ID W5NK29_LEPOC Unreviewed; 1032 AA.
AC W5NK29;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=SLIT-ROBO Rho GTPase activating protein 1 {ECO:0000313|Ensembl:ENSLOCP00000020988.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000020988.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000020988.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01034298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01034299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01034300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000021024.1; ENSLOCP00000020988.1; ENSLOCG00000016975.1.
DR GeneTree; ENSGT00950000182824; -.
DR HOGENOM; CLU_005715_0_0_1; -.
DR Proteomes; UP000018468; Linkage group LG8.
DR Bgee; ENSLOCG00000016975; Expressed in muscle tissue and 11 other cell types or tissues.
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:UP000018468};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 19..314
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 481..671
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 720..779
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 696..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..34
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 819..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 118251 MW; 05791320EF698139 CRC64;
MSNPARFKKD KEIIAEYETQ VKEIRAQLVE QQKCLEQQTE MRVQLLQDLQ DFFRKKAEIE
MEYSRNLEKL AERFMAKTRS TKDHQQYKKD QNLLSPVNCW YLLLNQVRRE SKDHATLSDI
YLNNVIMRFM QISEDSTRLF KKSKEITFQL QEDLMKVLNE LYTVMKTYHM YHTESISAEC
KLKEAEKQEG KQIGRSGDPV FSIRMEEKHQ RRSSVKKIEK MKEKRQAKYS ENKLKSIKAR
NEYLLTLEAT NSSVFKYYIH DLSDLIDCCD LGYHASLNRA LRTYLSAEYN LETSRHEGLD
IIENAVDSLD PRSDRQRFME MYPTAFCPPV KFEFQSHMGD EVCQITAQPP VQAELMLRFQ
QLQSRLTTLK IENEEIKKTT EATLQTIQDM VTIEDYDVSE CFQHSRSTES VKSTVSETYL
SKPSIAKRRA NQQETEQFYF MKFREFLEGS NLITKLQAKH DLLKRTLGEG HRAEYMTTSR
GRRNSHTRHQ DSGQVIPRVV ESCIRFINLY GLQHQGIFRV SGSQVEVNDI KNSFERGNDP
LTDEENNHDI NSVAGVLKLY FRGLENPLFP KERFNDLISC IRIENLYERA LYIRKILLTV
PRSVLIVMRY LFAFLNHLSQ YSDENMMDPY NLAICFGPTL MPVPDIQDQV SCQAHVNEII
KTIIIHHETI FPDAKELDGP VYEKCMAGDD YCDSPYSEHG TLEEVDQDGE TEPRTSDDEC
EPIEAIAKFD YIGRSARELS FKKGASLLLY QRASDDWWEG RHNGIDGLVP HQYIVVQDMD
DTFSDSLSLK TDSEASSGPV AEDKCSSKDI SSPTERLPES FVSRHRKRTE ALPSRRPLVR
PLDGHCAVHP SQGHVNAALE MSPASAVSHY SPRALLQSRN LAVDSPERRR RAGHGSLTNI
SRHDSLKKME SPPIRRSTSS GQYSGFTEPH KALDPETIAQ DIEETMNMAL NELRELERQS
SAQHAPDVVL DTLEQMKNAP APAGGCGEGL GPLHGGVPLR XLRPKPSVLP KTSPGQAPPP
PAQGSVDKSC TM
//
