ID A0A2R2MPA5_LINUN Unreviewed; 451 AA.
AC A0A2R2MPA5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN Name=LOC106153345 {ECO:0000313|RefSeq:XP_023932069.1};
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_023932069.1};
RN [1] {ECO:0000313|RefSeq:XP_023932069.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_023932069.1};
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_023932069.1; XM_024076301.1.
DR AlphaFoldDB; A0A2R2MPA5; -.
DR STRING; 7574.A0A2R2MPA5; -.
DR EnsemblMetazoa; XM_024076301.1; XP_023932069.1; LOC106153345.
DR KEGG; lak:106153345; -.
DR InParanoid; A0A2R2MPA5; -.
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 230..253
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 319..343
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT REGION 419..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 52823 MW; 0C6777616AF893E8 CRC64;
MIFNTNFSEI LIFQLIIYSL RNFMFNNSNK MAPFTEYLRP ILKSLRSDDD SFDRLNHRYS
AAVLLVFALL TTMKQYVGEP ILCWVPGRFT GAMEDYTNAM CWISNTYWVP FETRIPNPDD
PKPHIAYYQW VPIVLLLQAL LFKLPCVAWR LLSYNSGIDI QAMFKKLERD EIIEHKKMKS
NVKEVTRYLA RYLDATRDQP HGCCAWARRI MSSYLCVCVG KRRGNYLYML FLWIKILYMV
NGLGQMFLLN AFLGTQFTMY GYQIIEDLIN WRDWTETGRF PRTTLCDIKI RELGGNIHRH
TIQCGLPINF FNERIYMFLW FWLVFVSAGT IFGFFTWMSL FSVNERKVFV KKTISMTGKG
DSIEQNRDTK RLKNFVTKYL RMDGVFVLKL LAKNTSDVVI SRVVYSLWKR YLKRHKELQP
DGLPLTPKAN DASSPSAPPT DADDSEPPKG L
//
