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Database: UniProt
Entry: A0A452HCP2_9SAUR
LinkDB: A0A452HCP2_9SAUR
Original site: A0A452HCP2_9SAUR 
ID   A0A452HCP2_9SAUR        Unreviewed;      1027 AA.
AC   A0A452HCP2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
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:ENSGAGP00000012558.1, 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:ENSGAGP00000012558.1}
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   AlphaFoldDB; A0A452HCP2; -.
DR   Ensembl; ENSGAGT00000014395.1; ENSGAGP00000012558.1; ENSGAGG00000009645.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR007632; Anoctamin.
DR   InterPro; IPR049452; Anoctamin_TM.
DR   PANTHER; PTHR12308; ANOCTAMIN; 1.
DR   PANTHER; PTHR12308:SF51; ANOCTAMIN-8; 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: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        198..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        232..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        303..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        387..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   DOMAIN          187..791
FT                   /note="Anoctamin transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04547"
FT   REGION          471..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          900..1027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..488
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..632
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..858
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        900..922
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        970..985
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1006..1027
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1027 AA;  116624 MW;  9A30F62C6C84D577 CRC64;
     MSHKSWMKTV PTENCDVLMT FADTTDDHTL LWLLNHIRLG IPELIIQIRH HRHTKVYAFF
     VTATYESLLR GADEIGLRKP VKAEFGGGTR SFSCEEDYIY ENIENELFFF TSQERQNIIR
     YWLENLRAKH GESLHNIQFL EGQPVIPELV ARGVIQQVFP VHEQRILNRL MKSWVQAICE
     AQPLDEICDY FGVKIAMYFA WLGFYTSAMV YPAVFGSILY TFSENDQTSR DICCVVFAIF
     NVIWATLFLE EWKQRGAEFA YKWGTLDTPA ESIEEPRPQF RGLKRISPVT NVEEFYYPPW
     KRLLFQCLVS LPVCLICLSF VFFVMLGCFE LQEFVLSIKE LPRLIRFLPK IALALIVTAC
     DDVYRKIAYW LNDMENYRLQ SAYEKHLIIK IVLFQFVNSY LSLFYIGFYL KDMERLKEML
     ATLLITRQFL QNIKEVSQPH LYRKIQRGDL SLQNIRDISH TIFRLLAQRY TAPRPGPEPR
     PAEQPARPGP EPEGAGKGPQ GEKCLNGGCG VPEEEEKQES DSEDESVLDC GLKLKKVSFI
     ERAERRGREL GAMEDASFLE EGSPTMVEKG MDPASVFELA EDEEESDGPS GSPLPEAKEL
     AVTLRARRGR VAESQEEEEE EEGRKRNRAS WIDPPEENYS PHLTQAEVES CMKKYEDTFQ
     DYQEMFIQFG YVVLFSSAFP LAALCALINN IIEIHSDAFK LCTGLQRPFG QRVESIGQWQ
     KVMEAMGVLA IVVNCYLIGQ CGQLQRLFPW LSPEGAIISV VVLEHFALLL KYLIQVAIPD
     IPAWVAEEMA KLEYQRREAF KKHERQAQHH YQQQQRRKRE EEERQRQAEY HARKERETSR
     DEGKPEAAGQ DPGHEKSQAK IKGPSGLSHS SEKPKRPSSL LATNNVMKLK QIIPLQSKFL
     SGGSAGTAST ATAQSPTGSE NKLPGFLSFK FLKSPETKRD GGTEKVQSPT KPFNPGKLFN
     FGKSEGAGGS GASGNGTTAS PPQRPAPSSE GGEKQPPSKA HLNGLVDEGG MEEGELRAEE
     ESTGHKL
//
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