ID H2N6Q6_PONAB Unreviewed; 1261 AA.
AC H2N6Q6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 65.
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:ENSPPYP00000001321.3};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000001321.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000001321.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000001321.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; H2N6Q6; -.
DR Ensembl; ENSPPYT00000001366.3; ENSPPYP00000001321.3; ENSPPYG00000001141.3.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT00950000183110; -.
DR HOGENOM; CLU_006236_2_0_1; -.
DR InParanoid; H2N6Q6; -.
DR OMA; AWVEKRI; -.
DR OrthoDB; 5395569at2759; -.
DR TreeFam; TF351450; -.
DR Proteomes; UP000001595; Chromosome 1.
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:0051056; P:regulation of small GTPase mediated signal transduction; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20816; C1_GMIP-like; 1.
DR CDD; cd04409; RhoGAP_PARG1; 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 Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 192..462
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 612..657
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 671..886
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 481..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 297..324
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 361..413
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 541..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1261 AA; 142126 MW; 363451643C426E6A CRC64;
MIAHKQKKTK KKRAWASGQL STDVTTSEMG LKSLSSNSIF DPDYIKELVN DIRKFSHMLL
YLKEAIFSDC FREVIHIRLE ELLCVLKSIM NKHQNLNSVD LQNAAEMLTA KVKAVNFTEV
NEENKNDLFQ EVFSSIETLA FTFGNILTNF LMGDVGNDSL LRLPVSRETK SFENVSVESV
DSSSEKGNFS PLELDNVLLK NTDSIELALS YAKTWSKYTK NIVSWVEKKL NLELESTRNV
VKLAEATRTN IGIQEFMPLQ SLFTNALLND IESSHLLQQT IAALQANKFV QPLLGRKNEM
EKQRKEIKEL WKQEQNKMLE AENALKKAKL LCMQRQDEYE KAKSSMFRAE EEHLSSSGGL
AKNLNKQLEK KRRLEEEALQ KVEEANELYK VCVTNVEERR NDLENTKREI LTQLRTLVFQ
CDLTLKAVTV NLFHMQHLQA ASLADSLQSL CDSAKLYDPG QEYSEFVKAT NSTEEEKVDG
NVNKHLNSSQ PSGFGPANSL EDVVRLPDSS NKIEEDRCSN SADITGPSFI RSWTFGMFSD
SESTGGSSES RSLDSESISP GDFHRKLPRT PSSGTMSSAD DLDEREPPSP SETGPNSLGT
FKKTLMSKAA LTHKFRKLRS PTKCRDCEGI VVFQGVECEE CLLVCHRKCL ENLVIICGHQ
KLTGKIHLFG AEFTQVAKKE PDGIPFILKI CASEIENRAL CLQGIYRVCG NKIKTEKLCQ
ALENGMHLVD ISEFSSHDIC DVLKLYLRQL PEPFILFRLY KEFIDLAKEI QHVNEEQETK
KDSLEDKKWP NMCIEINRIL IKSKDLLRQL PASNFNSLHF LIVHLKRVVD HAEENKMNSK
NLGVIFGPSL IRPRPTTAPI TISSLAEYSN QARLVEFLIT YSQKIFDGSL QPQDVMCSIG
VVDQGGFPKP LLSPEERDIE RSMKSLFFSS KEDIHTSESE SKIFERATSF EESERKQNAL
EKCDACLSDK AQLLLDQEVE SASQKTEDGK TPKPLSLKSD RSTNNVERHT PRTKIRPVSL
PVDRLLLASP PNERNGRNMG NVNLDKFCKN PAFEGVNRKD TATTVCSKFN GFDQQTLQKI
QDKQYEQNSL TAKTTMIMPS ALQEKGVTTS LQISGDHSVN ATQPSKPYAE PVRSVREACE
RRSSDSYPLA PVRAPRTLQP QHWTTFYKPH APTISIRGNE EKPASPSAAV PPGTAHDPQS
LMVKSMPDPD KASACPGQAT GQPKEDSEEL GLPDVNPTCQ RPRLKRMQQF EDLEDEIPQF
V
//
