ID   A0A2Y9JUJ9_ENHLU        Unreviewed;       952 AA.
AC   A0A2Y9JUJ9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
GN   Name=LOC111150126 {ECO:0000313|RefSeq:XP_022363209.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022363209.1};
RN   [1] {ECO:0000313|RefSeq:XP_022363209.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022363209.1};
RG   RefSeq;
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_022363209.1; XM_022507501.1.
DR   AlphaFoldDB; A0A2Y9JUJ9; -.
DR   Proteomes; UP000248482; 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:SF13; ANOCTAMIN-1; 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:UP000248482};
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        331..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        408..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        490..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        536..560
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        580..601
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        706..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   DOMAIN          54..317
FT                   /note="Anoctamin dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16178"
FT   DOMAIN          320..899
FT                   /note="Anoctamin transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04547"
FT   REGION          89..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          928..952
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   952 AA;  109888 MW;  63C233EF2CFABB5E CRC64;
     MRVNEKYSTL PAEDRSVHII NICAIEDIGY LPSEGTLLNS LSVDPDAECK HGLYFRDGRR
     KVDYVLVYHP KRPSGGRTLA RRVQHGDVTP AARGARQDQP LPGKGSVGAA GGPEPPMDYH
     EDDKRFRREE YEGNLLEAGL ELERDEDTKI HGVGFIKIHA PWNVLCREAE FLKLKMPTKK
     LYHINEPRGL LKKISSVLQK ITDPIQPKVA EHRPQTTKRL SYPFSREKQH LFDLSDKDSF
     FDSKTRSTIV YEILKRTTCT KAKYSMGITS LLANGVYSAA YPLHDGDYEG ENVDFNDRKL
     LYQEWASYGV FYKYQPIDLV RKYFGEKIGL YFAWLGVYTQ MLIPASVVGI IVFLYGCATV
     DENIPSMEMC DHRQNITMCP LCDKTCSYWK MSSACATARA SHLFDNPATV FFSVFMALWA
     ATFMEHWKRK QMRLRYHWDL TGFEEEEEAV KDHPRAEYEA RVLEKSLRKE SKKKETDKVK
     LTWRDRFPAY FTNLVSIVFM IAVTFAIVLG VIIYRISMAA ALAMNSSPSV RSNIRVTVTA
     TAVIINLVVI ILLDEVYGCI ARWLTKIEVP KTEKSFEDRL IFKAFLLKFV NSYTPIFYVA
     FFKGRFVGRP GDYVYIFRSF RMEECAPGGC LMELCIQLSI IMLGKQLIQN NLFEIGIPKM
     KKFIRYLRLR RQSPPDHDPY VKRRQRYEED YTLEPFAGLT PEYMEMIIQF GFVTLFVASF
     PLAPLFALLN NIIEIRLDAK KFITELRRPV AVRAKDIGIW YNILRGVGKL AVIINAFVIS
     FTSDFIPRLV YLYMYSENGT MHGFVNHTLS SFNVSDFQNG TAPNDPLDLG YEVQICRYKD
     YREPPWSEHK YDISKDFWAV LAARLAFVIV FQNLVMFMSD FVDWVIPDIP KDISQQVHKE
     KVLMVELFMR EEQGKQQLLD TWMEKDRKKD EPCNNHGPKA CLDSPEYPGG AL
//