CXA4_RAT
ID CXA4_RAT Reviewed; 333 AA.
AC Q03190;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Gap junction alpha-4 protein;
DE AltName: Full=Connexin-37;
DE Short=Cx37;
GN Name=Gja4; Synonyms=Cxn-37;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RX PubMed=1370487; DOI=10.1016/s0021-9258(18)46052-8;
RA Haefliger J.-A., Bruzzone R., Jenkins N.A., Gilbert D.J., Copeland N.G.,
RA Paul D.L.;
RT "Four novel members of the connexin family of gap junction proteins.
RT Molecular cloning, expression, and chromosome mapping.";
RL J. Biol. Chem. 267:2057-2064(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Ovary;
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).
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 -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell
CC junction, gap junction.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000305}.
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DR EMBL; M76532; AAA40999.1; -; Genomic_DNA.
DR EMBL; BC078837; AAH78837.1; -; mRNA.
DR EMBL; BC086576; AAH86576.1; -; mRNA.
DR PIR; B42053; B42053.
DR RefSeq; NP_067686.1; NM_021654.2.
DR AlphaFoldDB; Q03190; -.
DR SMR; Q03190; -.
DR STRING; 10116.ENSRNOP00000019246; -.
DR iPTMnet; Q03190; -.
DR PhosphoSitePlus; Q03190; -.
DR PaxDb; Q03190; -.
DR PRIDE; Q03190; -.
DR Ensembl; ENSRNOT00000019246; ENSRNOP00000019246; ENSRNOG00000014357.
DR GeneID; 25655; -.
DR KEGG; rno:25655; -.
DR UCSC; RGD:2691; rat.
DR CTD; 2701; -.
DR RGD; 2691; Gja4.
DR eggNOG; ENOG502QU20; Eukaryota.
DR GeneTree; ENSGT01050000244914; -.
DR HOGENOM; CLU_037388_4_2_1; -.
DR InParanoid; Q03190; -.
DR OMA; KDPHVER; -.
DR OrthoDB; 903777at2759; -.
DR PhylomeDB; Q03190; -.
DR TreeFam; TF329606; -.
DR Reactome; R-RNO-190861; Gap junction assembly.
DR PRO; PR:Q03190; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000014357; Expressed in lung and 19 other tissues.
DR Genevisible; Q03190; RN.
DR GO; GO:0005922; C:connexin complex; IDA:RGD.
DR GO; GO:0005921; C:gap junction; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005243; F:gap junction channel activity; IBA:GO_Central.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; IMP:RGD.
DR GO; GO:0007154; P:cell communication; TAS:RGD.
DR GO; GO:0007267; P:cell-cell signaling; IMP:RGD.
DR GO; GO:0003158; P:endothelium development; IEP:RGD.
DR GO; GO:0048265; P:response to pain; IEP:RGD.
DR Gene3D; 1.20.1440.80; -; 1.
DR InterPro; IPR000500; Connexin.
DR InterPro; IPR002263; Connexin37.
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 Pfam; PF00029; Connexin; 1.
DR PRINTS; PR00206; CONNEXIN.
DR PRINTS; PR01134; CONNEXINA4.
DR SMART; SM00037; CNX; 1.
DR SMART; SM01089; Connexin_CCC; 1.
DR PROSITE; PS00407; CONNEXINS_1; 1.
DR PROSITE; PS00408; CONNEXINS_2; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Gap junction; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..333
FT /note="Gap junction alpha-4 protein"
FT /id="PRO_0000057817"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..76
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 292..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 333 AA; 37556 MW; ABAF5D9462CBBC97 CRC64;
MGDWGFLEKL LDQVQEHSTV VGKIWLTVLF IFRILILGLA GESVWGDEQS DFECNTAQPG
CTNVCYDQAF PISHIRYWVL QFLFVSTPTL IYLGHVIYLS RREERLRQKE GELRALPSKD
PHVERALAAI EHQMAKISVA EDGRLRIRGA LMGTYVISVL CKSVLEAGFL YGQWRLYGWT
MEPVFVCQRA PCPHVVDCYV SRPTEKTIFI IFMLVVGVIS LVLNLLELVH LLCRCVSREI
KARRDHDTRP AQGSASDPYP EQVFFYLPMG EGPSSPPCPT YNGLSSTEQN WANLTTEERL
TSTRPPPFVN AAPQGGQKSS SRPNSSASKK QYV
