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Database: UniProt
Entry: A0A183P320_9TREM
LinkDB: A0A183P320_9TREM
Original site: A0A183P320_9TREM 
ID   A0A183P320_9TREM        Unreviewed;       542 AA.
AC   A0A183P320;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN   Name=inx {ECO:0000256|RuleBase:RU010713};
GN   ORFNames=SMTD_LOCUS8756 {ECO:0000313|EMBL:VDP46362.1};
OS   Schistosoma mattheei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=31246 {ECO:0000313|WBParaSite:SMTD_0000875501-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMTD_0000875501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP46362.1, ECO:0000313|Proteomes:UP000269396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Denwood {ECO:0000313|EMBL:VDP46362.1}, and Denwood, Zambia
RC   {ECO:0000313|Proteomes:UP000269396};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; UZAL01029159; VDP46362.1; -; Genomic_DNA.
DR   STRING; 31246.A0A183P320; -.
DR   WBParaSite; SMTD_0000875501-mRNA-1; SMTD_0000875501-mRNA-1; SMTD_0000875501.
DR   Proteomes; UP000269396; 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:SF36; INNEXIN; 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:UP000269396};
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        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   REGION          300..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   542 AA;  62249 MW;  8559026D002D263F CRC64;
     MLNPEHKTIT VHFKRQRYIK AISIGRVITN HECQRRYNPS YYQLKLKLIF VAQLWTVMDL
     ASKAGDLEET LHSSVNHLEY IVKHLEDALI IRHRYKQSRK NNSSISTAQT SVSSPANTNE
     QIVNKDNSWY AILPLTISNR SRIPGPRPCS PQSSSYLNGL YLIIKALYVF NSTGQLFLLA
     RFLGQTTIFF GPQMLIDLII GTQWYQSGNF PRVSFCDLDM RKMGKNYHRY TLQCVLSINM
     FNEKIFIFLW FWFIGITLIN IHSFLRWCCR STFQTSRVCF IRSLLFNKIS MKINNNNINN
     NKSDYSSNNT NSNVTQNSDY QSTSQQSTTI QLADSLSSEC YNEQLSITDK KASAFFTEHI
     LGQDGVFVLR LIALNVGQYI ASKIACLIWD RYRLVNNTSK YTRTIKRTQE TPITTTTMMT
     TSTTATTTTT KSQTKHVVTS SIKQLSNIVQ NPPIPERKDK IKHNKELNSS TSNLNELDNI
     VRIRTLNASN TIGQYSQSLP SQSSIYSLRN SFNNSYDHCS HSDRNSSNNS RIQNLNQTNN
     FV
//
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