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CXA1_MACFA
ID   CXA1_MACFA              Reviewed;         382 AA.
AC   Q4R4S7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Gap junction alpha-1 protein;
DE   AltName: Full=Connexin-43;
DE            Short=Cx43;
GN   Name=GJA1; ORFNames=QflA-10385;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Frontal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Gap junction protein that acts as a regulator of bladder
CC       capacity. A gap junction consists of a cluster of closely packed pairs
CC       of transmembrane channels, the connexons, through which materials of
CC       low MW diffuse from one cell to a neighboring cell. May play a critical
CC       role in the physiology of hearing by participating in the recycling of
CC       potassium to the cochlear endolymph. Negative regulator of bladder
CC       functional capacity: acts by enhancing intercellular electrical and
CC       chemical transmission, thus sensitizing bladder muscles to cholinergic
CC       neural stimuli and causing them to contract. May play a role in cell
CC       growth inhibition through the regulation of NOV expression and
CC       localization. Plays an essential role in gap junction communication in
CC       the ventricles (By similarity). {ECO:0000250|UniProtKB:P08050,
CC       ECO:0000250|UniProtKB:P23242}.
CC   -!- SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts
CC       with SGSM3 (By similarity). Interacts with RIC1/CIP150 (By similarity).
CC       Interacts with CNST and CSNK1D (By similarity). Interacts (via C-
CC       terminus) with TJP1. Interacts (via C-terminus) with SRC (via SH3
CC       domain). Interacts (not ubiquitinated) with UBQLN4 (via UBA domain) (By
CC       similarity). Interacts with NOV. Interacts with TMEM65 (By similarity).
CC       {ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:P17302,
CC       ECO:0000250|UniProtKB:P23242}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17302};
CC       Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction
CC       {ECO:0000250|UniProtKB:P17302}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P23242}. Note=Localizes at the intercalated disk
CC       (ICD) in cardiomyocytes and the proper localization at ICD is dependent
CC       on TMEM65. {ECO:0000250|UniProtKB:P23242}.
CC   -!- PTM: Phosphorylation at Ser-325, Ser-328 and Ser-330 by CK1 modulates
CC       gap junction assembly. Phosphorylated at Ser-368 by PRKCG;
CC       phosphorylation induces disassembly of gap junction plaques and
CC       inhibition of gap junction activity. Phosphorylation at Ser-368 by
CC       PRKCD triggers its internalization into small vesicles leading to
CC       proteasome-mediated degradation (By similarity).
CC       {ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:P17302,
CC       ECO:0000250|UniProtKB:Q6TYA7}.
CC   -!- PTM: Sumoylated with SUMO1, SUMO2 and SUMO3, which may regulate the
CC       level of functional Cx43 gap junctions at the plasma membrane. May be
CC       desumoylated by SENP1 or SENP2 (By similarity).
CC       {ECO:0000250|UniProtKB:P17302}.
CC   -!- PTM: S-nitrosylation at Cys-271 is enriched at the muscle endothelial
CC       gap junction in arteries, it augments channel permeability and may
CC       regulate of smooth muscle cell to endothelial cell communication.
CC       {ECO:0000250|UniProtKB:P23242}.
CC   -!- PTM: Acetylated in the developing cortex; leading to delocalization
CC       from the cell membrane. {ECO:0000250|UniProtKB:P23242}.
CC   -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB169817; BAE01898.1; -; mRNA.
DR   RefSeq; NP_001270691.1; NM_001283762.1.
DR   AlphaFoldDB; Q4R4S7; -.
DR   SMR; Q4R4S7; -.
DR   STRING; 9541.XP_005551754.1; -.
DR   GeneID; 101867099; -.
DR   CTD; 2697; -.
DR   eggNOG; ENOG502QRAE; Eukaryota.
DR   OrthoDB; 823525at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005922; C:connexin complex; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR   GO; GO:0060348; P:bone development; ISS:UniProtKB.
DR   GO; GO:0046849; P:bone remodeling; ISS:UniProtKB.
DR   GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR   GO; GO:0007507; P:heart development; IEA:InterPro.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   Gene3D; 1.20.1440.80; -; 1.
DR   Gene3D; 1.20.5.1130; -; 1.
DR   InterPro; IPR035091; Alpha_helix_dom_sf.
