ID   A0A1S3KTC2_SALSA        Unreviewed;       945 AA.
AC   A0A1S3KTC2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
GN   Name=LOC106561971 {ECO:0000313|RefSeq:XP_013981941.1,
GN   ECO:0000313|RefSeq:XP_013981942.1, ECO:0000313|RefSeq:XP_013981943.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013981943.1};
RN   [1] {ECO:0000313|RefSeq:XP_013981941.1, ECO:0000313|RefSeq:XP_013981942.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013981941.1,
RC   ECO:0000313|RefSeq:XP_013981942.1};
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_013981941.1; XM_014126466.1.
DR   RefSeq; XP_013981942.1; XM_014126467.1.
DR   RefSeq; XP_013981943.1; XM_014126468.1.
DR   OrthoDB; 534027at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa11.
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:SF87; ANOCTAMIN; 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:UP000087266};
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        335..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        412..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        498..520
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        540..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        584..605
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        709..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   DOMAIN          56..321
FT                   /note="Anoctamin dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16178"
FT   DOMAIN          324..903
FT                   /note="Anoctamin transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04547"
FT   REGION          17..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          922..945
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        925..945
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   945 AA;  108982 MW;  3F6E3789A06C9CEC CRC64;
     MRRNDYYIPV SCEEKAADFG NTKDGGDSKY NKYDSIPLNS LKSDEAASGP KQGPTFQDGQ
     RRVDYVLTYH IQKPQSFRRK TSHFGDYRIL RSLRRSLSMM RGRDTPPPKE DPEVAAHKHR
     HDYHEDDKRF RQTEFEDNLR EMGLELEKDE GNKIPGIGFL KIHAPWNVLC REAEFMKLKM
     PTKKVYEVKQ GSDVVERINL FIRKVTAPLH PKVEPNRAQN VKHLSHPFSR EKQHLFDLSD
     RESFFDSKTR ASIVYEVLKR TRCTKAKYTM GITSLLGNGV YTAAYPLHDG DVDGMGPEAN
     DRKILYEEWA SYSVFYKYQP IGLIRKYFGE KIGLYFAWLG VYTQMLIPAA IVGAIVFLYG
     CATVDNDIPS MEICDPRNNI TMCPLCDRAC SYWKLKTACG TARASHLFDN PATVFFSIFM
     ALWAAMFMEH WKRRQMRLNY IWDLTGFEEE EQTHKGHHRA EYEIQVMQKT LKKQDMSPKD
     KKVKLTCTDR APAYMTGLFT MLFMVGVTFA VVFGVILYRI SIRAALHMSS NPTARTNIRA
     TVKGTAAVIN LVIIIIMDEV YGALARWLTL LEVPKTDKSF EERLIIKTFV LKFANAFSPI
     VYLAFFRGRM VGRPGDYLYV IGSYRMEECA HAGCLMELCI QLCITMLGKQ LIQNNLFEIG
     IPKIKKLIRR RKSDMDSQQQ EDYNMTLQRH EKDHFLGPFV GLSPEYMEMI IQFGMVTLFV
     ASFPLAPLFA LLNNIIEIRL DAKKFVTEVR RPIAGSAKDI GIWYNLLRGL SKVAVIVNAF
     VISFTSDFIP RLVYQYMYSP DGSMHGFVNH TLSYFNVSDF QPGTAPLQPM HLGYEVQICR
     YKDYRETPWS NTPYDLSKEF WAILACRLAF VVVFQNVVML MSDFVDWLIP DIPKDISLQI
     HKEKILMVEL FMKEEEGKKL LRDSHANQSP LQPRSRPASH TPSNC
//