DRP2_RAT
ID DRP2_RAT Reviewed; 957 AA.
AC Q9EPA0; G3V971;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Dystrophin-related protein 2;
DE Short=DRP-2;
GN Name=Drp2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=11083927; DOI=10.1006/mcne.2000.0895;
RA Roberts R.G., Sheng M.;
RT "Association of dystrophin-related protein 2 (DRP2) with postsynaptic
RT densities in rat brain.";
RL Mol. Cell. Neurosci. 16:674-685(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:EDM07026.1};
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH PRX, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11430802; DOI=10.1016/s0896-6273(01)00327-0;
RA Sherman D.L., Fabrizi C., Gillespie C.S., Brophy P.J.;
RT "Specific disruption of a Schwann cell dystrophin-related protein complex
RT in a demyelinating neuropathy.";
RL Neuron 30:677-687(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
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).
CC -!- FUNCTION: Required for normal myelination and for normal organization
CC of the cytoplasm and the formation of Cajal bands in myelinating
CC Schwann cells. Required for normal PRX location at appositions between
CC the abaxonal surface of the myelin sheath and the Schwann cell plasma
CC membrane. Possibly involved in membrane-cytoskeleton interactions of
CC the central nervous system. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q05AA6}.
CC -!- SUBUNIT: Interacts with PRX; this enhances phosphorylation
CC (PubMed:11430802). Identified in a dystroglycan complex that contains
CC at least PRX, DRP2, UTRN, DMD and DAG1 (By similarity).
CC {ECO:0000250|UniProtKB:Q05AA6, ECO:0000269|PubMed:11430802}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic density
CC {ECO:0000269|PubMed:11083927}. Cell projection, dendrite
CC {ECO:0000269|PubMed:11083927}. Perikaryon
CC {ECO:0000269|PubMed:11083927}. Cell membrane
CC {ECO:0000269|PubMed:11430802, ECO:0000305|PubMed:11083927}; Peripheral
CC membrane protein {ECO:0000305}. Note=Detected in Schwann cells at
CC periaxonal myelin membranes. {ECO:0000269|PubMed:11430802}.
CC -!- TISSUE SPECIFICITY: Detected in trigeminal nerve Schwann cells
CC (PubMed:11430802). Detected in brain cortex and hippocampus. Detected
CC in brain membrane fractions and highly enriched in the postsynaptic
CC density (at protein level). {ECO:0000269|PubMed:11083927,
CC ECO:0000269|PubMed:11430802}.
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DR EMBL; AF195787; AAG28484.1; -; mRNA.
DR EMBL; AF195788; AAG28485.1; -; mRNA.
DR EMBL; AC094684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473969; EDM07026.1; -; Genomic_DNA.
DR EMBL; CH473969; EDM07027.1; -; Genomic_DNA.
DR EMBL; CH473969; EDM07028.1; -; Genomic_DNA.
DR RefSeq; NP_076461.1; NM_023971.1.
DR RefSeq; XP_008771655.1; XM_008773433.2.
DR AlphaFoldDB; Q9EPA0; -.
DR SMR; Q9EPA0; -.
DR BioGRID; 249354; 2.
DR STRING; 10116.ENSRNOP00000037371; -.
DR iPTMnet; Q9EPA0; -.
DR PhosphoSitePlus; Q9EPA0; -.
DR PaxDb; Q9EPA0; -.
DR PRIDE; Q9EPA0; -.
DR Ensembl; ENSRNOT00000039864; ENSRNOP00000037371; ENSRNOG00000026704.
DR GeneID; 66027; -.
DR KEGG; rno:66027; -.
DR UCSC; RGD:621750; rat.
DR CTD; 1821; -.
DR RGD; 621750; Drp2.
DR eggNOG; KOG4286; Eukaryota.
DR GeneTree; ENSGT00940000153467; -.
DR InParanoid; Q9EPA0; -.
DR OMA; QADHVMD; -.
DR OrthoDB; 72477at2759; -.
DR PRO; PR:Q9EPA0; -.
DR Proteomes; UP000002494; Chromosome X.
DR Proteomes; UP000234681; Chromosome x.
DR Bgee; ENSRNOG00000026704; Expressed in frontal cortex and 9 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; IEA:InterPro.
DR GO; GO:0050808; P:synapse organization; IMP:RGD.
DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR CDD; cd00176; SPEC; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR017433; Dystrophin-related_2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 1.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF038205; Dystrophin-related_p2; 1.
DR SMART; SM00150; SPEC; 2.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..957
FT /note="Dystrophin-related protein 2"
FT /id="PRO_0000345016"
FT REPEAT 102..179
FT /note="Spectrin 1"
FT REPEAT 231..337
FT /note="Spectrin 2"
FT DOMAIN 358..383
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT ZN_FING 605..661
FT /note="ZZ-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 877..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 610
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 613
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 634
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 637
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05AA6"
FT MOD_RES 910
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05AA6"
FT CONFLICT 525
FT /note="Q -> K (in Ref. 1; AAG28484/AAG28485)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="K -> R (in Ref. 1; AAG28484/AAG28485)"
FT /evidence="ECO:0000305"
FT CONFLICT 928..929
FT /note="LC -> HS (in Ref. 1; AAG28484/AAG28485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 957 AA; 108045 MW; 1C245F6C90EB26BC CRC64;
MQPLVMQGCP YTLPRCHEWH AADRFHHSSS LRNTCPQPQV RAAVTIPAPP WDGAGDPCLS
PKLLNGSVGA VGPLEPSAMN LCWNEIKKKS HNLRARLEAF SDHSGKLQLP LQEIIDWLSQ
KDEELSAQLP LQGDVALVQQ EKETHAAFME EVKSKGPYIY SVLESAQAFL SQHPFEELEE
SHSESKDTSP RQRIQNLSRF VWKQATVASE LWEKLTARCV DQHRHIEHTL EHLLEIQGAM
EELSSTLTQA EGVRATWEPI GDLFIDSLPE HIQAIKLFKE EFSPVKDGVK LVNDLAHQLA
ISDVHLSMEN SRALEQINVR WKQLQVSVAE RLKQLQDAHR DFGPGSQHFL STSVQVPWER
AISPNKVPYY INHQAQTTCW DHPKMTELYQ TLADLNNIKF SAYRTAMKLR RVQKALRLDL
VTLTTALEIF NEHDLQASEH VMDVVEVIHC LTALYERLEE ERGILVNVPL CVDMSLNWLL
NVFDSGRSGK MRALSFKTGI ACLCGTEVKE KLQYLFSQVA NSGSQCDQRH LGALLHEAIQ
VPRQLGEVAA FGGSNVEPSV RSCFRFSTGK PVIEASQFLE WVNLEPQSMV WLAVLHRVTV
AEQVKHQTKC SICRQCPIKG FRYRSLKQFN VDICQTCFLT GKASKGNKLH YPIMEYYTPT
TSSENMRDFA TTLKNKFRSK QYFSKHPQRG YLPVQSVLES DCSETPASSP MLPHADTHSR
IEHFASRLAE MESQNCSFFN DSLSPDDSID EDQYLLRHSS PITDREPAFG QQAPCSMATE
SKGELEKILA HLEDENRILQ GELRRLKWQH EEAVEAPTLA EGSAEATPDH RNEELLAEAR
ILRQHKSRLE TRMQILEDHN KQLESQLQRL RELLLQPPTE SDGNGSAGSS LASSPRQSEG
SHPREKGQTT PDTEAADDVG SKSQDVSLCL EDIMEKLRHA FPSVRSSDVT ANTLLAS
