ID A0A1S3JSB5_LINUN Unreviewed; 1154 AA.
AC A0A1S3JSB5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=SLIT-ROBO Rho GTPase-activating protein 1 isoform X4 {ECO:0000313|RefSeq:XP_013412996.1};
GN Name=LOC106175501 {ECO:0000313|RefSeq:XP_013412996.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013412996.1};
RN [1] {ECO:0000313|RefSeq:XP_013412996.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013412996.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_013412996.1; XM_013557542.2.
DR AlphaFoldDB; A0A1S3JSB5; -.
DR EnsemblMetazoa; XM_013557542.2; XP_013412996.1; LOC106175501.
DR GeneID; 106175501; -.
DR OrthoDB; 2904755at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07656; F-BAR_srGAP; 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 PANTHER; PTHR14166:SF17; RHO-GAP DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14166; SLIT-ROBO RHO GTPASE ACTIVATING PROTEIN; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR01887; SPECTRNALPHA.
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|PROSITE-ProRule:PRU01077};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 35..315
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 498..686
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 740..799
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 201..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 129535 MW; 3146CF1EA474A297 CRC64;
MEGGSIEISR PKGLARNTSL RVSKRTRTQK QDLATHIRQQ LNEQLKCLDL RLENQMAMVA
EIQDFFKKRA EVEQEYSRNL DRLVKQVMVR HKADKQRRES WHLYSTYTCW QHLLAMTKKQ
SKDHGTVGDI YGNIMVQRLS EVMEDAQRMY KAYRDIGVDS HEEILSMLNK LQTAMKTYHI
YYNESKQAEN KLKTAESQKV KVEQHAGKSG LPSRKYRSIE KQAEKRQNKY QENKLKALKS
RNEYLLTIDA ANAALHKYSV DDLSDLLDGM DYGYHAAMAR LMMTTLSVEE NVKNSHKFAI
DLLNKGITDV GDARLDKKKF LESNSTIFAL PKKFEFQAHK GDEVIQVSAQ KSVQDELVQR
YDQLSKRLEE LKLENDEVWK SLEAADKTLM EMITSQEYDV TPYFQDPQKV PPKSPSEVAK
LKSNRSDIEV YYLEKFKEYV LGSNKVARLQ AQHTSIQKAL GEGVKIGQTT RPPSLPPKPR
KRRIGKAPTV GQPKLFGGSI EEYAEVTGVD VPLIIRSCVR IINLYGMHNQ GVFRVSGSQL
EINEFKAAFE KGEDPLIEMT DNISINSVAG VLKLYFRELR EPIFPTQMFD ALIDCTRIDN
VKDSITRLRE LITQLPRPVF VVLRYLFSFL NHLSEFSDEN MMDPYNLAIC FGPTLLPVPG
DKDPVTYQSY VNDLIKLILS HQEEIFPNDD GGTVYERMMM EEGSHRCSQY LGDRELAELS
DEEDEVDDDV VSEDDHLLEP EVTEAVALYD FEGRTGRELS FKKGDQLLLY SQVSSDWWDG
YFNGKEGLIP DKYIKIAQTP RDFELTRQVS QNDKRRSTES LPAKTYSASG PKVDEPLTVG
PLDKSVSQPN ISVDRTDRRQ HHHSRQDSSD QSLGSITSKS TDSVSLSELS LTSGDSKDNS
TDDLERDLDH ALSEVMTQVE SLGKQEEGLE GGRRDSGGRG DVMPLGKNSE RTRSESGTSS
SFGPQANRKF TIPPNPKHTP DLVLDLPPDA KDTESPSPPQ DQSDPDSPTS GAETFAKSNQ
CTLKKGMSNS MPRSLTHTST FRAGMDVVGE QGDVREGGVV KRSVSTSATI SARTGRSLPP
AYRESPERSV PSPTPSMEKA SSPGPAVAPK PSIKARPPVM KKPPKPGYLK LRGESPSSPA
DGSSSSPTGG PTAL
//
