ID A0A2K5BXN3_AOTNA Unreviewed; 1201 AA.
AC A0A2K5BXN3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 34.
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:ENSANAP00000001184.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000001184.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000001184.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_012300300.1; XM_012444877.1.
DR AlphaFoldDB; A0A2K5BXN3; -.
DR Ensembl; ENSANAT00000010877.1; ENSANAP00000001184.1; ENSANAG00000009119.1.
DR GeneID; 105711946; -.
DR CTD; 9411; -.
DR GeneTree; ENSGT00950000183110; -.
DR OMA; AWVEKRI; -.
DR OrthoDB; 5395569at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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:UP000233020};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 128..398
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 548..593
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 607..822
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 416..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 233..260
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 297..349
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 419..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 135304 MW; EA02A54766BB2CC7 CRC64;
MERRDSFKEV IHIRLEELLR VLKSIMNKHQ NLNSVDLQNA AEMLTAKVKA VNFTEVNEEN
KNDLFQEVFS SIETLAFTFG NILTNFLMGD VGSDSLLRLP VSREMKSFEN VSVESVDSSS
EKGNFSPLEL DSVLLKNTDS IDLALSYAKT WSKYTKNIVS WVEKKLNLEL ESTRNMVKLA
EATRTNIGIQ EFMPLQSLFT NALLNDIESS HLLQQTIAAL QANKFVQPLL GRKNEMEKQR
KEIKELWKQE QNKMLEAENA LKKAKLLCMQ RQDEYEKAKS SMFRAEEEHL SSSGGLAKNL
NKQLEKKRRL EEEALQKVEE ANELYKVCVT NVEERRNDLE NTKREILTQL RTLVFQCDLT
LKAVTVNLFH MQHLQAASLA NSLQSLCDSA KLYDPGQEYS EFVKATNSTE EEKVDGNVNK
HLNSSQTSGF GPANSLEDVI RLPDSSNKIE EDRCSNSADI TGPPFIRSWT FGMFSDSEST
GGSSESRSLD SESISPGDFH RKLPRTPSSG TMSSADDLDE REPPSPSEAG PNSLGTFKKT
LMSKAALTHK FRKLRSPTKC RDCEGIVVFQ GVECEECLLV CHRKCLENLV IICGHQKLPG
KIHLFGAEFT QVAKKEPDGI PFILKICASE IENRALCLQG IYRVCGNKIK TEKLCQALEN
GMHLVDISEF SSHDICDVLK LYLRQLPEPF ILFRLYKEFI DLAKEIQHVN EEQETKKDNP
EDKKWPDMYI EINRILLKSK DLLRQLPASN FNSLHYLIVH LKRVVDHAEE NKMNSKNLGV
IFGPSLIRPR PTTAPITISS LAEYSNQARL VEFLITYSQK IFDGSLQPQD VMCSTGVVSP
QVDQGCFPKP LLSPEERDTE RSMKSPFFSS KEDIHTAENE SKIFERATSF EESERKQNAL
EKCDACLSDK AQLLLDQEVE LASQKTEDGK SPKPLSLKSD RSTNNLERRT PRTKIRPVSL
PVDRLLLASP PNGRNGRNMG NVNLDKFYKN PAFEGVNRKD TATTVCSKFN GFDQQTLQKI
QDKQYEQNSV TVKTTVIVPS ALQEKGVTTP LQISGDHSVS ATQPSKPYIE PVRSVREVSE
RRSSDSCPLA PVRAPRTLQP QHWTTFYKPH APAISVRGNE EKPASPSTAV PPGTAHNPQG
LMVKSMPDPH KASACPGQGT GQPKENSEDV GLLDVNPACQ RPRLKRMQQF EDLEDEIPQF
V
//
