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Database: UniProt
Entry: A0A2U3VDS2_ODORO
LinkDB: A0A2U3VDS2_ODORO
Original site: A0A2U3VDS2_ODORO 
ID   A0A2U3VDS2_ODORO        Unreviewed;      1075 AA.
AC   A0A2U3VDS2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=SLIT-ROBO Rho GTPase-activating protein 3 isoform X4 {ECO:0000313|RefSeq:XP_004392775.1};
GN   Name=SRGAP3 {ECO:0000313|RefSeq:XP_004392775.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004392775.1};
RN   [1] {ECO:0000313|RefSeq:XP_004392775.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_004392775.1; XM_004392718.1.
DR   AlphaFoldDB; A0A2U3VDS2; -.
DR   GeneID; 101379372; -.
DR   CTD; 9901; -.
DR   OrthoDB; 2904755at2759; -.
DR   Proteomes; UP000245340; Unplaced.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07684; F-BAR_srGAP3; 1.
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   InterPro; IPR049581; SrGAP3_F-BAR.
DR   PANTHER; PTHR14166; SLIT-ROBO RHO GTPASE ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR14166:SF8; SLIT-ROBO RHO GTPASE-ACTIVATING PROTEIN 3; 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|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245340};
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          482..670
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          205..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          785..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          837..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          902..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1023..1075
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          359..386
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        785..816
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1075
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1075 AA;  121792 MW;  07349E3540DA531C CRC64;
     MSSQTKFKKD KEIIAEYEAQ IKEIRTQLVE QFKCLEQQSE SRLQLLQDLQ EFFRRKAEIE
     LEYSRSLEKL AERFSSKIRS SREHQFKKDQ YLLSPVNCWY LVLHQTRRES RDHATLNDIF
     MNNVIVRLSQ ISEDVIRLFK KSKEIGLQMH EELLKVTNEL YTVMKTYHMY HAESISAESK
     LKEAEKQEEK QFNKSGDLSM NLLRHEDRPQ RRSSVKKIEK MKEKRQAKYS ENKLKCTKAR
     NDYLLNLAAT NAAISKYYIH DVSDLIDCCD LGFHASLART FRTYLSAEYN LETSRHEGLD
     VIENAVDNLD SRSDKHTVMD MCNQVFCPPL KFEFQPHMGD EVCQVSAQQP VQTELLMRYH
     QLQSRLATLK IENEEVRKTL DATMQTLQDM LTVEDFDVSD AFQHSRSTES VKSAASETYM
     SKINIAKRRA NQQETEMFYF TKFKEYVNGS NLITKLQAKH DLLKQTLGEG ERAECGTTRG
     RRNARTRNQD SGQAIPLVVE SCIRYINLYG LQQQGIFRVP GSQVEVNDIK NSFERGEDPL
     VDDQNERDIN SVAGVLKLYF RGLENPLFPK ERFQDLISTI KLENPAERVH QIQQILITLP
     RVVIVVMRYL FAFLNHLSQY SDENMMDPYN LAICFGPTLM HIPDGQDPVS CQAHVNEVIK
     TIIIHHEAIF PSPRELEGPV YEKCMAGGEE YCDSPHSEPG TIDEVDHDNG TEPHTSDEEV
     EQIEAIAKFD YVGRSPRELS FKKGASLLLY HRASEDWWEG RHNGVDGLIP HQYIVVQDMD
     DAFSDSLSQK ADSEASSGPL LDDKASSKND LQSPTEHISD YGFGGVMGRV RLRSDGAAIP
     RRRSGGDTHS PPRGLGPSID TPPRAAACPS SPHKIPLTRG RIESPEKRRM ATFGSAGSIN
     YPDKKALSEG HSMRSTCGST RHSSLGDHKS LEAEALAEDI EKTMSTALHE LRELERQNTV
     KQAPDVVLDT LEPLKNPPGP ISSEPASPLH TIVIRDPDAA MRRSSSSSTE MMTTFKPALS
     ARLAGAQLRP PPMRPVRPVV QHRSSSSSSS GVGSPAVTPT EKMFPNSSAD KSGTM
//
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