ID A0A0D9RY99_CHLSB Unreviewed; 908 AA.
AC A0A0D9RY99;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=MICAL like 2 {ECO:0000313|Ensembl:ENSCSAP00000013588.1};
GN Name=MICALL2 {ECO:0000313|Ensembl:ENSCSAP00000013588.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000013588.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000013588.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000013588.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AQIB01147378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01147379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01147380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01147381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008017071.1; XM_008018880.1.
DR AlphaFoldDB; A0A0D9RY99; -.
DR STRING; 60711.ENSCSAP00000013588; -.
DR Ensembl; ENSCSAT00000015655.1; ENSCSAP00000013588.1; ENSCSAG00000017567.1.
DR GeneID; 103246882; -.
DR KEGG; csab:103246882; -.
DR CTD; 79778; -.
DR eggNOG; KOG0517; Eukaryota.
DR GeneTree; ENSGT00940000160222; -.
DR OMA; DWFQLIH; -.
DR OrthoDB; 2872403at2759; -.
DR BioGRID-ORCS; 103246882; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 28.
DR Bgee; ENSCSAG00000017567; Expressed in adrenal cortex and 5 other cell types or tissues.
DR GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0042805; F:actinin binding; IEA:Ensembl.
DR GO; GO:0031005; F:filamin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0030041; P:actin filament polymerization; IEA:Ensembl.
DR GO; GO:0070830; P:bicellular tight junction assembly; IEA:Ensembl.
DR GO; GO:0032456; P:endocytic recycling; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR CDD; cd21253; CH_MICALL2; 1.
DR CDD; cd09444; LIM_Mical_like_1; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF54; [F-ACTIN]-MONOOXYGENASE MICAL; 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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
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 4: Predicted;
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:UP000029965};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 1..107
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 186..248
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 725..876
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 117..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 739..773
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 262..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..661
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 908 AA; 98108 MW; F30262868A99435E CRC64;
MAAIRALQQW CRQQCEGYRD VNICNMTTSF RDGLAFCAIL HRHRPDLINF NALKKENIYE
NNKLAFCVAE EHLGIPALLD AEDMVALKVP DRLSILTYVS QYYNYFHGRS PIGGMAGVKR
ASEDSEEEPS EKKAPVQAAT LPSPTPARKP PLSPAQTNPV VQRRNGGTEG PPPKTGQVSV
GSSVSSICGI CGKHVHLVQR HLADGRLYHR SCFRCKQCSC TLHSGAYRAT GEPGAFVCTS
HLPTTTSASP KLPGLVPQRP GSMAVNSRTP CSPQKAQEAN KPKARPSAWE PAAGNSPARA
SVPTAPNPPA TSAASIRVRS PARPSESRLA PTPLEGKVRP RVTNSSPMGW SSAAQRTAAA
ASHPAVPPSA PDPRPATPQG GGAPRVAAPQ TTLSSSSTSA PTVDPPAWTP SASRTQQARN
KFFQTSAVPP GTSPAGRGPA SSLAPSRDSS KEQARDFLRQ ALSALEEAGA PTPGRPSPAT
APVPSSQPKT ETPQASPLAK PLQPTSPQAL GLPSRTDPPA PLSTSSTSQA SVSPPAGRRS
LAEPSGIGRV GAGSRPKPEA PTAKGKSTTL TQDRSASPQE GQEDGPAGWR ANLKPVDRRS
PAERTLKPKE PRALAELRAG EAPGKVSGSF SGSVHITLTP VRPERTPHPA SPGPSLPARS
PSPPRRRRLA IPASLDVSDN WLRPEPPEQE AQAQSWKEEE KKPHLQGKPG RPLSPANVPA
PPGETVTSPV RLHPDYLCPE EIQRRLQDIE RRLDALELRG VELEKRLRAA EGDDAEDGLM
VDWFWLIHKK QLLLRQESEL MYKSKDQRLE EQQLDIEGEL RRLMAKPEAL KSPQERQREQ
ELLERYVGTV NDRSDIVDSL DEDRLREQEE DQMLRDMIEK LGLQRKKSKF RLSKIWSPKS
KGKSSTSQ
//
