ID A0A1S3K2D3_LINUN Unreviewed; 403 AA.
AC A0A1S3K2D3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN Name=LOC106178232 {ECO:0000313|RefSeq:XP_013416795.1};
GN Synonyms=inx {ECO:0000256|RuleBase:RU010713};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013416795.1};
RN [1] {ECO:0000313|RefSeq:XP_013416795.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013416795.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_013416795.1; XM_013561341.1.
DR AlphaFoldDB; A0A1S3K2D3; -.
DR STRING; 7574.A0A1S3K2D3; -.
DR EnsemblMetazoa; XM_013561341.1; XP_013416795.1; LOC106178232.
DR GeneID; 106178232; -.
DR KEGG; lak:106178232; -.
DR InParanoid; A0A1S3K2D3; -.
DR OrthoDB; 2873211at2759; -.
DR Proteomes; UP000085678; Unplaced.
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:UP000085678};
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 97..114
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 208..232
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 291..314
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
SQ SEQUENCE 403 AA; 46824 MW; FA4D454CA2408E4E CRC64;
MAPFIDILSG VWKGVRCDDD FYDRLSHRYT ALIMVVFVVL ISSKQYVGDP IICWTPAEFT
GVYSSYANQV CWISNTYYLP FEERIPGANL PRAHIPYYQW VPIVMLLQAL LFYLPTIAWR
LSSCSTGIDV NTMVNCVTNL ALLDPDKRRD TIKYLVRHMD GYFGCRKTYD KECCGGGLRG
CITKVLICCK VGKRYGNHLT FLYLSVKVLF LANAIGQLFL LNAFLGTAYH LYGFDVLNDL
VLNRDWWFSG RFPRVTLCDF KVRQLGGNIH RHTVQCVLPI NLFNEKIYMF IWFWLVFVSA
ATVYGFVPWI NLFFKGERRH FVRKNLRLMG RLGHGENGGV MCKNFIHQYL RQDGTFVLKL
LGRNSNDMIV AEFTAELYDY FRKTYTKQDF EDAEEEPLQM ETV
//
