ID A0A3Q1BZK9_AMPOC Unreviewed; 1710 AA.
AC A0A3Q1BZK9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Dynamin-binding protein {ECO:0000256|ARBA:ARBA00018186};
DE AltName: Full=Scaffold protein Tuba {ECO:0000256|ARBA:ARBA00032587};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000019785.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000019785.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Golgi apparatus, Golgi stack
CC {ECO:0000256|ARBA:ARBA00004348}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
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DR Ensembl; ENSAOCT00000014707.1; ENSAOCP00000019785.1; ENSAOCG00000003431.1.
DR GeneTree; ENSGT00950000183088; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07589; BAR_DNMBP; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11798; SH3_DNMBP_C1; 1.
DR CDD; cd12141; SH3_DNMBP_C2; 1.
DR CDD; cd11794; SH3_DNMBP_N1; 1.
DR CDD; cd11795; SH3_DNMBP_N2; 1.
DR CDD; cd11796; SH3_DNMBP_N3; 1.
DR CDD; cd11797; SH3_DNMBP_N4; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 6.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR035820; DNMBP_SH3_C1.
DR InterPro; IPR035817; DNMBP_SH3_N1.
DR InterPro; IPR035818; DNMBP_SH3_N2.
DR InterPro; IPR035819; DNMBP_SH3_N3.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR22834:SF19; DYNAMIN-BINDING PROTEIN; 1.
DR PANTHER; PTHR22834; NUCLEAR FUSION PROTEIN FUS2; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 4.
DR PRINTS; PR00499; P67PHOX.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 6.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50044; SH3-domain; 6.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50002; SH3; 6.
PE 4: Predicted;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 2..61
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 66..130
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 152..211
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 277..336
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 884..1061
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1102..1311
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 1383..1446
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1646..1709
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 258..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 750..828
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1225..1261
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 264..278
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..710
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1710 AA; 193755 MW; 8AB9161E2E2B76A4 CRC64;
MEAGSVVRAV FEFLPSVSEE LPLFPGDVIE VLSVVDEFWL LGNKDGVTGQ FPSTFVEEVT
IPSTKPGDRL YVCINDFSSA EPGNLSLKRG DVVVGEAGGS MDLGETWQRG CNAWGVRGLF
PTSCVKEMNL SGRSRQLSER SAQAQASELP SYALGQARAL MSLHAQLNEE LDFREGDLII
ITGLPEPGWF QGELEGRRGI FPEGFVELMG PLRSPQEPED CQDLNNDPQQ YIDEDAYDAG
EGTEEEVMEE GEVFMRDDEE RKDAAVEEEQ EEEEEEEGGI YGVALYEFRA LEPGELDFDV
GDRIRVVSTL EDGWLEGELR GRRGIFPHRF VKLEDDGQKT AEETDVVEPV GGEKENSCRE
YSSDHLCPNG SENEPEWTTY EDHTVWDLDY FERTEEQRWQ RENKSSGAQT NNRGQRDGGN
RPDSRPRRPL APAHRGPERP KSSPPARPRL PPRPSLPARS HRQHAGTNSS RNQSNYTNGN
TRPLKSKLTH SLTLPSTHSG WSKDSRYYQR SSADGSFTNN RAASLSQALV NLVEGHKQKK
LTRHASVSDA DMMQHTADAR PRSQQTARGS NGILPSSITL EALTTSAGDL EAKLSQQLFE
FEKSLTTSYS DTNVGSGASR DVSPVADLNQ QSIISRHFSI LDYSDESDII RGSSHSPVSN
LMQSNSFSLE RRRTLRPPPP RPRVLRPAAP APYKPARPAP RPPPRCPRQN TTPPTGNSLT
SSPIFYSPDE PAANLLDQTS GGQAEFGDLA AAQEHEIQSQ LEAEQELERE MELESQRQRE
EEERYQLLLR LQEVEHDMEA YAHTAEELRA MLEEEEEETA RMQALENLEF CNYTLETLAL
EQQQLQEMTL LSSQPKPLDS LPALDTSPAA GTGTEDPELR MLEKRSKVIE ELLQTERDYI
KDLQMCVEEI IEPLQRKQVK NVDFEGLFGN ISSVIDLSQR LFDTLKETDS TGKVFLDFKG
ELEEVYKIYC QNHDDAISLL ETYEKDENIQ RHVLECLERL RGKTNYINLG SFLIKPVQRV
MRYPLLLMEL LGATPDSHHD RQQLTQAVQA VKEINVNINE YKRRKDLVVK YRKGDEDTFI
DKISKLSMHS IIKKSNRVSS HLKHLTGISP QIKDEAFDEA EKKFRLQERL IKSFIRDISL
YLQHIRESAS VKVLAAISFC DIYTERSLLD PERFQRAHRC ISDKQFTQFK ARTEDLVINP
LTQLLLMFAG PHKLIQKRFD KLLDYDNCKE RADRLKDRRV QDELQVARNN YEALNAQLLD
ELPKFHGAAE ELFTGCVRAF AQAQKDFMKT TLGELKPLLQ VFSNRVGTEG NLIAQFQEEY
SRVLQLLQSF SFCPENLPPA TVTKKPFEKK TLEKQASKKQ LQGPPNYIMQ TDEHRAGLLV
RYGPEKLFQA ERNFNAAQDL DVSILEGDLV GVIKQQDPMG SHNRWLIDNG VTKGFVYSSF
LKPYNPRRSH SDVSIESQSS NESGYGGSSP VFSRQNSNST LTFNQETATV SFSTSQPQSQ
SSPHPSLDSA SSRRSHLRDA PNLESASQTN SMNSSPHNPS NRRDFTEQTH RNTPSHRDTE
PSYRHSGNHR DSYDTGYGHK ETSDLSETDS CSSQRNNRAQ RYGHTEKSCS SYQWRNGDSS
SQKKCTYSRE EYIEPEPEPE LESELDGHQI YYALYSFNAR CANELSISAN QQLRILEFQD
MNGNSEWWLG EAGGRRGYVP SNYIRKSEYT
//
