GenomeNet

Database: UniProt
Entry: F1M907_RAT
LinkDB: F1M907_RAT
Original site: F1M907_RAT 
ID   F1M907_RAT              Unreviewed;       740 AA.
AC   F1M907;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 4.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Discs large MAGUK scaffold protein 2 {ECO:0000313|Ensembl:ENSRNOP00000052268.5};
GN   Name=Dlg2 {ECO:0000313|Ensembl:ENSRNOP00000052268.5,
GN   ECO:0000313|RGD:619895};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000052268.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000052268.5, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000052268.5,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000052268.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000052268.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   AlphaFoldDB; F1M907; -.
DR   Ensembl; ENSRNOT00000055401.5; ENSRNOP00000052268.5; ENSRNOG00000022635.8.
DR   RGD; 619895; Dlg2.
DR   VEuPathDB; HostDB:ENSRNOG00000022635; -.
DR   GeneTree; ENSGT00940000155156; -.
DR   HOGENOM; CLU_001715_4_2_1; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000022635; Expressed in frontal cortex and 17 other cell types or tissues.
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; cd12032; SH3_DLG2; 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; IPR035759; DLG2_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:SF6; DISKS LARGE HOMOLOG 2; 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; 2.
DR   SMART; SM00072; GuKc; 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   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..90
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          98..185
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          326..407
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          441..511
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          550..725
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
SQ   SEQUENCE   740 AA;  82032 MW;  244A6DB9DF102C1C CRC64;
     LEKHQNTIGN SGLGFSIAGG TDNPHIGDDP GIFITKIIPG GAAAEDGRLR VNDCILRVNE
     VDVSEVSHSK AVEALKEAGS IVRLYVRRRR PILETVVEIK LFKGPKGLGF SIAGGVGNQH
     IPGDNSIYVT KIIDGGAAQK DGRLQVGDRL LMVNNYSLEE VTHEEAVAIL KNTSDVVYLK
     VGKPTTIYMT DPYGPPDITH SYSPPMENHL LSGNNGTLEY KTSLPPISPG RYSPIPKHML
     VEDDYTRPPE PVYSTVNKLC DKPASPRHYS PVECDKSFLL STPYPHYHLG LLPDSDMTSH
     SQHSTATRQP SVTLQRAISL EGEPRKVVLH KGSTGLGFNI VGGEDGEGIF VSFILAGGPA
     DLSGELQRGD QILSVNGIDL RGASHEQAAA ALKGAGQTVT IIAQYQPEDY ARFEAKIHDL
     REQMMNHSMS SGSGSLRTNQ KRSLYVRAMF DYDKSKDSGL PSQGLSFKYG DILHVINASD
     DEWWQARRVI LDGDSEEMGV IPSKRRVERK ERARLKTVKF NAKPGVIDSK GDIPGLGDDG
     YGTKTLINYT RPVIILGPMK DRINDDLISE FPDKFGSCVP HTTRPKRDYE VDGRDYHFVI
     SREQMEKDIQ EHKFIEAGQY NDNLYGTSVQ SVRFVAERGK HCILDVSGNA IKRLQVAQLY
     PIAIFIKPKS LEPLMEMNKR LTEEQAKKTY DRAIKLEQEF GEYFTAIVQG DTLEDIYNQC
     KLVIEEQSGP FIWIPSKEKL
//
DBGET integrated database retrieval system