ANO4_BOVIN
ID ANO4_BOVIN Reviewed; 920 AA.
AC A6QLE6;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Anoctamin-4 {ECO:0000250|UniProtKB:Q32M45};
DE AltName: Full=Transmembrane protein 16D {ECO:0000250|UniProtKB:Q32M45};
GN Name=ANO4 {ECO:0000250|UniProtKB:Q32M45};
GN Synonyms=TMEM16D {ECO:0000312|EMBL:AAI47938.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI47938.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI47938.1};
RC TISSUE=Basal ganglia {ECO:0000312|EMBL:AAI47938.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has calcium-dependent phospholipid scramblase activity;
CC scrambles phosphatidylserine, phosphatidylcholine and
CC galactosylceramide (By similarity). Does not exhibit calcium-activated
CC chloride channel (CaCC) activity (By similarity).
CC {ECO:0000250|UniProtKB:Q8C5H1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q8C5H1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664;
CC Evidence={ECO:0000250|UniProtKB:Q8C5H1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(out) = a
CC beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(in);
CC Xref=Rhea:RHEA:38899, ChEBI:CHEBI:18390;
CC Evidence={ECO:0000250|UniProtKB:Q8C5H1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38900;
CC Evidence={ECO:0000250|UniProtKB:Q8C5H1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q8C5H1};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38573;
CC Evidence={ECO:0000250|UniProtKB:Q8C5H1};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q32M45};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q32M45}. Note=Shows
CC an intracellular localization. {ECO:0000250|UniProtKB:Q8C5H1}.
CC -!- MISCELLANEOUS: The term 'anoctamin' was coined because these channels
CC are anion selective and have eight (OCT) transmembrane segments. There
CC is some dissatisfaction in the field with the Ano nomenclature because
CC it is not certain that all the members of this family are anion
CC channels or have the 8-transmembrane topology.
CC -!- SIMILARITY: Belongs to the anoctamin family.
CC {ECO:0000250|UniProtKB:Q32M45}.
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DR EMBL; BC147937; AAI47938.1; -; mRNA.
DR RefSeq; NP_001095520.1; NM_001102050.1.
DR RefSeq; XP_005206653.1; XM_005206596.3.
DR AlphaFoldDB; A6QLE6; -.
DR SMR; A6QLE6; -.
DR STRING; 9913.ENSBTAP00000005430; -.
DR PaxDb; A6QLE6; -.
DR PRIDE; A6QLE6; -.
DR Ensembl; ENSBTAT00000005430; ENSBTAP00000005430; ENSBTAG00000004145.
DR Ensembl; ENSBTAT00000085221; ENSBTAP00000064573; ENSBTAG00000004145.
DR GeneID; 518739; -.
DR KEGG; bta:518739; -.
DR CTD; 121601; -.
DR VEuPathDB; HostDB:ENSBTAG00000004145; -.
DR VGNC; VGNC:25953; ANO4.
DR eggNOG; KOG2514; Eukaryota.
DR GeneTree; ENSGT00940000158600; -.
DR HOGENOM; CLU_006685_1_3_1; -.
DR InParanoid; A6QLE6; -.
DR TreeFam; TF314265; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000004145; Expressed in granulosa cell and 58 other tissues.
DR ExpressionAtlas; A6QLE6; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0061588; P:calcium activated phospholipid scrambling; IEA:InterPro.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR032394; Anoct_dimer.
DR InterPro; IPR007632; Anoctamin.
DR InterPro; IPR031293; Anoctamin-4.
DR PANTHER; PTHR12308; PTHR12308; 1.
DR PANTHER; PTHR12308:SF28; PTHR12308:SF28; 1.
DR Pfam; PF16178; Anoct_dimer; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Lipid transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..920
FT /note="Anoctamin-4"
FT /id="PRO_0000353189"
FT TOPO_DOM 1..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..389
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..512
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..680
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 681..701
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 702..733
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 755..850
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 851..871
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 872..920
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 38..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 920 AA; 107708 MW; 3AFFC6310F1862CD CRC64;
METSSSGITN GRTRVFHPVA KDVNILFDEL EAVNSPCKDD DSLLHPGNLT STSDDASRLE
AGGETVPEKN KLNGLYFRDG KCRIDYILVY RKSNPQMEKR EVFERNIRAE GLQMEKESSL
INSDIIFVKL HAPWEVLGRY AEQMNVRMPF RRKIYYLPRR YKFMSRIDKQ ISRFRRWLPK
KPMRLDKETL PDLEENDCYT APFSQQRIHH FIIHNKDTFF NNATRSRIVH HILQRIKYEE
GKNKIGLNRL LTNGSYEAAF PLHEGSYRSK NSIRTHGAVN HRHLLYECWA SWGVWYKYQP
LDLVRRYFGE KIGLYFAWLG WYTGMLFPAA FIGLFVFLYG VITLDHCQVS KEVCQATDII
MCPVCDKYCP FMRLSDSCVY AKVTHLFDNG ATVFFAVFMA VWATVFLEFW KRRRAVIAYD
WDLIDWEEEE EEIRPQFEAK YSKKERMNPI SGKPEPYQAF ADKCSRLIVS ASGIFFMICV
VIAAVFGIVI YRVVTVSTFA AFKWALIRNN SQVATTGTAV CINFCIIMLL NVLYEKVALL
LTNLEQPRTE SEWENSFTLK MFLFQFVNLN SSTFYIAFFL GRFTGHPGAY LRLINRWRLE
ECHPSGCLID LCMQMGIIMV LKQTWNNFME LGYPLIQNWW TRRKVRQEHG PERKISFPQW
EKDYNLQPMN AYGLFDEYLE MILQFGFTTI FVAAFPLAPL LALLNNIIEI RLDAYKFVTQ
WRRPLASRAK DIGIWYGILE GIGILSVITN AFVIAITSDF IPRLVYAYKY GPCAGQGEAG
QKCMVGYVNA SLSVFRISDF ENRSEPESDG SEFSGTPLKY CRYRDYRDPP HSLVPYGYTL
QFWHVLAARL AFIIVFEHLV FCIKHLISYL IPDLPKDLRD RMRREKYLIQ EMMYEAELER
LQKERKERKK NGKAHHNEWP
