ID Q52KF7_MOUSE Unreviewed; 817 AA.
AC Q52KF7;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 161.
DE SubName: Full=Discs large MAGUK scaffold protein 3 {ECO:0000313|Ensembl:ENSMUSP00000000901.7};
DE SubName: Full=Dlgh3 protein {ECO:0000313|EMBL:AAH94368.1};
GN Name=Dlg3 {ECO:0000313|Ensembl:ENSMUSP00000000901.7,
GN ECO:0000313|MGI:MGI:1888986};
GN Synonyms=Dlgh3 {ECO:0000313|EMBL:AAH94368.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH94368.1};
RN [1] {ECO:0000313|EMBL:AAH94368.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6 {ECO:0000313|EMBL:AAH94368.1};
RC TISSUE=Brain {ECO:0000313|EMBL:AAH94368.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2] {ECO:0007829|PubMed:18034455}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000000901.7, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000000901.7,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5] {ECO:0000313|Ensembl:ENSMUSP00000000901.7}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000000901.7};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; BC094368; AAH94368.1; -; mRNA.
DR RefSeq; NP_001277331.1; NM_001290402.1.
DR IntAct; Q52KF7; 2.
DR ProteomicsDB; 338812; -.
DR Antibodypedia; 342; 362 antibodies from 34 providers.
DR DNASU; 53310; -.
DR Ensembl; ENSMUST00000000901.13; ENSMUSP00000000901.7; ENSMUSG00000000881.13.
DR GeneID; 53310; -.
DR UCSC; uc009twp.3; mouse.
DR AGR; MGI:1888986; -.
DR CTD; 1741; -.
DR MGI; MGI:1888986; Dlg3.
DR VEuPathDB; HostDB:ENSMUSG00000000881; -.
DR GeneTree; ENSGT00940000159565; -.
DR HOGENOM; CLU_001715_4_2_1; -.
DR OrthoDB; 2879721at2759; -.
DR BioGRID-ORCS; 53310; 2 hits in 79 CRISPR screens.
DR ChiTaRS; Mpp3; mouse.
DR Proteomes; UP000000589; Chromosome X.
DR Bgee; ENSMUSG00000000881; Expressed in floor plate of midbrain and 239 other cell types or tissues.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:UniProt.
DR GO; GO:0031594; C:neuromuscular junction; IEA:InterPro.
DR GO; GO:0043005; C:neuron projection; IEA:InterPro.
DR GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 3.
DR CDD; cd12029; SH3_DLG3; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR019583; DLG1-4_PDZ_assoc.
DR InterPro; IPR016313; DLG1-like.
DR InterPro; IPR019590; DLG1_PEST_dom.
DR InterPro; IPR035763; DLG3_SH3.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23119; DISCS LARGE; 1.
DR PANTHER; PTHR23119:SF28; DISKS LARGE HOMOLOG 3; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF10600; PDZ_assoc; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM01277; MAGUK_N_PEST; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|EPD:Q52KF7,
KW ECO:0007829|MaxQB:Q52KF7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 131..218
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 226..313
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 386..467
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 501..571
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 627..802
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 32..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 90328 MW; F969768FA0D82350 CRC64;
MHKHQHCCKC PECYEVTRLA ALRRLEPPGY GDWQVPDPYG PSGGNGASSG YGGYSSQTLP
SQAGATPTPR TKAKLIPTGR DVGPVPPKPV PGKSTPKLNG SGPGWWPECT CTNRDWYEQV
NGSDGMFKYE EIVLERGNSG LGFSIAGGID NPHVPDDPGI FITKIIPGGA AAMDGRLGVN
DCVLRVNEVD VSEVVHSRAV EALKEAGPVV RLVVRRRQPP PETIMEVNLL KGPKGLGFSI
AGGIGNQHIP GDNSIYITKI IEGGAAQKDG RLQIGDRLLA VNNTNLQDVR HEEAVASLKN
TSDMVYLKVA KPGSIHLNDM YAPPDYASTF TALADNHISH NSSLGYLGAV ESKVTYPAPP
QVPPTRYSPI PRHMLAEEDF TREPRKIILH KGSTGLGFNI VGGEDGEGIF VSFILAGGPA
DLSGELRRGD RILSVNGVNL RNATHEQAAA ALKRAGQSVT IVAQYRPEEY SRFESKIHDL
REQMMNSSMS SGSGSLRTSE KRSLYVRALF DYDRTRDSCL PSQGLSFSYG DILHVINASD
DEWWQARLVT PHGESEQIGV IPSKKRVEKK ERARLKTVKF HARTGMIESN RDFPGLSDDY
YGAKNLKGQE DAILSYEPVT RQEIHYARPV IILGPMKDRV NDDLISEFPH KFGSCVPHTT
RPRRDNEVDG QDYHFVVSRE QMEKDIQDNK FIEAGQFNDN LYGTSIQSVR AVAERGKHCI
LDVSGNAIKR LQQAQLYPIA IFIKPKSIEA LMEMNRRQTY EQANKIFDKA MKLEQEFGEY
FTAIVQGDSL EEIYNKIKQI IEDQSGHYIW VPSPEKL
//
