ID A0A340XMQ7_LIPVE Unreviewed; 835 AA.
AC A0A340XMQ7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
GN Name=ANO3 {ECO:0000313|RefSeq:XP_007462671.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007462671.1};
RN [1] {ECO:0000313|RefSeq:XP_007462671.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_007462671.1; XM_007462609.1.
DR AlphaFoldDB; A0A340XMQ7; -.
DR GeneID; 103084063; -.
DR CTD; 63982; -.
DR OrthoDB; 534027at2759; -.
DR Proteomes; UP000265300; 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:UP000265300};
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 249..276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 326..344
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 401..425
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 445..468
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 496..519
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 613..635
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 663..687
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 760..789
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT DOMAIN 11..235
FT /note="Anoctamin dimerisation"
FT /evidence="ECO:0000259|Pfam:PF16178"
FT DOMAIN 238..803
FT /note="Anoctamin transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04547"
SQ SEQUENCE 835 AA; 98403 MW; BF4E4F13F63C57E9 CRC64;
MNYIASSGLL FKDGKKRIDY ILVYRKSNIQ YDKRNTFEKN LRAEGLMLEK EPAVANPDIM
FIKIHIPWDT LCKYAERLNI RMPFRKKSYY TDQRSKSMGR VQKYFRRIKK WMSQNPMVLD
KSAFPDLEES DCYTGPFSRA RIHHFIINNK DTFFSNATRS RIVYHMLQHT KYENGISKVG
ICKLINNGSY IAAFPPHEGA YKSNQPIKTH GPQNNRHLLY ERWARWGMWY KHQPLDLIRL
YFGEKIGLYF AWLGWYTGML IPAAIVGLCV FFYGILTMNA SQVSQEICKA TEVFMCPLCD
KNCSLQRLNE SCIYAKVTYL FDNGGTVFFA IFMAIWATVF LEFWKRRRST LTYTWDLIEW
EEEEETLRPQ FEAKYYKMER VNPISGKPEP HQPSSDKVTR LLVSISGIFF MISLVITAVF
AVVVYRLIVM EQFASFKWNF IKQHWQFATS AAAVCINFVI IMALNLAYEK IAYLLTNLEY
PRTESEWENS FALKMFLFQF VNLNSSIFYI AFFLGRFVGH PGKYNKLFNR WRLEECHPSG
CLIDLCLQMG VIMFLKQIWN NFMELGYPLI QNWWSRHKIK RGIQDASIPQ WENDWNLQPM
NIHGLMDEYL EMVLQFGFTT IFVAAFPLAP LLALLNNIIE IRLDAYKFVT QWRRPLPARA
TDIGIWYGIL EGIGILAVIT NAFVIAITSD YIPRFVYEYK YGPCASQFEY SESCLTGYVN
NSLSFFDLSE LGMGKSGYCR YRDYRGPPWS SKPYEFTLQY WHILAARLAF IIVFEHLVFG
IKSFIAYLIP DVPKNLYDRI RREKYLVQEM MYEAELEHLQ QQRRKSGHPV HHEWP
//