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Database: UniProt
Entry: A0A2B4SKA9_STYPI
LinkDB: A0A2B4SKA9_STYPI
Original site: A0A2B4SKA9_STYPI 
ID   A0A2B4SKA9_STYPI        Unreviewed;       908 AA.
AC   A0A2B4SKA9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
GN   Name=ANO4 {ECO:0000313|EMBL:PFX29539.1};
GN   ORFNames=AWC38_SpisGene5729 {ECO:0000313|EMBL:PFX29539.1};
OS   Stylophora pistillata (Smooth cauliflower coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Stylophora.
OX   NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX29539.1, ECO:0000313|Proteomes:UP000225706};
RN   [1] {ECO:0000313|Proteomes:UP000225706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA   Tambutte S., Allemand D., Aranda M.;
RT   "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT   digitifera provides evidence for extensive differences between species of
RT   corals.";
RL   bioRxiv 0:0-0(2017).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PFX29539.1}.
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DR   EMBL; LSMT01000064; PFX29539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B4SKA9; -.
DR   EnsemblMetazoa; XM_022928411.1; XP_022784146.1; LOC111324777.
DR   OrthoDB; 2909033at2759; -.
DR   Proteomes; UP000225706; 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:SF84; ANOCTAMIN; 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:UP000225706};
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        301..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        381..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        461..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        505..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        551..572
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        671..697
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        721..745
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        832..857
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   DOMAIN          54..286
FT                   /note="Anoctamin dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16178"
FT   DOMAIN          290..871
FT                   /note="Anoctamin transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04547"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          875..902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   908 AA;  104496 MW;  6C712EE67A6F0B53 CRC64;
     MLSRLLRKRK DPTMDRGSYS ELSQTDGSNQ GVELEVNISP LAESSADKSS TRDRDHGKRT
     DYVLVYETCK EKDGKDEESK KEAEALARSR RSFERRLQKK GLVLQHEIVI AEKEPEVQRH
     FVLIHAPWEL LASRAEDMKL KVPLQPNDVE FTSWPQSFCG RDRLEKMANW NPLIIHDATV
     RERADNFMGR FDKEHLTTYM NHEDKEIFFP TVDRMHVVYQ ILQNTRFAQD PQCLGLKRLV
     LDGAYIAHYP LHEGTENLCN EDSPVNDRQR LKRDWARLGR CFKFQPYDAI KDYFGHEIGL
     YFAWLGFYSA MLVPLAIVAL IVFLYGIITT GSHAPVQDVC DEKNDGVWYM CPLCDRQCSY
     WNLAPTTCLY TYVTNVFDND ATVILALAAS IWATLFLEFW KRREASLASE WHTSDFEEEE
     EPLRPEYVKS LTEEERNPFK PDPETGKIVY RASKMKQYRR YATVFSVIAF MICLVIAAII
     GVVVFRAATF AILSSNPDRV VQKRARILTT GFAACINLVA ITLLKYVYNK LAVWLTNWEN
     PATRSAYEDS FIWKMALFQF VNTFASIIYI AFFKSQSIVG SPGRYRRVLG KYRLDGCSEQ
     GCFLELCIQI AIIMVGQQII GNVIEVGIPS FQLWLKRRKA ADSGDRPQYV KDHELSELED
     HYLFWDYLEI VLQYGFVTMF VAAFPLAPIF ALINAVLEIR VDAINFVCYH RRPRAVRVED
     IGAWHGVLAA VTKIAVLMNA FILAFTSEFI PKLVYKYRFA PDRNSPGGGT LKGYINNSLA
     YIDLKTLYTW EPGTEPIEPT ANVNYTRDYC RYSGYFDNTY PYNRSKEYWN VVAARLAFVV
     VFQFLVYSIT SLIAWAVPDV PENLKFKQER EKQVVKEKLG APSDDDDSGE DEDDAVKTND
     DVTLVFGI
//
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