ID A0A1S3MX03_SALSA Unreviewed; 1318 AA.
AC A0A1S3MX03;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Trichohyalin-like isoform X2 {ECO:0000313|RefSeq:XP_014007635.1};
GN Name=LOC106575573 {ECO:0000313|RefSeq:XP_014007635.1};
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_014007635.1};
RN [1] {ECO:0000313|RefSeq:XP_014007635.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014007635.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family.
CC {ECO:0000256|ARBA:ARBA00007655}.
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DR RefSeq; XP_014007635.1; XM_014152160.1.
DR OrthoDB; 4213792at2759; -.
DR Proteomes; UP000087266; Chromosome ssa17.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR CDD; cd03061; GST_N_CLIC; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR002946; CLIC.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR00862; O-ClC; 1.
DR PANTHER; PTHR45476:SF1; CHLORIDE INTRACELLULAR CHANNEL PROTEIN 6; 1.
DR PANTHER; PTHR45476; CHLORIDE INTRACELLULAR CHANNEL PROTEIN 6-RELATED; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR PRINTS; PR01263; INTCLCHANNEL.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Chloride channel {ECO:0000256|ARBA:ARBA00023173};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022882};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT DOMAIN 1101..1163
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13409"
FT REGION 1..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..67
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..977
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1318 AA; 147482 MW; AE99B9BAD42A634B CRC64;
MAQSEPNGLS PDLSNGAIIH SPIGTCTDPD RQRQRDEEEE EEEDVELAEE VLELGEEVGE
DMEDIGMTGE GEGAADHFEV TMQASGSGGK EGEEGERGIE EEVGLQEKRE GDKGEGERTV
PVVVIEEEQE KSVEAVEEEK SAEREESAGA DKEREIEERE PPLPPPSPSL PETESINDEV
ERKDEETSPE AEKAQIVLPV DETEKTEDDV GLMTTEPPVL STNDEVASKE ELCTESRKPE
TTSTTDELAK GEQSGGQDAE MPISQETNDD GMARVSDESR SQVTDDCQTV STSDEVRETR
QEEGQEEEPK HQSANDNEGE SEESNNKLAK NRQVSQEERD ENQQGSEKST EKKEEVKSPI
TEEQGETTKA VLEKKEEGHQ ATEHQPPLFV TKKFIELGVV KSQATTAQQP QEVVTPPVEV
EGGSKSKAQP LIQPNESQEG ENGAKEEGGL QQTEQQLQVE EGDSDRAVEG GGGEREEPQQ
VGDNAVVGMD TGGSKVEVEQ KKEDNVDIAE EERRGGGMEE QTEKALEPDN AAREEGEKKE
GKVVAQPQVQ ILKGSAGATQ EDDDKDLEHV EEAFELEEGG DMEKEQPGEV ILDEPGAAEV
GGAEEMDNPV PVSEIGTGGA EGGGELEELP VTNINDNLDS QSEGAIEMAE EPEDLIEDES
KSALEGGSKR VEQPVPATKD EPVKFGKEYT AKERRKENKE EVELGVKGRK ARIENGFPGT
EEVKRQLLNE MLLSPTRLRQ GEMKEEATVK RDRVTPRRGS NDWIKKGAPE EVQTRRGSND
WNKKGAPEEV QTRRGSNDWN KKGAPEEVQT RRGSNDWNKK GAPEEVQTRR GSNDWNKKGA
PEEVQTRRGS NDWNKKAAPK EAQTRRGSND WNKKGAPEET QTRRGSNDWN KKGAPEEAQT
PWRREDWAKK AAPEEVQTRR RSDDWIKKAP EEAQTPGWRE DWIKKLSPEE AQTPERKEDG
IKKLSPEEAQ TPGRREDWIK ELKSVLKEEV LSPKRREEPV KKKKKKVVVM DEVPTFMHQR
TEVKKEKKKV VVMDEVPTFM HQRTEVKIEV KKEKEAQGEE KSVRLQSPTP HGEDRDSPDP
QEYEISLYVK AGSDGESIGN CPFSQRLFMI LWLKGVIFNV TTVDLKRKPA DLQDLAPGTN
PPFVTFNGEV KVDVNKIEEF LEEKLTPPRY PKLATKHPES NTAGIDVFSK FSAYIKNPRK
DTNDGLEKAL LKSLRRLDEF LRTPLPEEIN ANSTEDPQES TRCFLDGPDL TLADCNLLPK
LHIIKVVARK YRGFEIPVEM AGVWRYLNHA YKREEFTNTC PVEREIEFAY IDVAKRIK
//
