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Database: UniProt
Entry: A0A2U3W205_ODORO
LinkDB: A0A2U3W205_ODORO
Original site: A0A2U3W205_ODORO 
ID   A0A2U3W205_ODORO        Unreviewed;      1581 AA.
AC   A0A2U3W205;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, 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};
GN   Name=DNMBP {ECO:0000313|RefSeq:XP_004401963.1};
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_004401963.1};
RN   [1] {ECO:0000313|RefSeq:XP_004401963.1}
RP   IDENTIFICATION.
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_004401963.1; XM_004401906.1.
DR   STRING; 9708.A0A2U3W205; -.
DR   GeneID; 101363028; -.
DR   KEGG; oro:101363028; -.
DR   CTD; 23268; -.
DR   InParanoid; A0A2U3W205; -.
DR   OrthoDB; 25601at2759; -.
DR   Proteomes; UP000245340; 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   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; PF00018; SH3_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF14604; SH3_9; 2.
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:UP000245340};
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..126
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          145..204
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          243..302
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          789..972
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1013..1222
FT                   /note="BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51021"
FT   DOMAIN          1290..1353
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          1517..1580
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          216..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1355..1493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          715..760
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        350..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..658
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1355..1447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1581 AA;  177209 MW;  281A6ABD1CC13E5B CRC64;
     MEAGSVVRAI FDFCPSVSEE LPLFVGDVIE VLAVVDEFWL LGRKEDVTGQ FPSSFVETVT
     IPSLKAGERL FVCVCEFTSQ ELNSLPLHRG DLVILDGAPT APWLQGRSCW GARGFFPSSC
     VRELCLSSQS RCWCPQSALL QIPEYSMGQA RALMGLSAQL DEELDFREGD VITIIGVPEP
     GWFEGELEGR RGIFPEGFVE LLGPLRTVDE LVSSGNHDDC VINGEEETPT GEDERGPEDD
     EEQLGTYGIA LYRFQALEPN ELDFEVGDKI RILGTLEDGW LEGSLKGRTG IFPYRFIKLF
     SKTRAEEAMD PPQESSPTEI PAPSLGCSEN SLVVEGRRPE SPEYKAEKSN CVISETSASP
     PEHLTSEYEV NKNSHQDEDT SGGAPRSPGL GHKQSLAKDS SAEDPSEIIN GVSSQPQVPF
     PPRLQKHQYY STAGGGHQSS EQYADPLPFE ARTKDDSSLP PRGMSSPPKT LQKPVPPPHI
     GSCLLGPRVV TPSQLSSPLQ GMARCAKKHH APKENASSFC SAPERSDMKL GLQDKVFTAE
     AMALLHGEGN TDLDSKLTQQ LIEFEKSLSG PGLEQDKILR HFSIMDFNSE KDIVRGSSKL
     TSQQELPERR KALRPPPPRP RTPASASPHV LLDQNLKPEP PLAMRPSRPA PLPPSAQHRG
     TPVSPRLLTC TRPSCETPEK EGPESVDQTV DQTSQCPLVL VRVQEMEQDL DVGSRAQEEL
     NLALEEKQDE SLREETLEDL EFYESNIESL NMELQQLREM TLLSSQSSSP VVPPGSVYTE
     NPEQRMLEKR AKVIEELLQT ERDYVRDLEM CIEHIMVPLQ QAQIPNIDFE GLFGNMQMVI
     KVSKQLLADL EISDAVGPVF LDHRDELEGT YKVYCQNHDE AISLLEIYEK DEKIQKHLQD
     SLADLKSLYT EWGCTNYINL GSFLIKPVQR VMRYPLLLME LLNSTPESHP DKAPLTNAVL
     AVKEINVNIN EYKRRKDLVL KYRKGDEDSL MEKISKLNIH SIIKKSNRVS SHLKHLTGFA
     PQIKDEAFEE TEKNFRMQER LIKSFIRDLS LYLQHIRESA CVKVVAAVSM WDVCMEKGHR
     DLEQFEKVHR YISDQLFTHF KERTERLVIS PLNQLLSMFT GPHKLVQKRF DKLLDFYNCT
     ERAEKLKDKK TLEELQSARN NYEALNAQLL DELPKFQQFA QGLFTNCVHG YAEAHCDFVR
     RALEQLKPLL SSLKVAGKEG NLTAVFHEEH SRVLQQLQVF TFFPESLPAA RKPFERKTTD
     RPAARKPLLG LPSYMLQSEE LRASLLARYP PEKLFQAERN FNAAQDLDVS LLEGDLVGVI
     KKKDPMGSQN RWLIDNGVST GFVYSSFLKP YNARRSQSDA SVGSHSSTES EPGGSSPRFP
     RQNCSSTLTF NPSSMAVSFT SGSCQKQPQD ATSLKEPDQE TASASLNLGC SESSPSRCPT
     DPDSSSQPRL WDFPEAGRDI HQPGPALRSS RNSRHLETVG HSLPGRNGQG KDLMKGCTRT
     TQCLEDKNEE PESREAEGNQ VYFAVYTFKA RNPNELSVSA NQRLKILEFK DVTGNTEWWL
     AEVNGKKGYV PSNYIRKTEY T
//
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