(data stored in ACNUC25403 zone)

HOGENOM: MOUSE9_PE146

ID   MOUSE9_PE146                         STANDARD;      PRT;   426 AA.
AC   MOUSE9_PE146; Q9JIP4; Q5RL18; Q9CXS7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Pannexin-1; (MOUSE9.PE146).
GN   Name=Panx1;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE9.PE146.
CC       Mus musculus chromosome 9 NCBIM37  sequence 1..124076172 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:PANX1_MOUSE
CC   -!- FUNCTION: Structural component of the gap junctions and the
CC       hemichannels. May play a role as a Ca(2+)-leak channel to regulate
CC       ER Ca(2+) homeostasis (By similarity).
CC   -!- SUBUNIT: Homohexamer (By similarity). Forms homomeric or
CC       PANX1/PANX2-heteromeric intercellular channels on coexpression in
CC       paired Xenopus oocytes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential). Cell junction, gap junction. Endoplasmic reticulum
CC       membrane; Multi-pass membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed, including in cartilage,
CC       skin, spleen and brain.
CC   -!- PTM: N-glycosylation may play a role in cell surface targeting.
CC   -!- SIMILARITY: Belongs to the pannexin family.
CC   -!- GENE_FAMILY: HOG000063721 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000031934;ENSMUST00000056755;ENSMUSP00000053557.
DR   EMBL; AF207817; - ;
DR   EMBL; AK014033; - ;
DR   EMBL; AK053871; - ;
DR   EMBL; AK089764; - ;
DR   EMBL; AK156194; - ;
DR   EMBL; BC049074; - ;
DR   EMBL; CH466522; - ;
DR   EMBL; EU446265; - ;
DR   UniProtKB/Swiss-Prot; Q9JIP4; Q5RL18; Q9CXS7; -.
DR   EMBL; AF207817; AAF75838.1; -; mRNA.
DR   EMBL; AK014033; BAB29125.1; -; mRNA.
DR   EMBL; AK053871; BAC35567.1; -; mRNA.
DR   EMBL; AK089764; BAC40956.1; -; mRNA.
DR   EMBL; CH466522; EDL25014.1; -; Genomic_DNA.
DR   EMBL; BC049074; AAH49074.1; -; mRNA.
DR   IPI; IPI00228875; -.
DR   RefSeq; NP_062355.2; NM_019482.2.
DR   UniGene; Mm.142253; -.
DR   STRING; Q9JIP4; -.
DR   PhosphoSite; Q9JIP4; -.
DR   PRIDE; Q9JIP4; -.
DR   Ensembl; ENSMUST00000164273; ENSMUSP00000126405; ENSMUSG00000031934.
DR   GeneID; 55991; -.
DR   KEGG; mmu:55991; -.
DR   CTD; 24145; -.
DR   MGI; MGI:1860055; Panx1.
DR   GeneTree; ENSGT00390000009703; -.
DR   InParanoid; Q9JIP4; -.
DR   OrthoDB; EOG4HT8SW; -.
DR   ArrayExpress; Q9JIP4; -.
DR   Bgee; Q9JIP4; -.
DR   CleanEx; MM_PANX1; -.
DR   Genevestigator; Q9JIP4; -.
DR   GermOnline; ENSMUSG00000031934; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0055077; F:gap junction hemi-channel activity; ISS:UniProtKB.
DR   GO; GO:0022840; F:leak channel activity; ISS:UniProtKB.
DR   GO; GO:0050717; P:positive regulation of interleukin-1 alpha secretion; IMP:MGI.
DR   GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IMP:MGI.
DR   GO; GO:0034214; P:protein hexamerization; ISS:UniProtKB.
DR   GO; GO:0033198; P:response to ATP; IMP:MGI.
DR   InterPro; IPR000990; Innexin.
DR   Pfam; PF00876; Innexin; 1.
DR   PROSITE; PS51013; PANNEXIN; 1.
DR   HOGENOMDNA; MOUSE9.PE146; -.
KW   ENSMUSG000000319345old_1320000031; ENSMUSP000000535571old_1320000031;
KW   B1PL19_MOUSE; Q3U181_MOUSE; Q5RL18_MOUSE; AF207817; AK014033; AK053871;
KW   AK156194; BC049074; CH466522; EU446265;
KW   Calcium; Calcium channel; Calcium transport; Cell junction;
KW   Cell membrane; Complete proteome; Endoplasmic reticulum; Gap junction;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   426 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAIAHLATEY VFSDFLLKEP TEPKFKGLRL ELAVDKMVTC IAVGLPLLLI SLAFAQEISI
     GTQISCFSPS SFSWRQAAFV DSYCWAAVQQ KSSLQSESGN LPLWLHKFFP YILLLFAILL
     YLPALFWRFS AAPHLCSDLK FIMEELDKVY NRAIKAAKSA RDLDLRDGPG PPGVTENVGQ
     SLWEISESHF KYPIVEQYLK TKKNSSHLIM KYISCRLVTF VVILLACIYL SYYFSLSSLS
     DEFLCSIKSG VLKNDSTIPD RFQCKLIAVG IFQLLSLINL IVYALLIPVV VYTFFIPFRQ
     KTDILKVYEI LPTFDVLHFK SEGYNDLSLY NLFLEENISE LKSYKCLKVL ENIKSNGQGI
     DPMLLLTNLG MIKMDIIDGK IPTSLQTKGE DQGSQRVEFK DLDLSSEAAA NNGEKNSRQR
     LLNPSC
//

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