ID A0A0V1HR67_9BILA Unreviewed; 860 AA.
AC A0A0V1HR67;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN Name=inx-12 {ECO:0000313|EMBL:KRZ12117.1};
GN Synonyms=inx {ECO:0000256|RuleBase:RU010713};
GN ORFNames=T11_15569 {ECO:0000313|EMBL:KRZ12117.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ12117.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ12117.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ12117.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ12117.1}.
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DR EMBL; JYDP01000043; KRZ12117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1HR67; -.
DR STRING; 268475.A0A0V1HR67; -.
DR Proteomes; UP000055024; 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; 2.
DR PRINTS; PR01262; INNEXIN.
DR PROSITE; PS51013; PANNEXIN; 2.
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:UP000055024};
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 25..45
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 112..134
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT 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 322..346
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 550..571
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 635..661
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 726..750
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT REGION 438..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 101714 MW; 22B70A634622877F CRC64;
MDKLTQYLSS IKPYRDCDFI DRLNSFYTVI GTVCFAVLVS GWSFVGTPIQ CWFPAYFKGW
WIQYSLDYCY VQNTYFLPFT KSMPLKNYWD LIRNPIDIPE SVEKREERLI GYYQWVPFIL
ALVAVCFWMP MAFWRALNMH SVIIDNLDLY VSIFVKTMLQ PIVNFNYTQR FILHDFKSIS
VKTVCDMTSI VEHVEPLSRQ KNVDKIAQLL DHSTVLSARL HGRNLFTGRY ILLLYLAVKI
YYVINAVMLF FMLQHFLGVE DSFWGARVFY NLVYGRQWEE TGNFPRVTIC DFEVRELGNV
HRHSVQCVLM INMFNEKIFL FFWWWFVILA VLNFVNLLCW IASIIFDSFN SSYVISYLED
SARLEMSENE FLLNIEDFVK TCLQPDGMFL LRLIGTNSGD IVSKELVNSL WNRYISRKKS
NPKQLDDDQS LSEENQPILQ NYGDNNNNND GPFTDDSASS SREDFKESSL YTDHLHQRAA
NLHANLKSII RLKFIHLPIQ CWVPAQFTGA WEQYTENYCF VQNTYFLQLT NQIPVDYVER
DSREIGYYQW VPFILALQAF LFYLPCLIWR LTNWYSGISV LGITNMAVDA GNMDHETRKK
NVKTVAQHIR QSLYLQRELS TSGKLFGFLI YGKHYGIYVT GLYLLIKFLY ILNVVCQFLI
LNRFLGAQYT FWGFEILRDL AYGREWQESG HFPRVTMCDF DVRVLGNLHR WTVQCVLMIN
MFNEKIYLFL WWWFFIISIF TFLNFFYWIF VSFNQNMQVN FISRYLRVSD KISDTLPEQR
RVSKFVRREL RPDGVFLLRI IASNAGDIIA TELIKDLWTV YDAKQNHPTP PPVQSKKNMN
YDKNDQSPYK EEKMPLAGSH
//
