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Database: UniProt
Entry: A0A2K5BZN1_AOTNA
LinkDB: A0A2K5BZN1_AOTNA
Original site: A0A2K5BZN1_AOTNA 
ID   A0A2K5BZN1_AOTNA        Unreviewed;      1974 AA.
AC   A0A2K5BZN1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Dedicator of cytokinesis 4 {ECO:0000313|Ensembl:ENSANAP00000001884.1};
GN   Name=DOCK4 {ECO:0000313|Ensembl:ENSANAP00000001884.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000001884.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000001884.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00983}.
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DR   STRING; 37293.ENSANAP00000001884; -.
DR   Ensembl; ENSANAT00000016596.1; ENSANAP00000001884.1; ENSANAG00000004277.1.
DR   GeneTree; ENSGT00940000155659; -.
DR   OMA; MRDFGHS; -.
DR   Proteomes; UP000233020; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0032420; C:stereocilium; IEA:Ensembl.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR   GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR   GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
DR   GO; GO:1904694; P:negative regulation of vascular associated smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd08695; C2_Dock-B; 1.
DR   CDD; cd11705; DHR2_DOCK4; 1.
DR   CDD; cd12049; SH3_DOCK4_B; 1.
DR   Gene3D; 1.20.58.740; -; 1.
DR   Gene3D; 1.25.40.410; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.20.1270.350; Dedicator of cytokinesis N-terminal subdomain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR037811; C2_Dock-B.
DR   InterPro; IPR027007; C2_DOCK-type_domain.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037014; DHR2_DOCK4.
DR   InterPro; IPR026791; DOCK.
DR   InterPro; IPR035769; DOCK4_SH3.
DR   InterPro; IPR043161; DOCK_C_lobe_A.
DR   InterPro; IPR043162; DOCK_C_lobe_C.
DR   InterPro; IPR032376; DOCK_N.
DR   InterPro; IPR042455; DOCK_N_sub1.
DR   InterPro; IPR027357; DOCKER_dom.
DR   InterPro; IPR046769; DOCKER_Lobe_A.
DR   InterPro; IPR046770; DOCKER_Lobe_B.
DR   InterPro; IPR046773; DOCKER_Lobe_C.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR45653; DEDICATOR OF CYTOKINESIS; 1.
DR   PANTHER; PTHR45653:SF7; DEDICATOR OF CYTOKINESIS PROTEIN 4; 1.
DR   Pfam; PF06920; DHR-2_Lobe_A; 1.
DR   Pfam; PF20422; DHR-2_Lobe_B; 1.
DR   Pfam; PF20421; DHR-2_Lobe_C; 1.
DR   Pfam; PF14429; DOCK-C2; 1.
DR   Pfam; PF16172; DOCK_N; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51650; C2_DOCK; 1.
DR   PROSITE; PS51651; DOCKER; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..59
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          393..566
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1194..1600
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          1653..1733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1746..1974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1470..1497
