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Database: UniProt
Entry: A0A3B4H379_9CICH
LinkDB: A0A3B4H379_9CICH
Original site: A0A3B4H379_9CICH 
ID   A0A3B4H379_9CICH        Unreviewed;      1067 AA.
AC   A0A3B4H379;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=SLIT-ROBO Rho GTPase activating protein 1 {ECO:0000313|Ensembl:ENSPNYP00000028028.1};
GN   Name=SRGAP1 {ECO:0000313|Ensembl:ENSPNYP00000028028.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000028028.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000028028.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3B4H379; -.
DR   STRING; 303518.ENSPNYP00000028028; -.
DR   Ensembl; ENSPNYT00000028714.1; ENSPNYP00000028028.1; ENSPNYG00000021071.1.
DR   GeneTree; ENSGT00950000182824; -.
DR   Proteomes; UP000261460; Unplaced.
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};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          21..312
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          471..665
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          714..773
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          781..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          877..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          966..1067
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..804
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..830
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..852
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        907..922
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..1019
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1048..1067
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1067 AA;  121742 MW;  7A236F3940C6B6D3 CRC64;
     FSSITRSQKA KTSVYEYQPH ICIRAQLVEQ QKCLDQQTEM RVQLLQDLQD FFRKKAEIEM
     EYSRNLEKLA ERFMAKTRST KDHQQYKKDQ NLLSPVNCWY LLLNQVRRES KDHATLSDIY
     LNNVIMRFMQ ISEDSTRLLK KSKEIAFQLQ EDLMKVLNEL YTVMKTYHMY HSESISAESK
     LKEAEKQEEK QIGRADPVFS IRMEEKYQRR SSVKKIEKMK EKRQAKYSEN KLKSIKARNE
     YLLTLEATNS SVYKYYIHDL SDLIDCCDLG YHASLNRALR TYLSAEYNLE TSRHEGLDII
     ENAVDSLDPR SDRQRFMEMY PTAFCPPAKF EFQPHMGDEV CQISVQPPVN GELILRFQQL
     QSRIATLKIE NEEIKKTSEA TLTTIQDMVT IEDYDVSECF HHSRSTESVK STVSETYLSK
     PSIAKRRANQ QETEQFYFMK FREFLEGSNL ISKLQAKHDL LKRALGEGTF RTLRGRRNSH
     TRHQDSGQAI PRVVESCIRY INLYGLQHQG IFRVPGSQLE VNDIKNSFER GNDPLADDEN
     NHDINSVAGV LKLYFRGLEN PLFPKERFNE LLSCIRIENL YERALYIRKI LLTIPRSVLI
     VMRYLFAFLN HLSQYSDENM MDPYNLAICF GPTLMPTPDS QDQVSCQAHV NEIIKTIIIH
     HETIFPDVKE LDGPIYEKCM AGGDYCESPY SEHGALEEVD NEGGTETHTS EDEGEPIEAI
     AKFDYVGRSS RELSFKKGAS LLLYQRASED WWEGRHNGID GLVPHQYIVV QDIDDNFSDT
     LSQKADSEAS SGHAGEDKCS GKDIGSPNDT RISEAFITRK RSDPPSRRPP ARPSDVHCMV
     HTSQQSHSGH GGTPEMGSPV LGHFSPRDML RSRNHVAIDS PERRRRAGHS SLTNISRHES
     LKKMESPPIR RSTSSGQYTG FTDPLDPETI AQDIEETMNT ALNELRELER QSSAKHAPDV
     VLDTLEQRQT SGSSGGGPTP ASSSESLSPI HAVMLRSTAN TEPPTRRSTS SSNDSVSTFK
     PVVAPRMGVQ LKPPALRPKP MVLPKSNQAP QPPANSSQDP LDKSCTM
//
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