ID A0A498MNC6_LABRO Unreviewed; 922 AA.
AC A0A498MNC6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Protein tweety homolog {ECO:0000256|RuleBase:RU361114};
GN ORFNames=ROHU_026124 {ECO:0000313|EMBL:RXN18517.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN18517.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN18517.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN18517.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN18517.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable chloride channel. {ECO:0000256|RuleBase:RU361114}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU361114};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU361114}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the tweety family.
CC {ECO:0000256|ARBA:ARBA00009849, ECO:0000256|RuleBase:RU361114}.
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:RXN18517.1}.
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DR EMBL; QBIY01012713; RXN18517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498MNC6; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-UniRule.
DR CDD; cd07912; Tweety_N; 1.
DR InterPro; IPR006990; Tweety.
DR PANTHER; PTHR12424:SF4; PROTEIN TWEETY HOMOLOG 3; 1.
DR PANTHER; PTHR12424; TWEETY-RELATED; 1.
DR Pfam; PF04906; Tweety; 1.
PE 3: Inferred from homology;
KW Chloride {ECO:0000256|RuleBase:RU361114};
KW Chloride channel {ECO:0000256|RuleBase:RU361114};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|RuleBase:RU361114};
KW Ion transport {ECO:0000256|RuleBase:RU361114};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361114};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361114};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361114};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361114}.
FT TRANSMEM 464..485
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361114"
FT TRANSMEM 506..528
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361114"
FT TRANSMEM 631..652
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361114"
FT TRANSMEM 659..678
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361114"
FT TRANSMEM 809..830
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361114"
FT REGION 24..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..145
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 173..207
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 245..316
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 357..398
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 53..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 922 AA; 104349 MW; 85B00EB59F389CE2 CRC64;
MSVVAGELVT EEEVEDLAED SLCSSYVSDT EKKSRKKKVS GRPPPSPRTL SKSPKEADYS
VTQTSISMTS TPEYLKEALG MKKPKYSRSA SNGYVPGTPD YKDKEEMYDE IIDLKKTIQS
QKAESDKMKA KLRHLEEESA KKDRQIEQLL DPVKDPEYAR GLVDRKTDPR SIINGLKQRI
LRLEQQCKDK ENALSQLQSE LKTTNMQEMK ITVETYFEEV QRMRALLEST ERSNKTERKH
NRRQNKTLSA TVLKLTNTVQ QLESENQELK KELTQEEMNM MESPACRAKA YMDWSKQRLV
RRILELEKRV EQIKNLQITK ASDSQKSPDN KGTESKSANQ SDSVNTEMEP SVIKENDVHL
REAIKKLGKE NKELQEKLTQ REQEMGALTI EINCLKEKLE EEGKLRLVQG PSQSQICVNT
MAAVVNYSPP WWVNLFHRLP HFNLQFQLTG SDFRPEDSEY QKSVLLLGAV ALVCLALDLL
FLLFYSFWLC CRRRKNQDSP NADCCCTAWC VIIATLVCSA GIAVGFYGNG ETCDGMTRLT
YSLRHANQTV AGIDKLVSES TSSLNETLQE GLVQLETVYS KNTDYLSIVQ KLQGQLDELI
NLMVEVPFWS NTDLSLDNLA SVTEQYDWYR WLGYLGLLLF DVIICLLVLV GLIRNSRSIL
ISVCLLGVLT LVISWASLGL EFSVAVTASD FCVAPDSYIT KVTRENAVIN QDILQYYLKC
SMGQTNPFQQ KLSGSHKALV EMQDDVSELL RSAIREFPKT KSNLEEMQAV LNSTEVSLHH
LTALVDCRSL HMDYVQALTG LCYDGVEGLI YLVLFSFVTA LMFSSIVCSV PHTWQSKRSE
EEDGDETSAT LGPRAPHDNL YRVHMPSLYS CGSSTYGSEA SLPAAAHTVS NAPVTEYMSY
VMQITMLCER RKQKNEEEGL CF
//
