ID A0A3Q4H3V5_NEOBR Unreviewed; 1080 AA.
AC A0A3Q4H3V5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
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};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000016336.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000016336.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q4H3V5; -.
DR STRING; 32507.ENSNBRP00000016336; -.
DR Ensembl; ENSNBRT00000016775.1; ENSNBRP00000016336.1; ENSNBRG00000012590.1.
DR GeneTree; ENSGT00950000183110; -.
DR OMA; AWVEKRI; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000012590; Expressed in liver and 7 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20816; C1_GMIP-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 85..356
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 468..513
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 527..743
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 237..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1035
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1080
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1080 AA; 121414 MW; 177F2C3D7BC27DB2 CRC64;
VLKAIISKHQ SLNSVDILST AGTVIATVKG VNFKEVNEDN KHKHFGEIYA AIDTLAFTFG
NVVSDFLMGD VENGSVLGLP LTKRSRVREV QYLKSSPPVR AEEVDRTLQR QDSGVESALA
YAKAWSKYTK ELLAWVEKRL NMVDLTYIGI EFMPFREIYM TAFKNDIEYS QLILQTAAIL
QSNKFMQPLL ARKNELDKLR KEVKEQWQRE QKKMHEADTA LRKARLLQTQ RQDEYEKAKV
STSRLEEEQT GGGGGAAAAK QLEKRRRLEE EALQKAEEAK DHCKACQVDV GVKRVELVNT
KNEIITQIRE MVSQCDLTLK AVTVNWFQLQ QAQVVSLPVN HQTLCENAKL YEPGQRYIDF
VRSLPTDAPR LECHSLDSPA PFRPWTSANQ GGGMCSDSES AGGSSESRSM DSPTASPGDF
KRRLPRTPST GTMSSADDLD EREPPSPSDN GNSPGPFRNT QMSKAAQTHK LRKLRAPSKC
RECDSLVVFH GAECEECSLA CHKKCLETLA IQCGHKKLQG RLHLFGIDFT QSAKNSQDGI
PFIIRKCTSE IENRALSIKG IYRVNGAKSR VEKLCQAFEN GKDLVELSDL SPHDISNVLK
LYLRQLPEPL ILFRYYNDFI GLAKESQSII VEELEAQRVN PTTATPSQVS VELNRVLFKI
KDLLRQLPPA NYKTLQFLVE HLHRVTEQSE ENKMTASNLG IIFGPTLIKP RQADAEVSLS
SLVDYPYQAL IVELLIRHYQ MVFDTPLSPV SGTSPTEVDA QTRANTRLMQ QDKEQQLIRH
SKSLGDIKET LSFSSSVPEV AKSGERGLCR SHHITVTRVQ LRHPRNKLPS RPFSMPAERI
LNRSQIDENN SRNATDQDDR KGSGCDQSIE EVDETENTKT RAATHFRSTF IDTQTLRRTW
DKQYKHEVSS RTVKIGASSS TESAAVEGLS TSVPSTLSLG TTYTVAVRPN RTIKREDNVT
KYSPIATTFR APRTLQPPPG TFYKPPSGSK AKVLQNCAQA NSAEEEDEEE EEEEEGEIGI
EIEVSVDEPL EEDVEIEQTA ISQSPSCSPE EMDQNQAKPV YQRLRPRRLP EVEHREAHFV
//
