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Database: UniProt
Entry: A0A1I7VI62_LOALO
LinkDB: A0A1I7VI62_LOALO
Original site: A0A1I7VI62_LOALO 
ID   A0A1I7VI62_LOALO        Unreviewed;       501 AA.
AC   A0A1I7VI62; A0A1S0U699;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN   Name=inx {ECO:0000256|RuleBase:RU010713};
GN   ORFNames=LOAG_02718 {ECO:0000313|EMBL:EFO25769.1,
GN   ECO:0000313|WBParaSite:EN70_2838};
OS   Loa loa (Eye worm) (Filaria loa).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX   NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_2838};
RN   [1] {ECO:0000313|EMBL:EFO25769.1, ECO:0000313|Proteomes:UP000095285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Loa loa.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:EN70_2838}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- FUNCTION: Structural component of the gap junctions.
CC       {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; JH712245; EFO25769.1; -; Genomic_DNA.
DR   RefSeq; XP_003138303.1; XM_003138255.1.
DR   AlphaFoldDB; A0A1I7VI62; -.
DR   STRING; 7209.A0A1I7VI62; -.
DR   EnsemblMetazoa; EFO25769.1; EFO25769.1; LOAG_02718.
DR   GeneID; 9940103; -.
DR   KEGG; loa:LOAG_02718; -.
DR   WBParaSite; EN70_2838; EN70_2838; EN70_2838.
DR   CTD; 9940103; -.
DR   eggNOG; ENOG502RRNR; Eukaryota.
DR   InParanoid; A0A1I7VI62; -.
DR   OMA; ESWINII; -.
DR   OrthoDB; 2883020at2759; -.
DR   Proteomes; UP000095285; 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:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000990; Innexin.
DR   PANTHER; PTHR11893; INNEXIN; 1.
DR   PANTHER; PTHR11893:SF9; INNEXIN-7; 1.
DR   Pfam; PF00876; Innexin; 1.
DR   PRINTS; PR01262; INNEXIN.
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}; 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:UP000095285};
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        53..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        143..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        237..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   REGION          432..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  58100 MW;  BBE1EF0B91341ACA CRC64;
     MECMLPMGFS GAWEQYAENF CWAQDTYFVP PKVFVEDISA EERRERRISY YQWMPFFLLF
     QAACFKAPTL IWKYFAGQSG MKLGQILRLS SDPANSSLEV KKGNIEALCI HLQGALRFHE
     RVKKKKLVPH KICRILNLKY ANYYVATIYI LAKLAFLANA IFQISLMTRY LLPELRNDYG
     LESWINIIWP KNVSPSWHYS GIFPLVTLCD FEVREMGNIQ THTVQCVLVV NLFTEKIFIL
     LWAWFMVLAA LTSLSVFNWI YLLTENCSKE HFILNHLEMS GTPFDKNDPQ NKEHVDCFLH
     KYLGTDGIFV LRMVANHADV VFATELIASL WRSHYVFEER RKNISQMDKV WPQHQQRLEM
     ALLEEAETAR KISSDALNVL QRKRSIFFDS PYFVKRGSPT GVTIPKVPSR NILGSPCLLS
     RNNSKDSIIP FSPRLGNHPR GSTFSTESQG KLRRRHSMED IDIGGGRVKF ADSSDEEDRE
     KEKEKGPKSF NMTRKSSIKI W
//
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