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Database: UniProt
Entry: A0A3B4UFQ6_SERDU
LinkDB: A0A3B4UFQ6_SERDU
Original site: A0A3B4UFQ6_SERDU 
ID   A0A3B4UFQ6_SERDU        Unreviewed;       979 AA.
AC   A0A3B4UFQ6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
GN   Name=ANO8 {ECO:0000313|Ensembl:ENSSDUP00000017023.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000017023.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000017023.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   AlphaFoldDB; A0A3B4UFQ6; -.
DR   Ensembl; ENSSDUT00000017330.1; ENSSDUP00000017023.1; ENSSDUG00000012428.1.
DR   GeneTree; ENSGT00940000157019; -.
DR   OMA; YEQSKLG; -.
DR   Proteomes; UP000261420; Unplaced.
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:SF47; ANOCTAMIN; 1.
DR   Pfam; PF04547; Anoctamin; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280814};
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        182..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        287..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        370..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        627..650
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   DOMAIN          170..749
FT                   /note="Anoctamin transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04547"
FT   REGION          761..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          843..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          880..979
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..818
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..858
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..957
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   979 AA;  112119 MW;  D6109272DB37C447 CRC64;
     MGIVIYSIDD HTLLWLLNQI RVGIPQVSIQ IRQHKHTQAH AFFITTTFEN LLRGAEQMGI
     HKAVKPQYGG GMRRFSCEED NIYENIDSEL CFFTSQERQS IIKYWLDNLR AKQGEVLHNI
     HFLEGQPIIP ELVARGVIHQ MFPLHEQRIL NQLMTSWVQA VCERQPLDDI CDYFGVKIGM
     YFAWLGFYTN SMLYPAVIGF LLWILAEADQ TSQDICCVVF ALFNVVWATL FLERWKRREA
     ELAYRWGTLD TPAESLEEPR PQFRGVKRCS PITGCEEFYY PPWKRALFRW LVSLPICLLC
     LCFVFLAMLL CLELQEVVME IQELPGITRF IPKILLAITV TICDEVYKKI AYWLNDMENY
     RLQSAYENNL IIKMVFFEFI NSYLSLFYIG FYLKDMERLK EMLATLLIFR QFLQNIKEVL
     QPYLYEQNKL GVFTPKVIWE LLQAIMLKYG RLALGKAQAS ITAYSFLGPR GIPVGHTANG
     NPEPKRRGDL KAGFRLTEEE WDMNDSVLKQ RKVSFTEKVD YQDVTTDAQA GDYSFLEDSP
     TLVEEGMDPS SIFDSCDEDS DCELLSQESY PLCQRRKNVG EGREDKKSWI DPPEETKTVT
     LTQAEIESCM QTYEDTLQDY QEMFIQFGYV VLFSSAFPLA AMCALINNII EIRSDALKLC
     TGLQRPFGQR VENIGQWQTA MEAMGLIAII VNCYLIGQCG QLQRLFPWLS PEMTIISIVL
     LEHFAILLKY VIHVAIPDIP GWVAEEMAKL EYRRREAFKK HEQQAQHHFQ QQLRRRREEE
     ELQRQAELQA EARQESEYHR ADTHHQHHHD KVSGGKPGDK PKRPSSLLGN NNVMKLKQII
     PLQGKFSSGT SRSPAQSPTG GEAKLPGFLK FLKSPEVKKE PAVAVGPTPG STVTSSVPPS
     GQERSQSPNR TFSPGKLFSF SKSEGTVVCA NGTQPPTQAA NAQPNRYDLN TSQEELPSNE
     SDKGESRQLT DLENSGSKS
//
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