ID A0A2U3YCJ7_LEPWE Unreviewed; 427 AA.
AC A0A2U3YCJ7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Pannexin {ECO:0000256|RuleBase:RU010713};
GN Name=PANX1 {ECO:0000313|RefSeq:XP_006741427.1};
GN Synonyms=PANX {ECO:0000256|RuleBase:RU010713};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006741427.1};
RN [1] {ECO:0000313|RefSeq:XP_006741427.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006741427.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- PTM: S-nitrosylation inhibits channel currents and ATP release.
CC {ECO:0000256|PIRSR:PIRSR600990-50}.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00351, ECO:0000256|RuleBase:RU010713}.
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DR RefSeq; XP_006741427.1; XM_006741364.2.
DR AlphaFoldDB; A0A2U3YCJ7; -.
DR STRING; 9713.A0A2U3YCJ7; -.
DR GlyCosmos; A0A2U3YCJ7; 1 site, No reported glycans.
DR GeneID; 102731695; -.
DR KEGG; lww:102731695; -.
DR CTD; 24145; -.
DR OrthoDB; 2996841at2759; -.
DR Proteomes; UP000245341; Unplaced.
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:UP000245341};
KW S-nitrosylation {ECO:0000256|PIRSR:PIRSR600990-50};
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 33..55
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 107..129
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 210..235
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 267..297
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT REGION 383..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600990-50"
FT MOD_RES 347
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600990-50"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600990-51"
SQ SEQUENCE 427 AA; 48204 MW; F4CAF9C47D492400 CRC64;
MAIAHLATEY VFSDFLLKEP SEPKFKGLRL ELAVDKMVTC IAVGLPLLLI SLAFAQEISI
GTQISCFSPS SFSWRQAAFV DSYCWAAVQQ ASLQGDAGRL PLCLHKFFPY ILLLVAILLY
LPSLFWRFAA TPHLCSDLKF IMEELDKVYN RSIQAAKSMY DDQDMRDGAG PVSGLPENMG
QSLWEISESH FKYPIVEQYL KTKKNCKNLI IKYISCRLLT LSIILSACAY LGYYFSLSSL
SDEFVCNIKS GILRNDSSIP DRFQCKLIAV GIFQLLSLIN LVVYVLLAPV VIYTLFVPHR
QKTDVLRVYE ILPTFDVLHF KSEGYNDLSL YNLFLEENVS ELKSYRCLKV LENIKSSGQG
INPMLLLTHL GTIKMDVMDG KRPEPVEMTT EEPGDPMTEL KDSNEPSEIK VNNGETNARQ
RLLDSSC
//
