ID A0A3Q0SV90_AMPCI Unreviewed; 685 AA.
AC A0A3Q0SV90;
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=ANO1 {ECO:0000313|Ensembl:ENSACIP00000023950.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000023950.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000023950.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU280814}.
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DR AlphaFoldDB; A0A3Q0SV90; -.
DR Ensembl; ENSACIT00000024579.1; ENSACIP00000023950.1; ENSACIG00000018582.1.
DR GeneTree; ENSGT00940000157182; -.
DR OMA; QSEQGAF; -.
DR Proteomes; UP000261340; 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:SF13; ANOCTAMIN-1; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU280814};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU280814}.
FT TRANSMEM 58..82
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 135..151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 258..282
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 302..323
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 427..450
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 484..507
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT DOMAIN 2..44
FT /note="Anoctamin dimerisation"
FT /evidence="ECO:0000259|Pfam:PF16178"
FT DOMAIN 47..621
FT /note="Anoctamin transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04547"
SQ SEQUENCE 685 AA; 79259 MW; AE7EEFB17E2F860D CRC64;
TGITSLLGSG VYTAAYPLHD VSSTLLLLYE EWANYSVFYK YQPIGLVRKY FGEKIGLYFA
WLGLYTQMLI PASLVGVIVF LYGCATVDDN IPSMEICHPK NNITMCPLCD RVCSYWKLST
ACGTARASHL FDNPATVFFS IFMALWAAMF MEHWKRRQMR LNYEWDLTGF EDEEDHPRAE
YEFRVMQKSL RKGQKSQRKM EKLTFQDRLP AYMTNIVMLL LMIGVTFAIV FGVILYRIST
KAALHMSSSL ITRNHVQLTV KTTAAIINLV VILILDEVYG AVARWLTVLE APKTDKSFEE
RLIFKTFILK FVNAFTPIIY IAFFRGRLVG RPGSYLYVFD SYRMEECAHG GCLMELCIQL
SITMLGKQLI QNNLFEIGIP KLKKLIRFIR SKRGGFQEEE RQKKLTRYET DHFLEPFGGL
TPEYMEMIIQ FGFVTLFVAS FPLAPLFALL NNIIEIRLDA KKFVTELRRP VAARAKDIGI
WYNILRGVAK VAVIINAFVI SFTSDFIPRM VYQYMYSTDG SMHGFVNHTL SYFNVSHFQE
GKEPMDPSHL GYPVSICRYK DYREPPWSNT PYELSKEFWA VLAVRLAFVI VFQNVVMLMN
DIIDWLIPDI PKDISLQIHK EKILLVELFM KEEQGKSYIL DTYLVPHKYP PHHNTTCPNC
WQDTSTPSCC LHQILTLLFK CYSRN
//