transporter activity; IEA:Ensembl.
GO; GO:0030165; F:PDZ domain binding; IPI:CAFA.
GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0017124; F:SH3 domain binding; IDA:RGD.
GO; GO:0004871; F:signal transducer activity; IEA:Ensembl.
GO; GO:0007512; P:adult heart development; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IMP:RGD.
GO; GO:0015867; P:ATP transport; IMP:RGD.
GO; GO:0003294; P:atrial ventricular junction remodeling; IEA:Ensembl.
GO; GO:0048514; P:blood vessel morphogenesis; IEA:Ensembl.
GO; GO:0061337; P:cardiac conduction; IEA:Ensembl.
GO; GO:0007154; P:cell communication; IMP:RGD.
GO; GO:0010643; P:cell communication by chemical coupling; IEA:Ensembl.
GO; GO:0007267; P:cell-cell signaling; IDA:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEP:RGD.
GO; GO:0071467; P:cellular response to pH; IEA:Ensembl.
GO; GO:0002544; P:chronic inflammatory response; IMP:RGD.
GO; GO:0046697; P:decidualization; IEP:RGD.
GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0003158; P:endothelium development; IEP:RGD.
GO; GO:1905867; P:epididymis development; IEP:RGD.
GO; GO:0002070; P:epithelial cell maturation; IEA:Ensembl.
GO; GO:0016264; P:gap junction assembly; TAS:UniProtKB.
GO; GO:0007507; P:heart development; IEP:RGD.
GO; GO:0001947; P:heart looping; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
GO; GO:0060156; P:milk ejection reflex; IEA:Ensembl.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IMP:RGD.
GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:RGD.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IDA:RGD.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:RGD.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0061045; P:negative regulation of wound healing; IMP:RGD.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:RGD.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:2000987; P:positive regulation of behavioral fear response; IMP:RGD.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IMP:RGD.
GO; GO:0010652; P:positive regulation of cell communication by chemical coupling; IMP:RGD.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0003104; P:positive regulation of glomerular filtration; IMP:RGD.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:RGD.
GO; GO:0045844; P:positive regulation of striated muscle tissue development; IEA:Ensembl.
GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
GO; GO:0051259; P:protein oligomerization; IDA:RGD.
GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IEA:Ensembl.
GO; GO:2000810; P:regulation of bicellular tight junction assembly; IMP:RGD.
GO; GO:0030500; P:regulation of bone mineralization; IEA:Ensembl.
GO; GO:0046850; P:regulation of bone remodeling; IEA:Ensembl.
GO; GO:0051924; P:regulation of calcium ion transport; IMP:RGD.
GO; GO:0022898; P:regulation of transmembrane transporter activity; IMP:CAFA.
GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IEA:Ensembl.
GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IEA:Ensembl.
GO; GO:0034405; P:response to fluid shear stress; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0002931; P:response to ischemia; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0009268; P:response to pH; IDA:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
GO; GO:0055085; P:transmembrane transport; IDA:CAFA.
GO; GO:0010232; P:vascular transport; IMP:RGD.
Gene3D; 1.20.5.1130; -; 1.
InterPro; IPR035091; Alpha_helix_domain.
InterPro; IPR000500; Connexin.
InterPro; IPR002261; Connexin43.
InterPro; IPR013124; Connexin43_C.
InterPro; IPR034634; Connexin_C.
InterPro; IPR019570; Connexin_CCC.
InterPro; IPR017990; Connexin_CS.
InterPro; IPR013092; Connexin_N.
PANTHER; PTHR11984; PTHR11984; 1.
PANTHER; PTHR11984:SF70; PTHR11984:SF70; 1.
Pfam; PF00029; Connexin; 1.
Pfam; PF03508; Connexin43; 1.
PRINTS; PR00206; CONNEXIN.
PRINTS; PR01132; CONNEXINA1.
SMART; SM00037; CNX; 1.
SMART; SM01089; Connexin_CCC; 1.
SUPFAM; SSF118220; SSF118220; 1.
PROSITE; PS00407; CONNEXINS_1; 1.
PROSITE; PS00408; CONNEXINS_2; 1.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Gap junction; Isopeptide bond; Membrane; Phosphoprotein;
Reference proteome; S-nitrosylation; Transmembrane;
Transmembrane helix; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1652440,
ECO:0000269|PubMed:2987225}.
