UniProt: A0A2Y9E395

Database: UniProt
Entry: A0A2Y9E395_TRIMA

LinkDB:  A0A2Y9E395_TRIMA 
Original site:  A0A2Y9E395_TRIMA

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Ontology (6)   
   GO (6)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (4)   
   InterPro (2)   
   Pfam (1)   
   PROSITE (1)   
All databases (13)   

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ID   A0A2Y9E395_TRIMA        Unreviewed;       428 AA.
AC   A0A2Y9E395;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Pannexin {ECO:0000256|RuleBase:RU010713};
GN   Name=LOC101343896 {ECO:0000313|RefSeq:XP_004385608.1};
GN   Synonyms=PANX {ECO:0000256|RuleBase:RU010713};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004385608.1};
RN   [1] {ECO:0000313|RefSeq:XP_004385608.1}
RP   IDENTIFICATION.
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_004385608.1; XM_004385551.2.
DR   AlphaFoldDB; A0A2Y9E395; -.
DR   STRING; 127582.A0A2Y9E395; -.
DR   GlyCosmos; A0A2Y9E395; 1 site, No reported glycans.
DR   GeneID; 101343896; -.
DR   KEGG; tmu:101343896; -.
DR   InParanoid; A0A2Y9E395; -.
DR   OrthoDB; 2996841at2759; -.
DR   Proteomes; UP000248480; 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:UP000248480};
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        108..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        214..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          403..428
FT                   /note="Disordered"
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   428 AA;  48305 MW;  57A54C14E31A9B81 CRC64;
     MAIAHLATEY VFSDFLLKEP AEPKFKGLRL ELAVDKMITC IAVGLPLLLI SLAFAQEISI
     GTQISCFSPS SFSWRQAAFV DSYCWAAVQQ KDSLRSDTGN LPLWLHKFFP YILLLLAILL
     YLPSLFWRFT AAPHLCSDLK FIMEELDKVY NRAIKAAKSA RDLDVRDSTS PVTPVNENVG
     QSLWEIPESH FKYPIVEQYL KTKKNSNNLI VKYLSCRVLT LTITLLACIY LGYYFSLSSL
     SDEFVCSIKS GILKNDSTVP DQFQCKLIAV GIFQLLSFIN LAVYALLAPV LIYTLFVPFR
     QKTDVLKVYE ILPTFDILRF KSEGYNDLSL YNLFLEENIS ELKSYKCLKI LENIKSSGQG
     VDPMVLLTNL GMIKMDVVDS KTPQPAPSAV AREQENQMAE LQDLNVPSEK NANNGEANVR
     QRLMDSSC
//

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