ID A0A2Y9QE19_DELLE Unreviewed; 784 AA.
AC A0A2Y9QE19;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
GN Name=ANO4 {ECO:0000313|RefSeq:XP_022455740.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022455740.1};
RN [1] {ECO:0000313|RefSeq:XP_022455740.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022455740.1};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU280814}.
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DR RefSeq; XP_022455740.1; XM_022600032.1.
DR AlphaFoldDB; A0A2Y9QE19; -.
DR Proteomes; UP000248483; 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:SF28; ANOCTAMIN-4; 1.
DR Pfam; PF16178; Anoct_dimer; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280814};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
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 179..206
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 255..274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 331..357
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 377..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 426..447
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 546..568
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 596..620
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT DOMAIN 28..165
FT /note="Anoctamin dimerisation"
FT /evidence="ECO:0000259|Pfam:PF16178"
FT DOMAIN 168..749
FT /note="Anoctamin transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04547"
FT COILED 748..782
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 784 AA; 92218 MW; A4C56F8871315A76 CRC64;
MGFLLDWLHF CCSSRRKIYY LPRRYKFMSR IDKQISSFRR WLPKKPMRLD KETLPDLEEN
DCYTAPFSQQ RIHHFIIHNK DTFFNNATRS RIVHHILQRI KYEEGKNKIG LNRLLTNGSY
EAAFPLHEGS YRSKNSIRTH GAVNHRHLLY ECWASWGVWY KYQPLDLVRR YFGEKIGLYF
AWLGWYTGML FPAAFIGLFV FLYGVITLDH CQVSKEVCQA TDIIMCPVCD KYCPFMRLSD
SCVYAKVTHL FDNGATVFFA VFMAVWATVF LEFWKRRRAV IAYDWDLIDW EEEEEEIRPQ
FEAKYSKKER MNPISGKPEP YQAFADKCSR LIVSASGIFF MICVVIAAVF GIVIYRVVTV
STFAAFKWAL IRNNSQVATT GTAVCINFCI IMLLNVLYEK VALLLTNLEQ PRTESEWENS
FTLKMFLFQF VNLNSSTFYI AFFLGRFTGH PGAYLRLINR WRLEECHPSG CLIDLCMQMG
IIMVLKQTWN NFMELGYPLI QNWWTRRKVR QEHGPERKIS FPQWEKDYNL QPMNAYGLFD
EYLEMILQFG FTTIFVAAFP LAPLLALLNN IIEIRLDAYK FVTQWRRPLA SRAKDIGIWY
GILEGIGILS VITNAFVIAI TSDFIPRLVY AYKYGPCAGQ GEAGQKCMVG YVNASLSVFR
ISDFENRSEP ESDGSEFSGT PLKYCRYRDY RDPPHSLVPY GYTLQFWHVL AARLAFIIVF
EHLVFCIKHL ISYLIPDLPK DLRDRMRREK YLIQEMMYEA ELERLQKERK ERKKNGKAHH
NEWP
//