ID M7B760_CHEMY Unreviewed; 928 AA.
AC M7B760;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
GN ORFNames=UY3_18754 {ECO:0000313|EMBL:EMP24117.1};
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:EMP24117.1, 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: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU280814}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU280814}.
CC -!- SIMILARITY: Belongs to the anoctamin family.
CC {ECO:0000256|ARBA:ARBA00009671, ECO:0000256|RuleBase:RU280814}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU280814}.
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DR EMBL; KB603100; EMP24117.1; -; Genomic_DNA.
DR STRING; 8469.M7B760; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR007632; Anoctamin.
DR InterPro; IPR049452; Anoctamin_TM.
DR PANTHER; PTHR12308; ANOCTAMIN; 1.
DR PANTHER; PTHR12308:SF51; ANOCTAMIN-8; 1.
DR Pfam; PF04547; Anoctamin; 3.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280814};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU280814};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU280814}.
FT TRANSMEM 219..241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 253..276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 365..388
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 449..472
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 776..799
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT DOMAIN 208..309
FT /note="Anoctamin transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04547"
FT DOMAIN 310..506
FT /note="Anoctamin transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04547"
FT DOMAIN 526..890
FT /note="Anoctamin transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04547"
FT REGION 581..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 928 AA; 106625 MW; B82E3E64448A0B67 CRC64;
MSSAVSDKLF GKRLLQAGRY IMSHKSWMKT VPTENCDVLM TFTDTTDDHT LLWLLNHIRL
GIPELIIQIR HHRHTKVYAF FVTATYESLL RGADEIGLRK PVKAEFGGGT RSFSCEEDYI
YENIENELFF FSSQERQNII RYWLENLRAK HGESLHNIQF LEGQPVIPEL VARGVIQQVF
PVHEQRILNR LMKSWVQAIC EAQPLDEICD YFGVKIAMYF AWLGFYTSAM VYPAVFGSIL
YTFTENDQTS RDICCVIFAI FNVIWAXXXX XXXLFLGEWK QRGAEFAYKW GTLDTPAESI
EEPRPQFRAF LGEWKQRGAE FAYKWGTLDT PAESIEEPRP QFRGIKRISP VTNVEEFYYP
PWKQLLFQCL VSLPVCLICL SFVFLVMLGC FELQEFVLSI KELPRLIRFL PKIVLALIVT
ACDDVYRKIA YWLNDMENYR LQSAYEKHLI IKMVLFQFVN SYLSLFYIGF YLKDMERLKE
LLLIFSLSQS LVRQLRDALL PFITLQLHLF LISFKGLLRF GWSLAMLATL LITRQFLQNI
KEVSQPHLYR KIQRGDLSLQ NIRDVSHTIF RLLAQRYTAP RLGPEPRPAE QAARLGPEPE
GAGEGPQGEK CLNGGCGVPE EEEKRESDSE DESVLDCGLK LKKVSFIERA ERRGRELGAM
EDASFLEEGS PTMVEKGMDP ASIFELAEDE EETEGPSGSP LPEAKELAVT LRARRGRAAE
SQEEEEEEEG RKRNRASWID PPEENYSPHL TQAEVESCMK KYEDTFHDYQ EMFIQFGYVV
LFSSAFPLAA LCALINNIIE IRSDAFKLCT GLQRPFGQRK VMEAMGVLAI VVNCYLIGQC
GQLQRLFPWL SPEGAIISVV VLEHFALLLK YLIQVAIPDI PAWVAEEMAK LEYQRREAFK
DKEGKCPGQT KKAEECPEES GSEADPQI
//
