ID A0A2D0S7C2_ICTPU Unreviewed; 1428 AA.
AC A0A2D0S7C2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Dynamin-binding protein {ECO:0000256|ARBA:ARBA00018186};
DE AltName: Full=Scaffold protein Tuba {ECO:0000256|ARBA:ARBA00032587};
GN Name=dnmbp {ECO:0000313|RefSeq:XP_017338648.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017338648.1};
RN [1] {ECO:0000313|RefSeq:XP_017338648.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017338648.1};
RG RefSeq;
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 RefSeq; XP_017338648.1; XM_017483159.3.
DR GeneID; 108273721; -.
DR CTD; 23268; -.
DR OrthoDB; 25601at2759; -.
DR Proteomes; UP000221080; Chromosome 13.
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 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; 2.
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; 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; PF14604; SH3_9; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50002; SH3; 2.
PE 4: Predicted;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 598..781
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 822..1032
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 1100..1163
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1364..1427
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 242..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1164..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 946..982
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1164..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1278..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1428 AA; 169362 MW; 942D69E29F79FA42 CRC64;
MNGQIALGHP MVFAPVAWDF SRAPPRRGKS VEELMSDSWE RERYIQMHMH FQQQQQLQQP
QQPVICPQDF GPAPGYLEHQ AYLKQASGMH QTCWEYEDCD KIPYRDGFPQ QQNQFFYHTP
EAVFQEPRRP QEWTGNHCFY EPKEDVNLTD HRGNKDHVQS PQTKEFPNYI NRYRHNSWDV
DEYNDEREHY SRWDQNAYYD RDKRDYYDKK KGNYRERDRY DHRDSDYYDR KELDTYDRYN
QKDMDNYDHK DRMRRDYHDT RQRHKYAYRD TEHCGRREKE FSDHRDMDSY DRNQKDQYER
RVDRNYNRGG EQDHKEFNRY AYREKDRNDQ RDVDKYEQRK GDHSKYREKD IDDRRKVDYY
KHRENSDAEY KEKDHYALQG DAHPDLEYKD TYDSRKDSRY KLKEKVQYDR TEKGHYEHTE
QGLHEQRQKD SWRDRDYYQL RDADRHYYRD KGNRHHRSYD CYDNEVKLYC EDSEWEDDKY
EQKSRRYCKI STEGYSSDYD SWKHSKDTKN GVRIDPDSRR LDMEKQGWKK QKALYAGSLD
RNSFYRRTAP SSLRKSEFVI NRKEKQEMTL LSAQPKSLEP VPASAATTED PEQRMLEKRS
KVIAELLQTE RDYIKDLNMC KTEIILPLQR KQAQNVDFDG LFGNIDSVID LSTRLEEALQ
DTDSIGKVFL DFKSELEEVY KVYCQNHDDA IALLESYEKD ENIQKQVLEC LENLRTIYHG
WGKTNYINLG SFLIKPVQRV MRYPLLLMEL LNATPESHHD RKQLADAMSS IKEINVNINE
YKRRKDLVVK YRKGDEDRLI DKISKLSMHS IIKKSNRVSS HLKHLTGMAP QLKDEAFDEA
EKRFRLQERL IKSFIRDISL YLQHIRESAS VKVLSAISFC DIYTERQQQL GPERFQRAHR
CISDKQFTEF KERTEALVIS PLTQLLSMFA GPHKLIQKRF DKLLDYNNCK ERAERLKDKR
VQEELQAARN NYEALNAQLL DELPKFLRAA EELFTNCMQG FAQAQRDFMF LTLGELTPLL
QLSGIGGTEG NLVSLFQEEH SRVLQLLQSF SFFPENLPMP RKAYEKKTLE KQTPKKQLLS
PPNCIMQTDQ HRTGLLALYG PEKLFQAERN FNAAQDLDVS ILEGDIVGVI KQQDPMGSQN
RWLIDNGVTK GFVYSSFLKP YNPRQSHSDV SIESHSSIES GYGGSSPVFS RQNSNSTLTF
NHETSTVSFS SGHTQNHATL RPSQDSDVSH RIPHIDTPSP SYFPTNQRDT LDSTYRNSSN
QKELSETAVR NAANHRDYSE PLYQNPTNYR DSSDSSHTTP TNHRDPSDSS ETDSCSSNKS
SRHDASQRHT AYSSQQRQNG EYSVQKRRPQ YSADEYIEPD HELDGHQIYY ALYSFNARCA
NELSISANQR VRILEFQDMN GNQEWWLGEA GGRRGYVPSN YIRKSEYT
//