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Database: UniProt
Entry: R0LKP9_ANAPL
LinkDB: R0LKP9_ANAPL
Original site: R0LKP9_ANAPL 
ID   R0LKP9_ANAPL            Unreviewed;       348 AA.
AC   R0LKP9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Pannexin {ECO:0000256|RuleBase:RU010713};
DE   Flags: Fragment;
GN   Name=PANX {ECO:0000256|RuleBase:RU010713};
GN   ORFNames=Anapl_03764 {ECO:0000313|EMBL:EOB06274.1};
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839 {ECO:0000313|EMBL:EOB06274.1, ECO:0000313|Proteomes:UP000296049};
RN   [1] {ECO:0000313|Proteomes:UP000296049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23749191; DOI=10.1038/ng.2657;
RA   Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA   Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA   Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA   Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA   Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA   Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA   Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA   Rao M., Pitel F., Wang J., Li N.;
RT   "The duck genome and transcriptome provide insight into an avian influenza
RT   virus reservoir species.";
RL   Nat. Genet. 45:776-783(2013).
CC   -!- FUNCTION: Structural component of the gap junctions and the
CC       hemichannels. {ECO:0000256|RuleBase:RU010713}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU010713};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU010713}. Cell
CC       junction, gap junction {ECO:0000256|RuleBase:RU010713}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00351, ECO:0000256|RuleBase:RU010713}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00351,
CC       ECO:0000256|RuleBase:RU010713}.
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DR   EMBL; KB742622; EOB06274.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0LKP9; -.
DR   GlyCosmos; R0LKP9; 1 site, No reported glycans.
DR   Proteomes; UP000296049; Unassembled WGS sequence.
DR   GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
DR   GO; GO:0006812; P:monoatomic cation transport; IEA:InterPro.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0032732; P:positive regulation of interleukin-1 production; IEA:InterPro.
DR   InterPro; IPR000990; Innexin.
DR   InterPro; IPR039099; Pannexin.
DR   PANTHER; PTHR15759; PANNEXIN; 1.
DR   PANTHER; PTHR15759:SF5; PANNEXIN-1; 1.
DR   Pfam; PF00876; Innexin; 1.
DR   PROSITE; PS51013; PANNEXIN; 1.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|RuleBase:RU010713};
KW   Gap junction {ECO:0000256|ARBA:ARBA00022868, ECO:0000256|PROSITE-
KW   ProRule:PRU00351}; Glycoprotein {ECO:0000256|PIRSR:PIRSR600990-51};
KW   Ion channel {ECO:0000256|RuleBase:RU010713};
KW   Ion transport {ECO:0000256|RuleBase:RU010713};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00351}; Reference proteome {ECO:0000313|Proteomes:UP000296049};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00351};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW   ProRule:PRU00351}; Transport {ECO:0000256|RuleBase:RU010713}.
FT   TRANSMEM        48..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        150..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        216..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   REGION          318..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600990-51"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EOB06274.1"
FT   NON_TER         348
FT                   /evidence="ECO:0000313|EMBL:EOB06274.1"
SQ   SEQUENCE   348 AA;  39576 MW;  5DF6363E2F41CC94 CRC64;
     GAQISCFAPS SFSWRQAAYV DSYCWAAVQQ KQPSQSDLEN IPLWLHKFFP YILLLVAILL
     YLPCLFWRFT AAPHLSSDLK FIMEELDKAY NRAIKAANSV RSGDARDPTD LIPTANENPA
     QSLWEISESH FKYPIVEQYL RTKKNSKCLI IKYIFCRLLT LVIIFLACLY LGYYISLSSL
     SDEFLCTIKT GILKNDTTVP EVVQCKLIAV GVFKVLSYIN LIVYLLVMPL VVYAMFVPFR
     WNSGVLKVYE ILPTFDVLKL KSKCLDDLSL YLLFLEENVS ELKSYKCLKV LENIAVSEKF
     DVMQLLINLG TIKTDTVDGK PGTAVPEKPE ETPVEELEKD ATELQGKV
//
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