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Database: UniProt
Entry: A0A452HDJ0_9SAUR
LinkDB: A0A452HDJ0_9SAUR
Original site: A0A452HDJ0_9SAUR 
ID   A0A452HDJ0_9SAUR        Unreviewed;       929 AA.
AC   A0A452HDJ0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
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:ENSGAGP00000012875.1, 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:ENSGAGP00000012875.1}
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; A0A452HDJ0; -.
DR   Ensembl; ENSGAGT00000014755.1; ENSGAGP00000012875.1; ENSGAGG00000009879.1.
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:SF23; ANOCTAMIN-5; 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        317..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        480..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        525..547
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        574..592
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        691..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        747..767
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        840..869
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   DOMAIN          86..303
FT                   /note="Anoctamin dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16178"
FT   DOMAIN          306..883
FT                   /note="Anoctamin transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04547"
SQ   SEQUENCE   929 AA;  109056 MW;  6862E7F4772E5E24 CRC64;
     MNRLGRKDNE TLIEMSLATD GEDSNGPLCE TISNTESELR SNSEGLSSTE TSLLIPDHQV
     TGRRYNLFLK RRLRINKRHQ SKDSVFFRDG VRRIDFVLSY LDDPNKEEEK KVERRREFEK
     NLQKAGLELE TEDKKESEDG KTYFVKIHAP WEVLITYAEV LNIKAPIKEN DIPPTVENPL
     DCMLEPFRLP EKVMHPEPDY FTAPFSKSRQ ELYLIDNEST FFSASRRNRI VYYILTRCPY
     GTEEGKKKFG IKRLLSNGTY TAAYPLHDCQ YWKKSNDPNC DNERYTLYME WARFLRFYKE
     QPLDLIRKYY GEKIGIYFAW LGFYTEMLFF AALVGLICFL YGLFTMDENM SSTEICAPAI
     GGEIIMCPLC DEKCEYWKLN TTCESSKYSH LFDNVATLFF AIFMGIWVTL FLEFWKRRQA
     RLKYEWDLVD FEEEQQQLQL RPEYEAKCTH RKKNPVTQEM EPYLPLTSQA VRFCISGTTV
     LFWISLIIAS MIAVIVYRLA VYAAFASIME NTQTLQPISG LLTPQLATSV TASCLNFVII
     MILNFLYEKI AVWITDMEIP RTHLEYENRL TMKMFLFQFV NYYSSCFYVA FFKGKFVGYP
     GTYTYMFSRW RNEECDPAGC LIELTTQLTI VMAGKQIWGN IQEAIVPWIW NWWGRRKARC
     NPENLYSRWE QDHDLQSFGA LGLFYEYLEM VIQFGFITLF VASFPLAPLL ALMNNILEIR
     VDSWKLTTQF RRPVAAKAHS IGVWQEILNG MAILSVVTNA FIVAFTSDMI PRLVYYYAYS
     TNEDSPMSGY INNSLSVFQV SDFLEGKRPE NNPENFLTCR YRDYRYPPGH EKKYLHTMQF
     WHILAAKMAF IIIMEHIVFI VKFFVAWMIP DVPAEVKARI KREKFLTQKI LHEYELNKLK
     QKLCECKTYE NMEKEVIATE GKVELSQAM
//
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