ID   A0A3Q3BQL7_KRYMA        Unreviewed;      1070 AA.
AC   A0A3Q3BQL7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000028759.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000028759.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU280814}.
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DR   RefSeq; XP_017288062.1; XM_017432573.1.
DR   AlphaFoldDB; A0A3Q3BQL7; -.
DR   Ensembl; ENSKMAT00000029121.1; ENSKMAP00000028759.1; ENSKMAG00000021289.1.
DR   GeneID; 108245555; -.
DR   CTD; 566373; -.
DR   GeneTree; ENSGT00940000155840; -.
DR   OrthoDB; 534027at2759; -.
DR   Proteomes; UP000264800; Unplaced.
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:SF20; ANOCTAMIN-2; 1.
DR   Pfam; PF16178; Anoct_dimer; 1.
DR   Pfam; PF04547; Anoctamin; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280814};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
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        394..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        471..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        567..593
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        613..641
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        662..679
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        782..805
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        939..960
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   DOMAIN          94..380
FT                   /note="Anoctamin dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16178"
FT   DOMAIN          383..974
FT                   /note="Anoctamin transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04547"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1049..1070
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          534..561
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        9..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1070 AA;  120946 MW;  B9F930249CB805B6 CRC64;
     MALRRSPSST CAEPWSNGAG FRQPSTALSE SSSIHSDALC HLNRDMSGIG LKPMPYSILE
     PEALKEEPWS EESQHLLQVV GVTSSPQASG EGLYFCDGRR KVDYVLVFHH RRHSSIRSPA
     GAAFPQDELS IVSNGNFPPT VGSDSAPGRG GGGLRREEAA SVGEVFMELG NARGNEPMEA
     AAQEMHLIRQ EFESNLLEAG LEMERDRDVK THGPSFTRVH APWPVLCREA EFLKIKVPTK
     TSYELKEEKG FGSSMSTMWR KLNQPFQPKV SHQDHGSTKF ISHCFSRDKL HLYNITSKDT
     FFDNATRGRI VYEILRRTVC VRTCQTIGIS TLIAKGVYDA AFPLHDGDYK VIGQLEEQND
     RQVLHEEWAR YSAFYKYQPI DLVRKYFGEK IGLYFAWLGV YTQLLILASI VGIIVFGYGV
     ATMDTNIPSL EMCDDRLNFT MCPLCDGACD YWHLSTACGT ARASHLFDNP ATVFFAIFMS
     LWAVLFLEQW KRRQISLGFS WDLTGMDEDE DSIAFCDGKW SFMEHPRPKY ETILLQKRQK
     KQEKKKKKKK KEAAVEKLTW KDRLPGYFMN VSSILFMFGL TFSAVFGVIV YRITVSALMA
     MSPDPETKSN VRVTVTATAV IINLVVILIL DEIYGSVALW LTELEIPKTE TNFEEHLILK
     AFLLKFMNAY APIFYVAFFK GRFAGRPGSY VYVFNNYRME ECAPGGCLIE LCIQLSIIML
     GKQLIQNNIF EIGIPKLKKL IRALKEKKTT PKESEEERPP QQWNLDYALA PFEGLTPEYM
     EMIIQFGFVS LFVASFPLAP LFALLNNVIE IRLDAKKFVT ELRRPVAARA KDIGIWYNIL
     SGMGKLSVII NAFVISFTSD FVPRLVYQYM FSQTGTMHGF IDHTLSYFNV SNFRPGTAPL
     STEHGDISVC RYKDYREPPW SPDAYQFSKQ YWCVLSARLA FVILFQNLVM FLGLMVAWVI
     PDVPKTIVEQ LKREKKLLVN LFLQEEKEKL QLIQSLFVKD ASLHPDNQAP NQGQGFPILG
     RYSTLPIGPT AGDGGGGPRA RCRAASFSQF SGNSSSLPRK ENANSRHTAV
//