ID M7B101_CHEMY Unreviewed; 445 AA.
AC M7B101;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Otopetrin-1 {ECO:0000313|EMBL:EMP29100.1};
GN ORFNames=UY3_13795 {ECO:0000313|EMBL:EMP29100.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP29100.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the otopetrin family.
CC {ECO:0000256|ARBA:ARBA00006513}.
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DR EMBL; KB559124; EMP29100.1; -; Genomic_DNA.
DR AlphaFoldDB; M7B101; -.
DR STRING; 8469.M7B101; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015252; F:proton channel activity; IEA:InterPro.
DR InterPro; IPR004878; Otopetrin.
DR PANTHER; PTHR21522; PROTON CHANNEL OTOP; 1.
DR PANTHER; PTHR21522:SF35; PROTON CHANNEL OTOP2; 1.
DR Pfam; PF03189; Otopetrin; 2.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 261..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 48728 MW; 574FCF4385DC2AA8 CRC64;
MPGNSPTNSC SCATSLCHIF SEGAAYLHPF NIEFSLFSST MLYVVWKNKA ACRRQPHPCP
RGRFHLSGAF VGLVLGALAI SATFGVMISF GVLAKAPETV PEALRTYYIF SSVLLSAMFL
ASLVGIAAYR LQRDPASTDC SKSVVRSLDV TLLLGSSCGP LMVSVFSLVA IFFLHINGSL
HLLDLCFSLC KTIQVLGQNL FITEALYSRP AHQPHAPDSP PGNEWVFSIS GGHAEEPVQQ
DVAARPERKC ATCPRRARPS KCWARTSSSP KPFTPGPPTS HMPPTAPQAT NGSSPSPEAT
PKSRSSRTWL PALSVNAPHA RAAFFFVVRA GEGRGPGWWR RCSGGNYSLA KIPAGSQRSW
PRGEPERVSI RRKILQNISI LLIFYNISVW ILYAYGTRPH LVSQIELSFY GFTLWVIIVK
ISLPLGIFYR MHSVASLFEV YCKTC
//
