ID   A0A087RKE5_APTFO        Unreviewed;       979 AA.
AC   A0A087RKE5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
GN   ORFNames=AS27_14578 {ECO:0000313|EMBL:KFM13949.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM13949.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM13949.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM13949.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL226410; KFM13949.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087RKE5; -.
DR   Proteomes; UP000053286; Unassembled WGS sequence.
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:UP000053286};
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        389..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        466..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        541..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        584..608
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        636..659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        756..779
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        807..831
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        908..933
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   DOMAIN          150..375
FT                   /note="Anoctamin dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16178"
FT   DOMAIN          378..947
FT                   /note="Anoctamin transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04547"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   979 AA;  114959 MW;  F92ADBCAB0884D2A CRC64;
     MNTSKSETVK EHPLKPSRRS MPCLAQSQTH PQSLRKHSSF LQPNRVQPQP RPQPLSAGTS
     TATVDVVSER AKVMETLENN LLKLSNTEYS DPFLDIGKDK DTYTDDSEHG NYDARTDQSL
     LIQNKLTRQK IEPRTKSSLK TDAMASSGLF FKDGKKRIDY ILVYKKSSPQ VEKRSTFEKN
     LRAEGLMLER EPAVTNSDIM FVKIHCPWET LCKYAERMNI RMPFRKKCYY TDWRSKTMGS
     LQRNMRELKS WLPRNPMKLD KEALPDLEET DCYTAPFSRA RIHHFTINNK DSFFSNSTRS
     RIVHHMLQRT KYEDGKSKMG INRLLNNGTY EAAFPPHEGS HKSRHPIKTH GAQNHRHLLY
     ERWARWGMWY KYQPLDLIRR YFGEKIGLYF AWLGWYTGML IPAALVGLFV FLYGLFTMDS
     SQVSKEICEA NETIMCPMCE RNCTLQKLNE SCIYAKVTHL FDNGGTVFFA IFMAIWATVF
     LEFWKRRRAV LTYDWDLIDW EDEEEELRPQ FEAKYSQVER VNPITGKPEP FQPFPDKLSR
     LMVSVSGIFF MISLVLTAVF AVVVYRLVAM EQFASFKWYF IKKYWQIATS GTGVCINFMI
     IMSLNVVYEK VAYLLTDLEH PRTESEWENS FALKMFLFQF VNLNSSIFYI AFFLGRFAGR
     PGKYNKLFNR WRLEECHPSG CLIDLCLQMG VIMVLKQMWN NFMELGYPLL QNWWSRRKMK
     RGGQLMEHKI SLPQWEKDWN LQPMNLHGLM DEYLEMVLQF GFTTIFVAAF PLAPLLALLN
     NIIEIRLDAY KFVTQWRRPM PARATDIGIW YGILEGIGVL AVITNAFVIA ITSDYIPRFV
     YAYKYGPCTD QGYRQEKCLK GYVNSSLSVF DLSELGMGYS GYCRYRDYRA PPWSSTPYEF
     TLQFWHVLAA RLAFIIVFEH LVFGIKSFIA YLIPDMPKDL CDRMRREKYL VQEMMYEAEL
     EHLQRERKKN GKQYHHEWP
//