ID A0A1S3MH91_SALSA Unreviewed; 1301 AA.
AC A0A1S3MH91;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Molecule interacting with CasL protein 1 {ECO:0000256|ARBA:ARBA00044245};
DE EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
DE EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
GN Name=LOC106572625 {ECO:0000313|RefSeq:XP_014002449.1};
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_014002449.1};
RN [1] {ECO:0000313|RefSeq:XP_014002449.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014002449.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-methionyl-[F-actin] + NADPH + O2 = H2O + L-methionyl-
CC (R)-S-oxide-[F-actin] + NADP(+); Xref=Rhea:RHEA:51308, Rhea:RHEA-
CC COMP:12953, Rhea:RHEA-COMP:12956, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16044,
CC ChEBI:CHEBI:45764, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.14.13.225; Evidence={ECO:0000256|ARBA:ARBA00001591};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000547};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endosome membrane {ECO:0000256|ARBA:ARBA00004608}. Midbody
CC {ECO:0000256|ARBA:ARBA00004214}.
CC -!- SIMILARITY: Belongs to the Mical family.
CC {ECO:0000256|ARBA:ARBA00008223}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014002449.1; XM_014146974.1.
DR STRING; 8030.ENSSSAP00000050955; -.
DR PaxDb; 8030-ENSSSAP00000050955; -.
DR GeneID; 106572625; -.
DR OMA; AKTSEMQ; -.
DR OrthoDB; 5399346at2759; -.
DR Proteomes; UP000087266; Chromosome ssa15.
DR Bgee; ENSSSAG00000050253; Expressed in pharyngeal gill and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd22198; CH_MICAL_EHBP-like; 1.
DR CDD; cd09439; LIM_Mical; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF35; [F-ACTIN]-MONOOXYGENASE MICAL1; 1.
DR PANTHER; PTHR23167; CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED; 1.
DR Pfam; PF12130; bMERB_dom; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM01203; DUF3585; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR PROSITE; PS51848; BMERB; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 508..614
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 703..765
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1135..1281
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 651..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1145..1172
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 651..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..884
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1097
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1301 AA; 147083 MW; 4ABF2F3DEB55067D CRC64;
MANQDLTSPS HALFEQFVQA QTCKEVQRTF SELCHHLQVD PRDYQSFYTK LKERLNYWKA
KSLWVKLDKR AQHQDYQQGE VCAKNKCLVL GAGPCGLRTA IELALLGAHV VVLEKRDSFS
RNNVLHLWPY TIYDLRGLAA KKFYGKFCTG ALDHISIRQL QLILLKVCLL LGVEVQTGVE
FKGFVEPSGA TGWMAKLFPD NHPAGKFQFD VFIYAGGGSF VPYGFKRKEL RGKLAIGITC
NFINRHTAAE AQVAEISGVA RIYNQKFFQD LLAETGIDLE NIVYYKDDTH YFVMTAKKKS
LLKMGVIKQD FSDADKLLAQ VNVDQEALLR YAYDAAQFST GHCLPDMQFA QNHAGQPDVA
MFDFTCMHRA ENASLVRERK GKKLLMGLVG DCLVEPFWPL GTGIARGFLA AFDTAWMVRS
WGKGRPHMEV LAERESLYQL LSQTTPENTS KKYSAFSIDP ATRYQHVNLN SVKAIQVKRL
YDVEERLNPG RPTKKPKGKW SHLQQDSVGA FEVLLKWCQQ HTAGYDRVKV NDLNQSWRSG
LALCALINTF RPRVIDMSSL EESNAVYNNQ LAFNFLEREL GIPPIMSANE MSFKGQIDKL
SMVHYLTQIH DAFNERTPTK EPQSLPLKPS KTLSFRAAVV FLNNLKHNSL QRRKERLASK
KEEKGMMGEE KDPVAPLSAP KVTPDPVNPD PELSLTPGIS SNEECYFCCQ RVYVLERIST
EGKLFHRSCF TCHQCGTTLR LGGYTFNQHT GKFYCELHSE QLEMENGEQC PSVQDTIEDH
NEKERGVNGI SSEEHSPCPS EDDDEEYSLD LGLPKPIAPQ GEEHPSSKQS NPVEEPHIPP
NPPIDVFLKK GFNAFNVEEE KQGKERVEDP PSYPPTPVPK PRLSCSDIPS PQASPPVPKP
RTVLPTPKRD MSPAHVGEKG SLRAAGEKGT PKAAPDPDSR AKQSLRKLQL TDKKNPLVNL
SFSLDSDSET PGSSSCSSST ATAGGPSPPK PPDCQEEEEG YWIGGPRPAG HIRELRNRRC
FRRKEEPDEG QGQHGRVRSK FSPWNLSSPR PRRDYRFSVL NSHPEVHYHH SVSEDGGADH
DDDDDDDDDD DDELDMFGVD GMDLYDDKFQ IIPSDPVKAE KLQLMKVRTL MRRAKTSEMQ
RFHKAQSIQR RLEEIEVTYK ELEDKGVVLE QVLRGEEDSC GSPGMIDQWV HLVHQKNTLV
SEESDLMVAS RQLELEDKQS TLEMELRQYE LDDSEKTVEQ QAEEERVLQD MLEVVDMRNS
LVAFLDEKRL QETDTDEQQS TSLLEVKRHS TASVGAQVYW A
//