DR   InterPro; IPR000500; Connexin.
DR   InterPro; IPR002261; Connexin43.
DR   InterPro; IPR013124; Connexin43_C.
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   PANTHER; PTHR11984; PTHR11984; 1.
DR   PANTHER; PTHR11984:SF33; PTHR11984:SF33; 1.
DR   Pfam; PF00029; Connexin; 1.
DR   Pfam; PF03508; Connexin43; 1.
DR   PRINTS; PR00206; CONNEXIN.
DR   PRINTS; PR01132; CONNEXINA1.
DR   SMART; SM00037; CNX; 1.
DR   SMART; SM01089; Connexin_CCC; 1.
DR   SUPFAM; SSF118220; SSF118220; 1.
DR   PROSITE; PS00407; CONNEXINS_1; 1.
DR   PROSITE; PS00408; CONNEXINS_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell junction; Cell membrane; Disulfide bond;
KW   Endoplasmic reticulum; Gap junction; Isopeptide bond; Membrane;
KW   Phosphoprotein; Reference proteome; S-nitrosylation; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P08050"
FT   CHAIN           2..382
FT                   /note="Gap junction alpha-1 protein"
FT                   /id="PRO_0000313000"
FT   TOPO_DOM        2..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P08050"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..76
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P08050"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..155
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P08050"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        177..207
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P08050"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..382
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P08050"
FT   REGION          244..382
FT                   /note="Interaction with NOV"
FT                   /evidence="ECO:0000250|UniProtKB:P08050"
FT   REGION          264..382
FT                   /note="Interaction with UBQLN4"
FT                   /evidence="ECO:0000250|UniProtKB:P23242"
FT   REGION          279..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         5
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08050"
FT   MOD_RES         247
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P23242"
FT   MOD_RES         255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17302"
FT   MOD_RES         262
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17302"
FT   MOD_RES         271
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P23242"
FT   MOD_RES         275
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P23242"
FT   MOD_RES         306
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23242"
FT   MOD_RES         314
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17302"
FT   MOD_RES         325
FT                   /note="Phosphoserine; by CK1"
FT                   /evidence="ECO:0000250|UniProtKB:P17302"
FT   MOD_RES         326
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P23242"
FT   MOD_RES         328
FT                   /note="Phosphoserine; by CK1"
FT                   /evidence="ECO:0000250|UniProtKB:P17302"
FT   MOD_RES         330
FT                   /note="Phosphoserine; by CK1"
FT                   /evidence="ECO:0000250|UniProtKB:P17302"
FT   MOD_RES         344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17302"
FT   MOD_RES         365
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23242"
FT   MOD_RES         368
FT                   /note="Phosphoserine; by PKC/PRKCG and PKC/PRKCD"
FT                   /evidence="ECO:0000250|UniProtKB:P23242"
FT   MOD_RES         369
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23242"
FT   MOD_RES         373
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08050"
FT   DISULFID        54..192
FT                   /evidence="ECO:0000250|UniProtKB:P17302"
FT   DISULFID        187..198
FT                   /evidence="ECO:0000250|UniProtKB:P17302"
FT   CROSSLNK        144
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250|UniProtKB:P17302"
FT   CROSSLNK        237
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250|UniProtKB:P17302"
SQ   SEQUENCE   382 AA;  43036 MW;  6C98B9A614612C4A CRC64;
     MGDWSALGKL LDKVQAYSTA GGKVWLSVLF IFRILLLGTA VESAWGDEQS AFRCNTQQPG
     CENVCYDKSF PISHVRFWVL QIIFVSVPTL LYLAHVFYVM RKEEKLNKKE EELKVAQTDG
     VNVEMHLKQI EIKKFKYGIE EHGKVKMRGG LLRTYIISIL FKSIFEVAFL LIQWYIYGFS
     LSAVYTCKRD PCPHQVDCFL SRPTEKTIFI IFMLVVSLVS LALNIIELFY VFFKGVKDRV
     KGKSDPYHAT SGALSPTKDC GSQKYAYFNG CSSPTAPLSP MSPPGYKPVT GDRNNSSCRN
     YNKQASEQNW ANYSAEQNRM GQAGSTISNS HAQPFDFPDD NQNSKKLAAG HELQPLAIVD
     QRPSSRASSR ASSRPRPDDL EI
 
 
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