LRA25_RAT
ID LRA25_RAT Reviewed; 189 AA.
AC Q566R4;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Leucine repeat adapter protein 25 {ECO:0000303|PubMed:25107909};
DE AltName: Full=Mammary tumor virus receptor 2 {ECO:0000312|EMBL:AAH93377.1};
GN Name=Fam89b {ECO:0000312|RGD:1311544};
GN Synonyms=Lrap25 {ECO:0000303|PubMed:25107909},
GN Mtvr2 {ECO:0000312|EMBL:AAH93377.1};
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] (ISOFORMS 1 AND 2), AND INTERACTION WITH
RP CDC42BPA AND CDC42BPB.
RC TISSUE=Brain;
RX PubMed=25107909; DOI=10.1074/jbc.m114.588079;
RA Lee I.C., Leung T., Tan I.;
RT "Adaptor protein LRAP25 mediates myotonic dystrophy kinase-related Cdc42-
RT binding kinase (MRCK) regulation of LIMK1 protein in lamellipodial F-actin
RT dynamics.";
RL J. Biol. Chem. 289:26989-27003(2014).
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 MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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).
CC -!- FUNCTION: Negatively regulates TGF-beta-induced signaling; in
CC cooperation with SKI prevents the translocation of SMAD2 from the
CC nucleus to the cytoplasm in response to TGF-beta. Acts as an adapter
CC that mediates the specific recognition of LIMK1 by CDC42BPA and
CC CDC42BPB in the lamellipodia. LRAP25-mediated CDC42BPA/CDC42BPB
CC targeting to LIMK1 and the lamellipodium results in LIMK1 activation
CC and the subsequent phosphorylation of CFL1 which is important for
CC lamellipodial F-actin regulation. {ECO:0000250|UniProtKB:Q9QUI1}.
CC -!- SUBUNIT: Interacts with SKI (By similarity). Interacts (via LRR repeat)
CC with CDC42BPA (via AGC-kinase C-terminal domain) and CDC42BPB (via AGC-
CC kinase C-terminal domain) (PubMed:25107909). Interacts (via LRR repeat)
CC with LIMK1 (via LIM zinc-binding domains). Forms a tripartite complex
CC with CDC42BPA, CDC42BPB and LIMK1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9QUI1, ECO:0000269|PubMed:25107909}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QUI1}. Cell
CC projection, lamellipodium {ECO:0000250|UniProtKB:Q9QUI1}. Note=Co-
CC localizes with CDC42BPA, CDC42BPB and LIMK1 in the lamellipodium.
CC {ECO:0000250|UniProtKB:Q9QUI1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q566R4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q566R4-2; Sequence=VSP_059109;
CC -!- SIMILARITY: Belongs to the FAM89 family. {ECO:0000305}.
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DR EMBL; AC134224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093377; AAH93377.1; -; mRNA.
DR RefSeq; NP_001015013.1; NM_001015013.1. [Q566R4-1]
DR AlphaFoldDB; Q566R4; -.
DR SMR; Q566R4; -.
DR STRING; 10116.ENSRNOP00000016987; -.
DR PaxDb; Q566R4; -.
DR Ensembl; ENSRNOT00000016987; ENSRNOP00000016987; ENSRNOG00000024239. [Q566R4-1]
DR GeneID; 309170; -.
DR KEGG; rno:309170; -.
DR UCSC; RGD:1311544; rat. [Q566R4-1]
DR CTD; 23625; -.
DR RGD; 1311544; Fam89b.
DR eggNOG; ENOG502S05U; Eukaryota.
DR GeneTree; ENSGT00940000153370; -.
DR HOGENOM; CLU_128818_0_0_1; -.
DR InParanoid; Q566R4; -.
DR OMA; EAIQECK; -.
DR OrthoDB; 1585340at2759; -.
DR PhylomeDB; Q566R4; -.
DR PRO; PR:Q566R4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000024239; Expressed in skeletal muscle tissue and 20 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:RGD.
DR GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; ISO:RGD.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR InterPro; IPR039499; LURA1/LRA25.
DR Pfam; PF14854; LURAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Leucine-rich repeat;
KW Phosphoprotein; Receptor; Reference proteome; Repeat.
FT CHAIN 1..189
FT /note="Leucine repeat adapter protein 25"
FT /id="PRO_0000441754"
FT REPEAT 86..114
FT /note="LRR"
FT /evidence="ECO:0000305|PubMed:25107909"
FT REGION 55..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5H3"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5H3"
FT VAR_SEQ 98..110
FT /note="Missing (in isoform 2)"
FT /id="VSP_059109"
SQ SEQUENCE 189 AA; 20169 MW; B1626D622E0E1761 CRC64;
MNGLPSTEAP GGAGCALAGL PPLPRGLSGL LNASGGSWRE LERVYSQRSR IHDELSRAAR
APDGPRHAAG SANLGSAAGP RRPVNLDSAL AALRKEMVGL RQLDMSLLCQ LWGLYESIQD
YKHLCQDLSL CQDLSSSLHS DSSYPPDAGL SDDDEPPDAS LPPDPPPLTV PQTHNARDQW
LQDAFQISL