CHAIN 2 382 Gap junction alpha-1 protein.
/FTId=PRO_0000057804.
TOPO_DOM 2 13 Cytoplasmic.
{ECO:0000305|PubMed:1371548}.
TRANSMEM 14 36 Helical. {ECO:0000305}.
TOPO_DOM 37 76 Extracellular.
{ECO:0000305|PubMed:1371548}.
TRANSMEM 77 99 Helical. {ECO:0000305}.
TOPO_DOM 100 154 Cytoplasmic.
{ECO:0000305|PubMed:1371548}.
TRANSMEM 155 177 Helical. {ECO:0000305}.
TOPO_DOM 178 208 Extracellular.
{ECO:0000305|PubMed:1371548}.
TRANSMEM 209 231 Helical. {ECO:0000305}.
TOPO_DOM 232 382 Cytoplasmic.
{ECO:0000305|PubMed:1371548}.
REGION 244 382 Interaction with NOV.
{ECO:0000269|PubMed:15181016,
ECO:0000269|PubMed:15213231}.
REGION 264 382 Interaction with UBQLN4.
{ECO:0000250|UniProtKB:P23242}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 247 247 Phosphotyrosine.
{ECO:0000250|UniProtKB:P23242}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000250|UniProtKB:P17302}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 262 262 Phosphoserine.
{ECO:0000250|UniProtKB:P17302}.
MOD_RES 271 271 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P23242}.
MOD_RES 275 275 Phosphothreonine.
{ECO:0000250|UniProtKB:P23242}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 326 326 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000269|PubMed:12417300}.
MOD_RES 368 368 Phosphoserine; by PKC/PRKCG and
PKC/PRKCD. {ECO:0000269|PubMed:24500718,
ECO:0000305|PubMed:12417300}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000269|PubMed:12417300}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000269|PubMed:12417300}.
DISULFID 54 192 {ECO:0000250}.
DISULFID 187 198 {ECO:0000250}.
CROSSLNK 144 144 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 237 237 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
MUTAGEN 368 368 S->A: Loss of phosphorylation by
PKC/PRKCD. {ECO:0000269|PubMed:24500718}.
CONFLICT 2 2 G -> A (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 16 16 A -> T (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 28 28 V -> I (in Ref. 5; AA sequence).
{ECO:0000305}.
TURN 256 259 {ECO:0000244|PDB:1R5S}.
STRAND 263 265 {ECO:0000244|PDB:1R5S}.
STRAND 283 285 {ECO:0000244|PDB:2N8T}.
STRAND 297 300 {ECO:0000244|PDB:1R5S}.
HELIX 317 325 {ECO:0000244|PDB:1R5S}.
HELIX 342 348 {ECO:0000244|PDB:1R5S}.
TURN 349 352 {ECO:0000244|PDB:1R5S}.
STRAND 360 362 {ECO:0000244|PDB:1R5S}.
TURN 366 370 {ECO:0000244|PDB:1R5S}.
STRAND 379 381 {ECO:0000244|PDB:3CYY}.
SEQUENCE 382 AA; 43031 MW; 0196416EA6A69490 CRC64;
MGDWSALGKL LDKVQAYSTA GGKVWLSVLF IFRILLLGTA VESAWGDEQS AFRCNTQQPG
CENVCYDKSF PISHVRFWVL QIIFVSVPTL LYLAHVFYVM RKEEKLNKKE EELKVAQTDG
VNVEMHLKQI EIKKFKYGIE EHGKVKMRGG LLRTYIISIL FKSVFEVAFL LIQWYIYGFS
LSAVYTCKRD PCPHQVDCFL SRPTEKTIFI IFMLVVSLVS LALNIIELFY VFFKGVKDRV
KGRSDPYHAT TGPLSPSKDC GSPKYAYFNG CSSPTAPLSP MSPPGYKLVT GDRNNSSCRN
YNKQASEQNW ANYSAEQNRM GQAGSTISNS HAQPFDFPDD NQNAKKVAAG HELQPLAIVD
QRPSSRASSR ASSRPRPDDL EI


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