ID M4AXG9_XIPMA Unreviewed; 1042 AA.
AC M4AXG9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=SLIT-ROBO Rho GTPase activating protein 1 {ECO:0000313|Ensembl:ENSXMAP00000019164.2};
GN Name=SRGAP1 {ECO:0000313|Ensembl:ENSXMAP00000019164.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000019164.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000019164.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000019164.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; M4AXG9; -.
DR Ensembl; ENSXMAT00000019192.2; ENSXMAP00000019164.2; ENSXMAG00000019097.2.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000182824; -.
DR HOGENOM; CLU_005715_0_0_1; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd04383; RhoGAP_srGAP; 1.
DR CDD; cd11955; SH3_srGAP1-3; 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 Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035648; srGAP1/2/3_SH3.
DR PANTHER; PTHR14166; SLIT-ROBO RHO GTPASE ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR14166:SF15; SLIT-ROBO RHO GTPASE-ACTIVATING PROTEIN 1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..285
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 441..633
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 682..741
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 747..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1042 AA; 118692 MW; CC34BB17A53CBB81 CRC64;
MFSEIRTQLV EQQKCLDQQT EMRVQLLQDL QDFFRKKAEI EMEYSRNLEK LAERFMAKTR
STKDHQQYKK DQNLLSPVNC WYLLLNQVRR ESKDHATLSD IYLNNVIMRF MQISEDSTRL
LKKSKEIAFQ LQEDLMKVLN ELYTVMKTYH MYHSESINAE SKLKDAEKQE EKQIGRGDPV
FSIRMEKKIE KIKEKRQAKY SENKLKSIKA RNEYLLTLEA TNASVFKYYI HDLSDLIDCC
DLGYHASLNR ALRTYLSAEY NLETSRHEGL DIIENAVDSL DPRSDRQRFM EMYPTAFCPP
AKFEFQSHMG DEVCHITAQP PVNGELILRF QQLQSRLATL KIENEEVKKT SEATLTTIQD
MVTIEDYDVS ECFHHSRSTE SVKSTVSETF LSKPSIAKRR ANQQETEQFY FMKFREFLEG
SNLISKLQAK HDLLKRTLGD GTVKVLFFAL PCDSGQAIPR VVESCIRYIN LYGLQHQGIF
RVSGSQLEVN DIKNSFERGN DPLTDDEDNH DINSVAGVLK LYFRGLENPL FPKERFNDLL
SCIRTDNLYE RALYIRKILL TIPRSVLIVM RYLFAFLNHL SQYSDENMMD PYNLAICFGP
TLMPTPDTQD QVSCQAHVNE IIKTIIIHHE TIFPDGKELE GPIYEKCMAG GDYCESPYSE
HGALEEVDNE GGTETHTSED EGEPIEAIAK FDYVGRSSRE LSFKKGASLL LYQRASEDWW
EGRHNGIDGL VPHQYIVVQD IDDNFSDSLS QKADSEASSG HAGEDKCSGK DISSPTDTRI
SEAYIARHRK RSDPPTRRPP ARPSNVHCML HSSQQGHGVT PEMGSPVLGH FSPRDMLRSH
NHMPMDSPER RRRTGHSSLT NISRHESLKK MESPPIRRST SSGQYTGFTD SHHHHSGKPL
DPETIAQDIE ETMNTALNEL RELERQSSAK HAPDVVLDTL EQRQTAGSGG GGPTMASSNE
SLSPIHGVML RSTANTEPPI RRSTSSSSEA MSTFKPMVAP RMGVQLKPPA LRPKPMVMPK
SNQAPQPPAG SAQDPLDKSC TM
//
