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Database: UniProt
Entry: A0A6P5AG89_BRABE
LinkDB: A0A6P5AG89_BRABE
Original site: A0A6P5AG89_BRABE 
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.
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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
//
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