ID A0A2K6FI07_PROCO Unreviewed; 1037 AA.
AC A0A2K6FI07;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Multifunctional ROCO family signaling regulator 1 {ECO:0000313|Ensembl:ENSPCOP00000013607.1};
GN Name=MFHAS1 {ECO:0000313|Ensembl:ENSPCOP00000013607.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000013607.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000013607.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K6FI07; -.
DR STRING; 379532.ENSPCOP00000013607; -.
DR Ensembl; ENSPCOT00000024211.1; ENSPCOP00000013607.1; ENSPCOG00000018440.1.
DR GeneTree; ENSGT00940000158928; -.
DR OMA; IVCPKNG; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IEA:Ensembl.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway; IEA:Ensembl.
DR GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; IEA:Ensembl.
DR GO; GO:0043030; P:regulation of macrophage activation; IEA:Ensembl.
DR GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; IEA:Ensembl.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020859; ROC_dom.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF39; MALIGNANT FIBROUS HISTIOCYTOMA-AMPLIFIED SEQUENCE 1 HOMOLOG; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08477; Roc; 1.
DR SMART; SM00364; LRR_BAC; 11.
DR SMART; SM00369; LRR_TYP; 13.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF82615; Polo-box domain; 1.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 398..644
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT REGION 430..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1037 AA; 115227 MW; FB65F161EE9A78D1 CRC64;
MAGKDSGNLK TVRLWRDAAL RARKLRSNLR QLTLSAAGGS DPLESPDAPL LVLPANIGDI
EVLNLGNNGL EEVPDGLGSA LGSLRVLILR RNRFARLPPA VAELGHHLTE LDVSHNRLIA
LGAEVVSALR ELRKLNLSHN QLPALPAQLG ALAHLEELDV SFNRLAHLPD SLSCLSRLRT
LDVDHNQLTA FPRQLLQLPA LEELDVSSNR LRGLPEDISA LSALKILWLS GAELGTLPAG
FCELASLESL MLDNNGLQAL PAQFSRLQRL KMLNLSSNLF EEFPAALLPL AGLEELYLSR
NQLTSVPSLI AGLGRLLTLW LDNNRIRYLP DSIVELTGLE ELVLQGNQIA VLPDNFGQLS
RVGLWKIKDN PLIQPPYEVC MKGIPYIAAY QKELAHSQPA VQPRLKLLLM GHKAAGKTLL
RHCLTEDRVE GGQGAGDKEQ SFPPSPAPVS KGIEVTSWTA DASRGLRFIV YDLAGDESYE
VIQPFFLSPG ALYVLVVNLA TYEPRRFPSA VGSFLRRVGA RVPHAVVCIV GTHTDLCGER
ELEEKCLDIH RQIALQEKHD AEGLSRLARV VDEALARDFE LRSASPHAAY YGVSDKNLRR
RKAHFQYLLN HRLQILSPVL PVSCRDPRQL QRLRDKLLSV AEHREIFPNL HRVLPRSWQV
LEELHFQPPQ AQRLWLSWWD SARLGLQAGL TEDRLQSALS YLHESGKLLY FEDSPALKEH
VFHNLTRLID ILNVFFQRDA SLLLHKLLLG TSGEGEGEGE SSTTMALSTP SQDLLRATQL
HHYVEGFLLH GLLPAHVIRL LLKPHVQAQQ DLQLLLELLE KMGLCYCLNK PKGKPLNGST
AWYKFPCYVQ NEVPHAEAWI NGTNLAGQSF VAEQLQIEYS FPFTFPPGLF ARYSVQINSH
VVHRSDGKFQ IFAYRGKVPV VVSYRPAKGV LQPDTLSIAS HASLPNIWTA WQAITPLVEE
LNVLLQEWPG LHYTVHILCS KCLKRGSPNP HAFPGELLSQ PRPEGVAEII CPKNGSERVN
VALVYPPTPT VISPCSK
//