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1653..1703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1706..1720
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1761..1780
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1801..1878
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1880..1894
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1927..1943
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1974 AA;  226204 MW;  DEB419C89DF21A40 CRC64;
     RWIGFIASFR GTVPYGLSLE IGDTVQILEK CDGWYRGFAL KNPNIKGIFP SSYVHLKNAC
     VKNKGQFEMI IPTEDSVITE MTSTLRDWGT MWKQLYVRNE GDLFHRLWHI MNEILDLRRQ
     VLVGHLTHDR MKDVKRHITA RLDWGNEQLG LDLVPRKEYA MVDPEDISIT ELYRLMEHRH
     RKKDTPVQAS SHHLFVQMKS LMCSNLGEEL EVIFSLFDSK ENRPISERFF LRLNRNGLPK
     APDKPERHCS LFVDLGSSEL RKDIYITVHI IRIGRMGAGE KKNACSVQYR RPFGCAVLSI
     ADLLTGETKD DLILKVYMCN TESEWYQIHE NIIKKLNARY NLTGSNAGLA VSLQLLHGDI
     EQIRREYSSV FSHGVSITRK LGFSNIIMPG EMRNDLYITI ERGEFEKGGK SVARNVEVTM
     FIVDSSGQTL KDFISFGSGE PPASEYHSFV LYHNNSPRWS ELLKLPIPVD KFRGAHIRFE
     FRHCSTKEKG EKKLFGFSFV PLMQEDGRTL PDGTHELIVH KCEENTNLQD TTRYLKLPFS
     KGIFLGNNNQ AMKATKESFC ITSFLCSTKL TQNGDMLDLL KWRTHPDKIT GCLSKLKEID
     GSEIVKFLQD TLDTLFGILD ENSQKYGSKV FDSLVHIINL LQDSKFHHFK PVMDTYIESH
     FAGALAYRDL IKVLKWYVDR ITEAERQEHI QEVLKAQEYI FKYIVQSRRL FSLATGGQNE
     EEFRCCIQEL LMSVRFFLSQ ESKGSGALSQ SQAVFLSSFP AVYSELLKLF DVREVANLVQ
     DTLGSLPTIL HVDDSLQAIK LQCIGKTVES QLYTNPDSRY ILLPVVLHHL HIHLQEQKDL
     IMCARILSNV FCLIKKNSSE KSVLEEIDVI VTSLLDILLR TILEITSRPQ PSSSAMRFQF
     QDVTRTGFLN RESLKWQSYT EQLFSLCRHT YEVPLSSRHT DFLLQIFTVF RILIRPEMFP
     KDWTVMRLVA NNVIITTVLY LSDALRKNFL NENFDYKIWD SYFYLAVIFI NQLCLQLEMF
     TPSKKKKVLE KYGDMRVTMG CEIFSMWQNL GEHKLHFIPA LIGPFLEVTL IPQPDLRNVM
     IPIFHDMMDW EQRRSGNFKQ VEAKLIDKLD SLMSEGKGDE TYRELFNSII PLFGPYPSLL
     KKIERETWRE SGVSLIATVT RLMERLLDYR DCMKMGEVDG KKIGCTVSLL NFYKTELNKE
     EMYIRYIHKL YDLHLKAQNF TEAAYTLLLY DELLEWSDRP LREFLTYPMQ TEWQRKEHLH
     LTIIQNFDRG KCWENGIILC RKIAEQYESY YDYRNLSKMR MMEASLYDKI MDQQRLEPEF
     FRVGFYGKKF PFFLRNKEFV CRGHDYERLE AFQQRMLNEF PHAIAMQHAN QPDETIFQAE
     AQYLQIYAVT PIPESQEVLQ REGVPDNIKS FYKVNHIWKF RYDRPFHKGT KDKENEFKSL
     WVERTSLYLV QSLPGISRWF EVEKREVVEM SPLENAIEVL ENKNQQLKTL ISQCQTRQMQ
     NINPLTMCLN GVIDAAVNGG VSRYQEAFFV KEYILSHPED GEKIARLREL MLEQAQILEF
     GLAVHEKFVP QDMRPLHKKL VDQFFVMKSS LGIQEFSACM QASPIHFPNG SPRVCRNSAP
     ASVSPDGTRV IPRRSPLSYP AVNRYSSSSL SSQASAEVSN ITGQSESSDE VFNMQPSPST
     SSLSSTHSAS PNVTSSAPSS ARASPLLSDK HKHSRENSCL SPRERPCSAI YPTPVEPSQR
     MLFNHIGDGA LPRSDPNLSA PEKAVNPTPS SWSLDSGKEA KNMSDSGKLI SPPVPPRPTQ
     TASPARHTTS ISPSPAGRSP LKGSVQSFTP SPVEYHSPGL ISNSPVLSGS YSSGISSLSR
     CSTSETSGFE NQVNEQSAPV PVPVPMPLPV PVPTYGGEEP VRKESKTPPP YSVYERTLRR
     PVPLPHSLSI PVTPEPPALP PKPLAARSSH LENGARRTDP GPRPRPLPRK VSQL
//
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