ID A0A1V4JYT0_PATFA Unreviewed; 1183 AA.
AC A0A1V4JYT0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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|EMBL:OPJ77304.1};
GN ORFNames=AV530_007657 {ECO:0000313|EMBL:OPJ77304.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ77304.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ77304.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ77304.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ77304.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ77304.1}.
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DR EMBL; LSYS01005497; OPJ77304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JYT0; -.
DR STRING; 372326.A0A1V4JYT0; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20816; C1_GMIP-like; 1.
DR CDD; cd04409; RhoGAP_PARG1; 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; IPR001060; FCH_dom.
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; SM00055; FCH; 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:UP000190648};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 218..488
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 675..720
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 734..949
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 555..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 330..425
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 582..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1183 AA; 131336 MW; 234411F8E040612B CRC64;
MLRQNGGSNK RGLGLARLST SNFFTISNSG NWGMGRSTKS SSLSSISSNS DCYDNPVVDP
EYIMQLVNDV RKFADVLLYL KEAILSEENQ DGLHQVVHER LGELLRVLKA VINKHQALNS
VDILSAAGTV IAKVKAVNFK EVNEENKREL FSEIFSSIET LAFTFGNSVS DFLMGDVDNG
SSLGLPVSRR SRSFENLSVE SGGSRHERDD IQGHLRAEEV DNMLLRNDNG IESALSYAKA
WSKYTKDVVA WVEKKLSLEV ECAKNLAKMA ETAKSVVGHQ DYMPFQSIFI NAFQNDIENN
QLWQQTAAAL LSNKFVQPLL GRKNELDRQR KDIKELWQRE QKKMQELEAA LRKAKLLYTQ
RQDEYEKAKT CAARAEEEHL GSSGSFVKDF SKQLEKKRRL EEEALQKAEE ANEHYKASMA
EVEEKRNYLE SFKSDVLTQL RELIHQCDLT LKAATVNLFQ LQHAQVVSLP VNCQSLCESA
KLYDPGQQYS EFVRSLPKEG VTIESGSFET QNSQVDGVFN KQSTDSVHTS HGNLSQCSGD
FLAQTLDDVG SPIYHRSQKI GEKRSSSSTD IQAMRGPPPF RSWSVGNQSG GMCSDSESAG
GSSESRSMDS PSASPGDFKR RLPRTPSTGT MSSADDLDER EPPSPSDCGL NDLTSETANS
PGPFRDANMS KAAQTHKLRK LRALSKCREC DSLVVFQGAE CEECSLACHK KCLETLAIQC
GHKKLHGRLH LFGVEFAQAA KNVPDGIPFI IKKCTSEIES RALNVKGIYR VNGAKSRVEK
LCQAFENGKD LVELSELYAH DISNVLKLYL RQLPEPLILF RLYNEFIGLA KESQNVNEEL
DAKQASPKSK KRQSICIELN RIIIKIKDLL KQLPVPNYNT LQYLIGHLHR VTEQSNENKM
SASNLGIIFG PTLIRPRQTD ATVSLSSLVD YPYQARVVEL LITFYEKIFD VSLKPLLNTS
QSEETVFTVR VALSAEERES QQPRKSFAVK EGILIAPSEN RAADGAALFL ESNNTKNTKE
QVETSVTECV SLPLTGTKPE GSGKSNSLTE SSATSILDFN TSAPKETGDA ASPASERDND
SFISLGEDSH KTNFLPAKPN RQITKVPLRV PRTKPATRPV SLPVDRILPP CVLNERNSRN
AGGISPEKLG RSPTIEEVSE QGCTYRALLF QSGNHPRVVS CMD
//
