ID A0A0K0E952_STRER Unreviewed; 380 AA.
AC A0A0K0E952;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN Name=inx {ECO:0000256|RuleBase:RU010713};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|Proteomes:UP000035681, ECO:0000313|WBParaSite:SSTP_0000603600.1};
RN [1] {ECO:0000313|Proteomes:UP000035681}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SSTP_0000603600.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) 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 AlphaFoldDB; A0A0K0E952; -.
DR WBParaSite; SSTP_0000603600.1; SSTP_0000603600.1; SSTP_0000603600.
DR Proteomes; UP000035681; 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-5; 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|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU010713};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00351}; Reference proteome {ECO:0000313|Proteomes:UP000035681};
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};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU010713}.
FT TRANSMEM 101..118
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 278..302
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
SQ SEQUENCE 380 AA; 45578 MW; C0EE3D7EFCFFC8B8 CRC64;
MFHIPFIDET VHKLFNKSYY DDTIGRICST LTPRILIFFT LFVSAKQYIG DPIKCWVPQE
FEDSWEEYAE DICFVKNTYY IPKNESIPKD QFRRNQAEIG YYQWVPIILL LMAFMFYLPK
LIRNLLIKQT GIDLDTIIIE AIALKNYNEK DRGEILKRLK NYLNECLELN NQDNSFCLGY
STSEDNRLLC LTTINLFANF LHTINIMIQF SFVNKFLGPK YTMWGYEVVK NLVYGNEWED
SPIFPRVTLC DFQVRRLANI HHYTVQCVLM INMINEKIFL FIWFWFLFVI VISIINFLYS
IWKFSIPINR EKNLNSYFKD YIGKRDGSIY FKKIFSKFIN KYIKADGYFI LNYIERQVGG
VLFKEIVREL FNDFFQKEVK
//