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Database: UniProt
Entry: A0A452GU04_9SAUR
LinkDB: A0A452GU04_9SAUR
Original site: A0A452GU04_9SAUR 
ID   A0A452GU04_9SAUR        Unreviewed;       926 AA.
AC   A0A452GU04;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000005222.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000005222.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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}.
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DR   AlphaFoldDB; A0A452GU04; -.
DR   STRING; 38772.ENSGAGP00000005222; -.
DR   Ensembl; ENSGAGT00000006084.1; ENSGAGP00000005222.1; ENSGAGG00000004239.1.
DR   Proteomes; UP000291020; 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:SF22; ANOCTAMIN-7; 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:UP000291020};
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        305..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        383..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        461..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        506..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        549..570
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        676..698
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        726..750
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        807..829
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   DOMAIN          55..294
FT                   /note="Anoctamin dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16178"
FT   DOMAIN          297..850
FT                   /note="Anoctamin transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04547"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          870..898
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"
SQ   SEQUENCE   926 AA;  106730 MW;  7C494F52370EEF31 CRC64;
     MQRKKIKADD HANLMSEDQN AKGPYYGSLS QAPIEVSELS KPSQATHVTQ STANVFSDGR
     TRIDFVLVWE ADPQEQEGQN EETTAESEVP RWRRAVDVHK TWRKKFLNKL QAAGICIEKH
     MVQDEKKVVH YVLLNAPWSV LCYYAEDLRL RLPLQALPNQ ASNWSDRVAK QLGVPSLLHE
     EVPNLPMDYY TCHFKVNKLA WFLGSNEQDT FFSSTQRHRI LYEILATTPY GHLKQGEVGV
     DRLLSENVFA AAFPLHEGPF AVPADRLAPE SLTERQVLFQ YWARWQKWNR YQPLDHIRRY
     FGEKIALYFA WLGFYTGWLL PAAVVGTLVF IAGIFLMLSD IPAQEICESE DQYQMCPLCK
     ECPQWQLSSI CSMFKAGRLF DHGGTIFFSI FMSLWAVTFL EYWKRMNATL AHRWDCSDFE
     DIEERPRPQF TAMAPMTMEN PITGAEEPYF PKRNRVKRVT AGLMVIIMMI AVVVMFLISI
     ILYRAIVSIL VSRSGNFLFV ASASRIASLT GSVVNLIFIL ILSKIYIALA HFLTKWEMHR
     TQTKYEDAFT FKVFVFQFVN FYSSPIYIAF FKGRFVGYPG HYKTLLGIRN EDCGAGGCLT
     ELAQELLVIM VGKQVINNVQ EIVIPKLKGW WQKYKLRSKK RKSKEAQLGL AQQVPWESNY
     ELLVCEGLFD EYLEMVLQFG FITIFVAACP LAPLFALLNN WVEIRLDAQK FVCEYRRPVA
     ERAQGIGIWF YILEVITHLA VISNAFLIAF TSDFLPRLYY QYTRASDLQG YVNFTLAYAP
     KHFASQHNVT CRYRAYRDEN GRYSLTYWNL LAIRLGFIIV FEHVVFFIAR VIDLMVPDIP
     ESLEIKVKRE RYLAKQALAE NQALFEREEV RATSTTMQTA PKDWELGGMH ENQGPSHLQM
     TTSTHTVAAS LEAHPQQQFE PEAESP
//
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