ID A0A452HF47_9SAUR Unreviewed; 1557 AA.
AC A0A452HF47;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000013451.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000013451.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000013451.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the GAPVD1 family.
CC {ECO:0000256|ARBA:ARBA00008489}.
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DR STRING; 38772.ENSGAGP00000013451; -.
DR Ensembl; ENSGAGT00000015391.1; ENSGAGP00000013451.1; ENSGAGG00000010278.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd05129; RasGAP_RAP6; 1.
DR Gene3D; 1.10.246.120; -; 1.
DR Gene3D; 1.20.1050.80; VPS9 domain; 1.
DR InterPro; IPR041545; DUF5601.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR045046; Vps9-like.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR23101:SF25; GTPASE-ACTIVATING PROTEIN AND VPS9 DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR23101; RAB GDP/GTP EXCHANGE FACTOR; 1.
DR Pfam; PF18151; DUF5601; 1.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF109993; VPS9 domain; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 3: Inferred from homology;
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT DOMAIN 213..422
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT DOMAIN 1417..1557
FT /note="VPS9"
FT /evidence="ECO:0000259|PROSITE:PS51205"
FT REGION 516..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1557 AA; 173344 MW; 771E3E0C4C727A78 CRC64;
MPAHLSPPGT TSPRRPGAQA ACAVTGLFVL AEGERRKQPR GLGGAAAAGD GERRRHMHSE
YSVVLSPSKM VKLDIHTLAH HLKQERLYVN SEKQLIQRLN TDVLKTAEKL YHTAWISKQQ
RINLDRLIIT SAEASPAECC QHAKVLEDTQ FVDGYKQLGF QETAYGEFLN RLRENPRLIA
SSLVAGEKLN QDNTQSVIYT VFTSIYGNCI MQEDESYLLQ VLRYLIEFEL KESDNPRRLL
RRGTCAFSIL FKLFSEGLFS AKLFLTATLH EPIMQLLVED EDHLETDASK LIERFSSAQQ
EKLFGEKGTE RFKQKVQEMV DSNEAKLVAL VNKFIGYLKQ NTYCFPHSLR WILSQMYKTL
SCVDRLEVGE VRAMCTDLLL ACFICPAVVN PEQYGIISDA PINEVARFNL MQVGRLLQQL
AMTGSEEGDP HMKSNLGKFD KSCVAAFLDV VISGRAVETP PMSSVNLLEG LSRTVVYMTY
SQLINLVGFM RNVMSSDQLK EDRMALENLL ANLPQNRHGK SSSLEMTPYN TPQLSPATTP
ANKKNRLPIG QQLAAITAWD TSTTNLSAHI NLVTPFATRS RNRSNIPMDQ HGDHEGSSQE
SIQEVQPEEV LVISLGTGPQ LTPGMMSENE VLNMQLADGG QGDVPVDETK LHGKPDKTLR
FSLCSDNLEG ISEGPSNRSN SVSSLDLEGE SVSELGAGPS GSNGVEALQL LEHEQATTQD
NLDDKLRKFE IRDMMGLTDD RDISETVSET WSTDVLGSDF DPNIDEDRMQ EIAGTAAENM
LGSLLCLPGS GSVLLDPCTG STISETTSEA WSVEVLPSDS EAPDLKQEER LQELESCSGL
GSTSDDTDVR EVSSRPSTPG LSVVSGISAT SEDIPNKIED LRSECSSDFG GKDSVTSPDM
DETAHGASQL TSPPSQSDSL LALFDPLSSH EGVSAVVRPK VHYARPAHPP PDPPILEGAM
GGNEARFPNF GSHILIPTDL EAFKQRHSYP ERLVRSRSSD IVSSVRRPMS DPGWNRRPGN
EERELPTQTS NIGAAASGPA PQSSSSSPSK DSSRGENEER KDSDDEKSDR NKPWWRKRFV
SAMPKAPIPF RKKEKQEKDK DDFVSERFST LQDDPNPRLS AQAQAAEDIL DKYRNAIKRT
SPSEGAIVNF ESAEVIGDGE SIHDSPRDEA LQNMSADDLP DSASQVAQPQ DSAFSYRDAK
KKLRLALCSA DSIAFPMLTH STRNGLPDHT DPDDNEIVCF LKVQLAEAIN LQDKNLMAQL
QETMRCVSRF DNRTCRKLLA SIAEDYRKRA PYIAYLTRCR QGLQTTQAHL ERLLQRVLRD
KEVANRYFTT VCVRLLLESK EKKIREFIQD FQKLTAADDK TAQVEDFLQF LYGAMAQDVI
WQNASEEQLQ DAQLAIERSV MNRIFKLSFY PNQDGDILRD QVLHEHIQRL SKVVTANHRA
LQIPEVYLRE APWPSAQSEI RTISAYKTPR DKVQCILRMC STIMNLLSLA NEDSVPGADD
FVPVLVFVLI KANPPCLLST VQYISSFYAN CLTGEESYWW MQFTAAVEFI KTIDDRK
//
