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Database: UniProt
Entry: M3WHB8_FELCA
LinkDB: M3WHB8_FELCA
Original site: M3WHB8_FELCA 
ID   M3WHB8_FELCA            Unreviewed;      1970 AA.
AC   M3WHB8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 3.
DT   24-JAN-2024, entry version 74.
DE   SubName: Full=Dedicator of cytokinesis 4 {ECO:0000313|Ensembl:ENSFCAP00000011734.5};
GN   Name=DOCK4 {ECO:0000313|Ensembl:ENSFCAP00000011734.5,
GN   ECO:0000313|VGNC:VGNC:61573};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000011734.5, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000011734.5, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011734.5,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000011734.5, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011734.5,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000011734.5}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011734.5};
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   EMBL; AANG04000096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_011278815.1; XM_011280513.2.
DR   STRING; 9685.ENSFCAP00000011734; -.
DR   PaxDb; 9685-ENSFCAP00000011734; -.
DR   Ensembl; ENSFCAT00000012658.6; ENSFCAP00000011734.5; ENSFCAG00000012655.6.
DR   GeneID; 101082809; -.
DR   KEGG; fca:101082809; -.
DR   CTD; 9732; -.
DR   VGNC; VGNC:61573; DOCK4.
DR   eggNOG; KOG1998; Eukaryota.
DR   eggNOG; KOG3166; Eukaryota.
DR   GeneTree; ENSGT00940000155659; -.
DR   HOGENOM; CLU_000595_2_0_1; -.
DR   InParanoid; M3WHB8; -.
DR   OMA; MRDFGHS; -.
DR   OrthoDB; 8258at2759; -.
DR   Proteomes; UP000011712; Chromosome A2.
DR   Bgee; ENSFCAG00000012655; Expressed in brain and 10 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
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; 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; 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   Pfam; PF07653; SH3_2; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          6..67
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          401..574
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1199..1605
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          1658..1738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1751..1970
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1475..1502
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1658..1708
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1711..1725
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1766..1785
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1806..1884
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1970 AA;  225582 MW;  61ABBA6DA7F7E32A CRC64;
     MWIPTEHEKY GVVIASFRGT VPYGLSLEIG DTVQILEKCD GWYRGFALKN PNVKGIFPSS
     YVHLKNACVK NKGQFEMVIP TEDSVITEMT STLRDWGTMW KQLYVRNEGD LFHRLWHIMN
     EILDLRRQVL VGHLTHDRMK DVKRHITARL DWGNEQLGLD LVPRKEYAMV DPEDISITEL
     YRLMEHRHRK KDTPVQASNH HLFVQMKSLM CSNLGEELEV IFSLFDSKEN RPISERFFLR
     LNRNGLPKAP DKPERHCSLF VDLGSSELRR DIYITVHIIR IGRMGAGEKK NACSVQYRRP
     FGCAVLSIAD LLTGETKDDL ILKVYMCNTE SEWYQIHENI IKKLNARYNL TGSNAGLAVS
     LQLLHGDIEQ IRREYSSVFS HGVSITRKLG FSNIIMPGEM RNDLYITIER GEFEKGGKSV
     ARNVEVTMFI VESSGQILKD FISFGSGEPP ASEYHSFVLY HNNSPRWSEL LKLPIPVDKF
     RGAHIRFEFR HCSTKEKGEK KLFGFSFVPL MQEDGRTLPD GTHELIVHKC EENTNLQDTT
     RYLKLPFSKG ILLGNNHQAM KATKESFWIT SFLCSTKLTQ NGDMLDLLKW RTHPDKITGC
     LSKLKEIDGS EIVKFLQDTL DTLFGILDEN SQKYGSKVFD SLVHIINLLQ DSKFHHFKPV
     MDTYIESHFA GALAYRDLIK VLKWYVDRIT EAERQEHIQE VLKAQEYIFK YIVQSRRLFS
     LATGGQNEEE FRCCIQELLM SVRFFLSQES KGSGALSQSQ AVFLSSFPAV YSELLKLFDV
     REVANLVQDT LGSLPTIVHV DDSLQAVKLQ CIGKTVESQL YTNPDSRYIL LPVVLHHLHM
     HLQEQKDLIM CARILSNVFC LIKKNSSEKS VLEEIDVIVA SLLDILLRTI LEITSRPQSS
     GSAMRLQFQD VTGEFVACLL SLLRQMTDRH YQQLLDSFNT KEELRDFLLQ IFTVFRILIR
     PEMFPKDWTV MRLVANNVII TTVLYLSDAL RKNFLNENFD YKIWDSYFYL AVIFINQLCL
     QLEMFTPSKK KKVLEKYGDM RVTMGCEIFS MWQNLGEHKL HFIPALIGPF LEVTLIPQPD
     LRNVMIPIFH DMMDWEQRRT GNFKQVEAKL IDKLDSLMSE GKGDETYREL FNSIIPLFGP
     YPSLLKKIER ETWRESGVSL IATVTRLMER LLDYRDCMKM GEVDGKKIGC TVSLLNFYKT
     ELNKEEMYIR YIHKLYDLHL KAQNFTEAAY TLLLYDELLE WSDRPLREFL TYPMQTEWQR
     KEHLHLAIIQ NFDRGKCWEN GIILCRKIAE QYESYYDYRN LSKMRMMEAS LYDKIMDQQR
     LEPEFFRVGF YGKKFPFFLR NKEFVCRGHD YERLEAFQQR MLNEFPHAIA MQHANQPDET
     IFQAEAQYLQ IYAVTPIPES QEVLQREGVP DNIKSFYKVN HIWKFRYDRP FHKGTKDKEN
     EFKSLWVERT SLYLVQSLPG ISRWFEVEKR EVVEMSPLEN AIEVLENKNQ QLKTLISQCQ
     TRQMQNINPL TMCLNGVIDA AVNGGVSRYQ EAFFVKEYIL SHPEDGEKIA RLRELMLEQA
     QILEFGLAVH EKFVPQDMRP LHKKLVDQFF VMKSSLGIQE FSACIQASPV HFPNGSPRVC
     RNSAPASMSP DGTRVIPRRS PLSYPAVNRY SSSSLSSQAS AEVSNITGQS ESSDEVFNMQ
     PSPSTSSLSS THSASPNVTS SAPSSARASP LLSDKHKHSR ENSCLSPRER PCSAIYPTPG
     ETSQRLLFNH IGDGALPRSD PNLSAPEKAV NPTPSSWSLD SGKEAKNMSD SGKILSPPVP
     PRPTQTASPA RHTTSVSPSP AGRSPLKGSV QSFTPSPVEY HSPGLISNSP VLSGSYSSGI
     SSLSRCSTSE TSGFENQVNE QSAPAAGPGY SGPEEPVRKE SKTPPPYSVY ERTLRRPVPL
     PHSLSIPVTA EPPALPPKPL AARPGHLENG TRRTEPGPRP RPLPRKVSQL
//
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