ID A0A3B5QWY3_XIPMA Unreviewed; 1692 AA.
AC A0A3B5QWY3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Dynamin-binding protein {ECO:0000256|ARBA:ARBA00018186};
DE AltName: Full=Scaffold protein Tuba {ECO:0000256|ARBA:ARBA00032587};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000034850.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000034850.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000034850.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 8083.ENSXMAP00000034850; -.
DR Ensembl; ENSXMAT00000021382.1; ENSXMAP00000034850.1; ENSXMAG00000008159.2.
DR GeneTree; ENSGT00950000183088; -.
DR InParanoid; A0A3B5QWY3; -.
DR OMA; YCGNHEA; -.
DR OrthoDB; 25601at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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:0060271; P:cilium assembly; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR CDD; cd07589; BAR_DNMBP; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11798; SH3_DNMBP_C1; 1.
DR CDD; cd11794; SH3_DNMBP_N1; 1.
DR CDD; cd11796; SH3_DNMBP_N3; 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; 5.
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; 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; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 3.
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:UP000002852};
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 276..335
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 868..1050
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1091..1300
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 1372..1435
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1627..1691
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 332..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1436..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 752..812
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1214..1253
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 332..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..696
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1692 AA; 191864 MW; 86D1EA910B633E6C CRC64;
MEPGSVVRAV FEFLPSVSEE LPLFPGDVIE VLGVVDEFWL LGNKDGVTGQ FPSTFVEEVT
IPGTKPGDRL YVCINDFSSA QSGTLPLKRG DVVVGETRGS LNLGDSWQRG SNAWGLRGLF
PVSCVKELNL SGRSRQLSER SAQAQALELP PYALGQARAL MSLHAQLNEE LDFREGDLII
ITGLPEPGWF QGELEGQRGI FPEGFVELLG PLRSPQVPDD GQYLNEDSQE LIYKDAYDAG
EGPEEEVMEE GEVFLDQEEE QLQEAIIEEE HEEEEEEGLC GVGLYEFRAI EPGELDFNVG
DRIRIVSTLE DGWLEGELRG QRGIFPHRFI KMEGNEQKTA EEKHAEEEKD NDENSNHTSP
NGSENVPESR VYEDHTVWDL DYFENTQEQS LMHEYSTATG QARTIEQNEM NRRPELQPHR
PAPPPNRPSE RPRSTPPARP RLPPRPSLPP HRSELQVSPK SNGNQPNYTN KNRRTLQPKR
TQSLNNCAPG WSKDKMYLQR PPAEISTTNN RSSSISHTLN TIIEGNKQQR LTRHASMSDA
DMTHSAVAHS HYQNKTRGPN GTLPTSITSE ALATSASDLE AKLSQQLFEF EKSLTSSYSD
TNVSSAAFRD LSPSADLNQQ SQVSRHFSIL GYSNENDIIR GSSRSPVSNL SHSNNSSLER
RRTLRPPPPR PRVQRPPPPT VYRPTRPAPR PPARSPRQNA SYPAGTERTN SPSFYNLEKT
TTNDAVEIHT ELGDPTATHE HETLQDTDPD LNREMEAETE RQREEEERYQ VLLRLQEVEQ
EMEEYARTAE ELRAMLEEEE EETARMQTLE NLEFCNYTLE TLALEQQHLQ EMTLLSSQPK
PVDSGPVSDE APAAGTDPED PGQRMLEKRS KVIEELLQTE EDYVNDLQMC IDEIIVPLQE
RKVEVDFEGL FGNISSVIDL SQRLLDRLQE SESVGVVFLD FKAELEEVYK LYCQNHDDAI
SLLESYEKKE NIQGHVLECL ERLRAIYRKQ GKTNYINLGS FLIKPVQRVM RYPLLLSELQ
GATPENHPDR DQLTQAVQAI KQINVNINEY KRRKDLVVKY RKGDEESFID KIAKLSVHSI
IKKSNRVSSH IKHLTGISLQ VKNEEFDDAE KKFRLQERLI KSFIRDVSMY LQHIRESASV
NVLAAISFID IYTERSVLDP ERFQRAHRCI SDKQFTQFKE RAEALVIKPL SQLLVMFAGP
HKLIQKRFDK LLDYDNCKER ADRLKDRRVR DELQVARNNY EALNAQLLDE LRKFNGVAEE
LFKDCVGAFA QAQKDFMKLT LGELRPLLQF SNKVGAEGNL ITQFQEEYHR VLKLLQSFSF
CPENLPQPAG TMKRPFEKKT LEKQSTKKQS QGPPNYAVQT DEHRSALLAG YAPEKLYQAE
RNFNAAQDLD ISIQEGDLVG VIKQQDPMGS NNRWMIDNGV TQGFVYSSFL KPYNPRRSHS
DVSIESQSSN ESGYGGSSPV FSRQNSNSTL TFNQDGATVS YSAAPQSHPS PQPSLDSASS
RRGQATSNPD AVTQSSSSRS QSSRRDYADQ SHRSGGTHRD SEPAHRHSGS QRDSYESRNR
DTSDYSETDS SSSQMNSSRS KRHGHADRSY SSHQWRDGDG TRKSAYSLDE YAEPEPEPEP
EPESELDGHQ IYYALYSFNA RCANEMSISA NERLRILEFQ DLNGNGEWWL GEADGGRRGY
VPSNYIRKSE YT
//
