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Database: UniProt
Entry: A0A2K5IV76_COLAP
LinkDB: A0A2K5IV76_COLAP
Original site: A0A2K5IV76_COLAP 
ID   A0A2K5IV76_COLAP        Unreviewed;       549 AA.
AC   A0A2K5IV76;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000020386.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000020386.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU280814}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, 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_011806371.1; XM_011950981.1.
DR   AlphaFoldDB; A0A2K5IV76; -.
DR   Ensembl; ENSCANT00000043354.1; ENSCANP00000020386.1; ENSCANG00000033602.1.
DR   GeneID; 105518118; -.
DR   CTD; 55129; -.
DR   OrthoDB; 534027at2759; -.
DR   Proteomes; UP000233080; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IEA:UniProt.
DR   InterPro; IPR007632; Anoctamin.
DR   InterPro; IPR049452; Anoctamin_TM.
DR   PANTHER; PTHR12308; ANOCTAMIN; 1.
DR   PANTHER; PTHR12308:SF40; ANOCTAMIN-10; 1.
DR   Pfam; PF04547; Anoctamin; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280814};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233080};
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        97..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        132..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        203..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        289..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        390..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        480..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   DOMAIN          89..515
FT                   /note="Anoctamin transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04547"
SQ   SEQUENCE   549 AA;  63482 MW;  362C490B8E903690 CRC64;
     MKVTLSALNT SESSFTPLVV IELAQDVKEE TKEWLKNRII AKKKDGVRRL LTSGIVIQVF
     PLHDNEALKK LEDTWYTRFA LKYQPIDSIR GYFGETIALY FGFLEYFTFA LIPMAVIGLP
     YYLFVWEDYD KYVIFASFNL IWSTVILEVW KRGCADMTYR WGTLLMKRKF EEPRPGFHGV
     LGINPITGKE EPLYPSYKRQ LRIYLVSLPF VCLCLYFSLY VMMIYFDLEV WALGLHENSG
     SEWTSVLLYV PSIIYAIVIE IMNRLYRYAA EFLTSWENHR LESAYQNHLI LKVLVFNFLN
     CFASLFYIAF VLKDMKLLRQ SLATLLITSQ ILNQIVESLL PYWLQRKHGV RVKRKMQALK
     ADIDATLHEQ VILEKEMGTY LGTFDDYLEL FLQFGYVSLF SCVYPLAAAF AVLNNFTEVN
     SDALKMCRVF KRPFSEPSAN IGVWQLAFET MSVISVVTNC ALIGMSPQVN AIFPESKADL
     ILIVVAVEHA LLALKFILAF AIPDKPRHIQ MKLARLEFES LEALKQQQMK LVTENLKEEP
     KESGKEKAT
//
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