ID A0A2U9CF19_SCOMX Unreviewed; 1387 AA.
AC A0A2U9CF19;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative breakpoint cluster region protein-like {ECO:0000313|EMBL:AWP15097.1};
GN ORFNames=SMAX5B_015178 {ECO:0000313|EMBL:AWP15097.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP15097.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP15097.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendritic spine
CC {ECO:0000256|ARBA:ARBA00004552}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
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DR EMBL; CP026258; AWP15097.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000031438; -.
DR OrthoDB; 2916231at2759; -.
DR Proteomes; UP000246464; Chromosome 16.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd08686; C2_ABR; 1.
DR CDD; cd04387; RhoGAP_Bcr; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 4.10.280.30; Bcr-Abl oncoprotein oligomerisation domain; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR037769; Abr/Bcr.
DR InterPro; IPR015123; Bcr-Abl_oncoprot_oligo.
DR InterPro; IPR036481; Bcr-Abl_oncoprot_oligo_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23182:SF3; BREAKPOINT CLUSTER REGION PROTEIN; 1.
DR PANTHER; PTHR23182; BREAKPOINT CLUSTER REGION PROTEIN BCR; 1.
DR Pfam; PF09036; Bcr-Abl_Oligo; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF19057; PH_19; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF69036; Bcr-Abl oncoprotein oligomerization domain; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 615..808
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1009..1136
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1170..1364
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 80..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..55
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 165..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1387 AA; 154808 MW; 0FD4F1AE98B802A2 CRC64;
MVEPVGFIEA WKAQFPESEP PKMELRSVGG IEHELERCKA TIRRLEQEVN KERFRMIYLQ
TLLAKERKSY DKQRWGFRRT PLNEGVDPAA PQGAESQSQQ PHMQETGVVG VVVGGGGYGA
VCGGAAVDRS RFQPLGDGAS RTKPRPPPAR KSASHGDGLE SAFEVPQQVE STSCDSLDGL
SPSKQRGGVS VSPRRPTLPP PDKELPSDPK DKLGMGLGVA ALRSNFERIK RANSHSGVDV
AKGQEKQLPP PPPPFYTNME FHHERGLVRV NDREVSDKIS TLGSQAMQME RKRSLHSLPG
NLATVAGELR ARPVYRGRST ESTCGYDAEY EDGEPNQRHS GRANGGKPPP PPWQPSDFQA
YSSVYVGGVM MGEGGGGDGR AGGGGGSGVT MREHGGADDH LLTWPRRSYS PGSFEDVGGG
GGYTPDCSSN ENLTSSEEDF SSGQSSHVSP SPTTAFRRPF REKSRSPSQN SQNSQHSLDS
SSPPTPQSQK RHHRQQGGHV VMSEATIVSV RKTGQIWPPA AHHDLLPHGR TSHDNSFHGD
HLDGHFTGTP PTYGYDADRA EEQRRHHDIL PYIDDSPSSS PHLSSKSRSS RDTLSSGSLE
SSKSTECDLE KGLEMRKWVL SGILATEETY LSHLEALLLP MKPLKAAATT SQPVLTVAQI
ETIFFKVPEL YEIHKEFYDG LLPRVQQWSH HQRVGDLFQK LASQLGVYRA FVDNYELAVE
TAEKCCQANT QFAEISENLK VRSPKDSKDQ TAKNSLEALL YKPVDRVTRS TLVLHDLLKH
TPTGHLDHPL LQDALRISQN FLSSINEETT PRRQSMTVKK GENRQLLRDS FMVELVEGAR
KLRHVFLFTD LLLCAKLKKQ IGGKNQQYDS KWYIPLTELT FQGPEETEPL TIPQVPDEEL
DAMKVKISHL RSEIQREKRA NKGSKVIDRL RKKLSEQESL LLLTSPSMPL RVYNKNGKGY
GFLLSSDYER AEWREIIKEQ QKKCVKTSSL TSMELQMLTN SCVKLQTVHH IPLSINKEED
ESPGLCGFLN VIVHSASGLK QSLNLYCTME VDSFGFFSSK AKTRVYRYTT EPKWNEEFEI
ELEGSQTLRL LCYEKCYNKT KQNKEDGEGA DRIMGKGQIP LDPQTLQGKD WQRTVIPMNG
IEVKLSVKFT SREFSLKRMP SRKPMGVFGI KISTVTKRER SKVPYIVRQC LEEIERRGME
EVGIYRVSGV ATDIQALKTA FDTNNKDVSV MMSEMDVNAI AGTLKLYFRE LPEPLFTDDL
YPNFAGGITL SDSVAKESCM LNLLLSLPEP NLVTFLFLLD HLKRVAEKEC INKMSLHNLA
TVFGPTLLRP SEKDSKIPTN PTQPISMGDS WSLEVMAQVQ VLLYFLQLET IPTPDSKRQS
ILFSTEV
//
