ID M3XW97_MUSPF Unreviewed; 1274 AA.
AC M3XW97;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Rho GTPase-activating protein 29 {ECO:0000256|ARBA:ARBA00040783};
DE AltName: Full=Rho-type GTPase-activating protein 29 {ECO:0000256|ARBA:ARBA00042921};
GN Name=ARHGAP29 {ECO:0000313|Ensembl:ENSMPUP00000003347.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000003347.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000003347.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
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DR EMBL; AEYP01031841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01031842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3XW97; -.
DR STRING; 9669.ENSMPUP00000003347; -.
DR Ensembl; ENSMPUT00000003412.1; ENSMPUP00000003347.1; ENSMPUG00000003377.1.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT00950000183110; -.
DR HOGENOM; CLU_006236_2_0_1; -.
DR InParanoid; M3XW97; -.
DR OMA; AWVEKRI; -.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20816; C1_GMIP-like; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR15228:SF7; RHO GTPASE-ACTIVATING PROTEIN 29; 1.
DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 192..474
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 625..670
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 684..899
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 361..413
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 494..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1274 AA; 143491 MW; 18B417D5D3FE4DD4 CRC64;
MIAHKQKKTK KKRILSSGQL STDVTTPEMG LKSISSNSIF DPDYIKELVN DIRKFSHMLL
YLKEAILSDC FKEVIHIRLD ELLHVLKSVM NKHQNLNSLD LQNAAEMLTA KVKAVNFTEV
NEENKNDLFR EVFSSIETLA FTFGNILTNF LMGDVGNDSL LRLPVSRESK SFENVSVESV
DSSNEKGNFS PIELDSVLLK NTDSVELALS YAKTWSKYTK NIVSWVEKKL NLELESTRNV
VKLAEATRSN IGIQEFMPLQ SLFTSALLND IKNSRLLQQT IAALQANKFV QPLLGRKNEM
EKQRKEIKEL WKQEQNKLLE TETALKKAKL LCMQRQDEYE KAKSSMFRAE EEHLCSSGGS
VKNLNKQLEK KRRLEEEALQ KVEEANELYK VCVTNVEERR NDLENTKREI LTQLQKLVFQ
CDLTLKAGKL LGVRLLDVMV TVNLFQMQHL QAASLANNLQ SLCDSAKLYD PGQEYSEFVK
ATNATEEEKV DGNINKPLTN SPHTSGYRPT DSLEDVVRLP DSSSKIEEDR CSNSADVTGP
SFIRSWTFGM FSDSESTGGS SESRSLDSES ISPGDFHRKL PRTPSSGTMS SADDLDEREP
PSPSEAGPNS LGTFKKTLMS KAALTHKFRK LRSPTKCRDC EGIVVFQGVE CEECLLVCHR
KCLENLVIIC GHQKLPGKIH LFGAEFIQVA KKEPDGIPFV LKICASEIEN RALCLQGIYR
VCGNKIKTEK LCQALENGMH FVDISEFSSH DICDVLKLYL RQLPEPFILF RLYKEFIDLA
KEIQHVNEEQ ESKKDNPEDK KWPSTCIEIN RILIKSKDLL RQLPVSNFNS LHYLIVHLKR
VVDHAEENKM NSKNLGVIFG PSLIRPRPTT APVTISSLAE YSNQARLVEF LITYSQKIFD
GSLQPQEVVV YSTGGGVPHV DQGCLPKPLL SPEERDPEHS MKTLFFSSKE DMHTVDSETK
IFEPATSFEE SERKQNALEK CDTFLIDNKV GLLVNQELES ASQKMEDVCK TYKPLTLKSE
RETNSVERHA PRTKVRPASL PVDRLLLLAS PPNERTVRNM GNVNSDKFCK NPTFDGVSRK
DIPTIVCSKL DGFDQQTLQK TRERQYEQNG LSAKTAAGMG TVSVRIGGDQ PDSAPWPSKP
YTEPVRSVRQ VSERRSSDSC PPAAVRAPRT LQPQHWTTFY KPRAPTSSLR GDEERLATPS
PALPPSTAPT PQGPLLKTVP ASDKAPAAST QSTSKPGENS EERDLPEVPP ACQRPRLKRM
QQFEDLEDEI PQFV
//
