ID A0A3Q3BGV6_KRYMA Unreviewed; 846 AA.
AC A0A3Q3BGV6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
GN Name=ANO3 {ECO:0000313|Ensembl:ENSKMAP00000029040.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000029040.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000029040.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU280814}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU280814}.
CC -!- SIMILARITY: Belongs to the anoctamin family.
CC {ECO:0000256|ARBA:ARBA00009671, ECO:0000256|RuleBase:RU280814}.
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DR AlphaFoldDB; A0A3Q3BGV6; -.
DR STRING; 37003.ENSKMAP00000029040; -.
DR Ensembl; ENSKMAT00000029403.1; ENSKMAP00000029040.1; ENSKMAG00000021521.1.
DR GeneTree; ENSGT00940000156257; -.
DR OMA; TMGRNMR; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR InterPro; IPR032394; Anoct_dimer.
DR InterPro; IPR007632; Anoctamin.
DR InterPro; IPR049452; Anoctamin_TM.
DR PANTHER; PTHR12308; ANOCTAMIN; 1.
DR PANTHER; PTHR12308:SF16; ANOCTAMIN-3; 1.
DR Pfam; PF16178; Anoct_dimer; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280814};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
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 251..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 328..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 403..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 447..470
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 498..521
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 622..644
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 672..696
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 775..800
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT DOMAIN 27..237
FT /note="Anoctamin dimerisation"
FT /evidence="ECO:0000259|Pfam:PF16178"
FT DOMAIN 240..814
FT /note="Anoctamin transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04547"
SQ SEQUENCE 846 AA; 99678 MW; 6A8C84ECA4BE7E0D CRC64;
LGACDQDDSQ LLPHQILKKR SDSSGLFFRD GKKRIDYILV YKKSSPQVEK RCTFEKNLRA
EGLMLEKEPS MTNNDIMFVK IHAPWDTLCK YAEQMNIRMP FRFHLKCQQI KSWLPKNPMK
LDKEALPDLE ESDCYTAPFS RARMHHFTIN NRESFFSNST RSRIVHHVLQ RTKYEDGKSK
MGINRLLGNN TYEAAFPPHE GGYKSRHPIK THGAQNHRHL LYERWARWGI WYKYQPLDLI
RRYFGEKIGL YFAWLGWYTG MLIPAALVGL FVFLYGLFTM DSSQVSKEIC EANTTIMCPM
CEETCEPWTL SDSCVFAKVT HLFDNGGTVF FAIFMAIWAT VFLEFWKRRR AELTYDWDLI
DWEEEEEELR PQFEAKYSRV ERVNPISGKP EPFQPFSDKL SRLMVSVSGI FFMISLVLTA
VFAVVVFRLI AMEKFASFNW HFVKKNWQFA TSGTGVCINF MIIMSLNVVY EKVAYLLTNL
EHPRTESEWE NSFALKMFLF QFVNLNSSTF YIAFFLGRFA GRPGKYNKLF NRWRLEECHP
SGCLIDLCLQ MGVIMFFKQI WNNFMELGYP LLQNWWSRRK MKQGGGGRPN VENKTQLPQW
DKDWNLQPMN AHGLVDEYLE MVLQFGFTTI FVAAFPLAPL LALLNNIIEI RLDAYKFVTQ
WRRPMPARAT DIGIWHGILE GIGVLAVITN AFVIAITSDY IPRFVYAFKY GPCVDKGQHH
ADECLQGYMN SSLSVFDMWE LKNSSKFRYC RYRDYRAPPW SSVPYEFTLQ FWHVLAARLA
FIIVFEHLVF GIKSFIAYLI PDMPKDLCDR MRREKYLMQE MMYEAELEHL QKERKKNGKR
YHHEWP
//