ID A0A6P5AG89_BRABE Unreviewed; 1633 AA.
AC A0A6P5AG89;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 10-JUN-2026, entry version 24.
DE SubName: Full=Uncharacterized protein LOC109486100 isoform X2 {ECO:0000313|RefSeq:XP_019645344.1};
GN Name=LOC109486100 {ECO:0000313|RefSeq:XP_019645344.1};
OS Branchiostoma belcheri (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7741 {ECO:0000313|Proteomes:UP000515135, ECO:0000313|RefSeq:XP_019645344.1};
RN [1] {ECO:0000313|RefSeq:XP_019645344.1}
RP IDENTIFICATION.
RC TISSUE=Gonad {ECO:0000313|RefSeq:XP_019645344.1};
RG RefSeq;
RL Submitted (JAN-2026) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_019645344.1; XM_019789785.1.
DR GeneID; 109486100; -.
DR OrthoDB; 120383at2759; -.
DR Proteomes; UP000515135; Unplaced.
DR GO; GO:0097060; C:synaptic membrane; IEA:TreeGrafter.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; IEA:TreeGrafter.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00030; C2; 1.
DR CDD; cd06718; PDZ_Par6-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR052118; Rho-GAP_regulator.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR057459; SYDE1/2_C2.
DR PANTHER; PTHR46150; RHO GTPASE-ACTIVATING PROTEIN 100F; 1.
DR PANTHER; PTHR46150:SF3; RHO GTPASE-ACTIVATING PROTEIN 100F; 1.
DR Pfam; PF25336; C2_SYDE; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468, ECO:0000256|PROSITE-
KW ProRule:PRU00172}; Reference proteome {ECO:0000313|Proteomes:UP000515135}.
FT DOMAIN 49..120
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 703..822
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 857..1050
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 146..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1549..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..332
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..552
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1633 AA; 182139 MW; 0D261EA4C8F10089 CRC64;
MQEPRGSPGK RRPEVLPENM FIRVLHGSLR RVAGAEERPI ADGTALVRTV ELTRAPGEML
GFYIRQGNGL DRDHGIFVSR IMAGSLVDRY GLLRIGDEIL TVNSVDVSYM KLAEVVAIMQ
IPTRLVMNVT TQKYATLPVK GGIQKGDQLA VENKNPTRTP NKPRRSASQR ISRSPKTPGR
QKAKRLERSS SLEDKRRIPF QKDQISDDFS DFEKFLFNPP SLKEKPLPEI PKDCKRPTKT
PPAPPPSKDK EKIKEALCSG KRLTRLDLAV ARTKLDEAYH QAYDLLLNSL EKEEEERAKA
AKQSQRDSSA STDDGSKTPV AEEVEEQPEE EDGRGSPEGE ACVTEVPLTW TKLDRSLRSH
HLESLQHHSS RSSSDREEWG DDDIQGDSYV EHNPIYESDE DDYNTAPLWS EGQGHTPNGF
IKKNGPLMDG GTDEDDPRND PQDYSNESDR ADYETGTWKS DKTWQSDSSC APADMAESPL
LQRKGRVGKI GEVHARAVLS PPRSPSNITV KKKQEWYQRR AKISPELARR ISGENEEEQG
QEEENIGEPE EPDLSRSRSP KREGFWSALS QLSPTTVRKF GWKKPATNRS QSVEEENRAN
IGTDSDDSPK MTQRNHALLP EIALTPEQKL SSLQNKGKVV AKYHLDSTSN SDNGSTTRGG
GGVSSVFTRT RLYRSFNRDR SNNDRTMEKI PNGDLAGRGV DLGSYKKCKS DDGNKGGLCP
VSGILAIELY SLKGMKVFKK SSKDLYCVIE VDGAPRARTV VRDGEQEVVW NEKFALELND
AYQICFNFYN WDNIRRHKVN CAGTLNLSHL TRQANEKIAL KMDPRGTMYV TLTLDPNMED
GVHSLNPSPG LGRLFGMDLD RVVEEEGGGV HIPLIVKKCV SEVEDRGLSV VGIYRLCGSA
YRKKDLRDEF EIDSIRTDIS ADKYPDINVV TGVLKDFLRE LPEPLFSPAL SDIVCAKPSD
KEPEEMLQCL GPVQKLTLGY LLDHLKRVAA NCAVNKMDYN NLAVCFGPVL CSPPQGSDVD
GAQGALLAAI DFRKHIAALQ TLLELWPADR DPNADKDQGT PNDEGEDKDE PNNNDLPESD
STLLYSRLRG NTSSSEDSRP EADRTDSDTS QRSHEPSPRL GRDGSPCTGR LQVYDEVFEE
TAANVPTRYQ SYEEVEEFTA EGGKIEQSTL ERRMVERGKM VQRDRSFRGD RPARVRVKVE
DDYMDMEGGG LQEEKKSPRR SGGAKTEGKE RDENIANESK DSVVGERDIE NTAEELMAKP
RSRISRKHEK EYVNLAPYRA ALGVSSADDE GDSKVAASPK LKQQETPKSP AKAYIDYAQL
SKSRERLSDS SSSREQLTDS SERLTESPKP HNQREQASLR DRGGQASGSE KAYIDMSQLR
GHRKMYQQRS RTEEIHARYP GKESEEHTPT IQVSSTESIV RRRLRSFEGD SRGEQQGPAP
FPRAGAQAEG SADQRGCRQR GRARAATDSA LFIHEGDSDF EEDRLLARDF ARRLPLQTPV
PESLSVDEGI DVRALSPQDL SVDVDLSTKF HDIDRLVSET IKDTLLASTS PYKGGAKASR
SKDSLDSGAV LSPSMSRDVM AMGGSQPSPE SYGSRDEGWS DIDQWILERW NSIDHLMETW
TLSDNPSTDA SDC
//