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LRCH3_MOUSE
ID   LRCH3_MOUSE             Reviewed;         778 AA.
AC   Q8BVU0; B2RXA0; Q3U222; Q3UZ74;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=DISP complex protein LRCH3 {ECO:0000250|UniProtKB:Q96II8};
DE   AltName: Full=Leucine-rich repeat and calponin homology domain-containing protein 3 {ECO:0000312|MGI:MGI:1917394};
GN   Name=Lrch3 {ECO:0000312|MGI:MGI:1917394};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-415 AND SER-625, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC   Testis;
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).
CC   -!- FUNCTION: As part of the DISP complex, may regulate the association of
CC       septins with actin and thereby regulate the actin cytoskeleton.
CC       {ECO:0000250|UniProtKB:Q96II8}.
CC   -!- SUBUNIT: Component of the DOCK7-induced septin displacement/DISP
CC       complex, at least composed of DOCK7, LRCH3 and MYO6.
CC       {ECO:0000250|UniProtKB:Q96II8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96II8}.
CC   -!- CAUTION: Predicted to contain a signal peptide and to be secreted.
CC       However, this is not consistent with an interaction with DOCK7 and MYO6
CC       and the suggested function in cytoskeleton organization.
CC       {ECO:0000250|UniProtKB:Q96II8}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE21984.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAE33320.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK134026; BAE21984.1; ALT_INIT; mRNA.
DR   EMBL; AK155550; BAE33320.1; ALT_FRAME; mRNA.
DR   EMBL; AK076529; BAC36380.1; -; mRNA.
DR   EMBL; CH466521; EDK97821.1; -; Genomic_DNA.
DR   EMBL; BC151058; AAI51059.1; -; mRNA.
DR   CCDS; CCDS37315.1; -.
DR   RefSeq; NP_001074724.1; NM_001081255.1.
DR   RefSeq; NP_001297603.1; NM_001310674.1.
DR   AlphaFoldDB; Q8BVU0; -.
DR   SMR; Q8BVU0; -.
DR   BioGRID; 213886; 2.
DR   STRING; 10090.ENSMUSP00000023491; -.
DR   iPTMnet; Q8BVU0; -.
DR   PhosphoSitePlus; Q8BVU0; -.
DR   EPD; Q8BVU0; -.
DR   jPOST; Q8BVU0; -.
DR   MaxQB; Q8BVU0; -.
DR   PaxDb; Q8BVU0; -.
DR   PeptideAtlas; Q8BVU0; -.
DR   PRIDE; Q8BVU0; -.
DR   ProteomicsDB; 292031; -.
DR   Antibodypedia; 2704; 96 antibodies from 18 providers.
DR   Ensembl; ENSMUST00000023491; ENSMUSP00000023491; ENSMUSG00000022801.
DR   GeneID; 70144; -.
DR   KEGG; mmu:70144; -.
DR   UCSC; uc007yzr.1; mouse.
DR   CTD; 84859; -.
DR   MGI; MGI:1917394; Lrch3.
DR   VEuPathDB; HostDB:ENSMUSG00000022801; -.
DR   eggNOG; KOG0532; Eukaryota.
DR   GeneTree; ENSGT00940000158330; -.
DR   InParanoid; Q8BVU0; -.
DR   TreeFam; TF318428; -.
DR   BioGRID-ORCS; 70144; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Lrch3; mouse.
DR   PRO; PR:Q8BVU0; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q8BVU0; protein.
DR   Bgee; ENSMUSG00000022801; Expressed in manus and 228 other tissues.
DR   ExpressionAtlas; Q8BVU0; baseline and differential.
DR   Genevisible; Q8BVU0; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0032185; P:septin cytoskeleton organization; ISS:UniProtKB.
DR   Gene3D; 1.10.418.10; -; 1.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00369; LRR_TYP; 5.
DR   SUPFAM; SSF47576; SSF47576; 1.
DR   PROSITE; PS50021; CH; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Leucine-rich repeat; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..778
FT                   /note="DISP complex protein LRCH3"
FT                   /id="PRO_0000253485"
FT   REPEAT          56..79
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          81..104
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          105..127
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          128..150
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          152..172
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          173..195
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          197..218
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          220..239
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          240..264
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          266..290
FT                   /note="LRR 10"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          645..758
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REGION          56..290
FT                   /note="Mediates interaction with DOCK7"
FT                   /evidence="ECO:0000250|UniProtKB:Q96II8"
FT   REGION          382..642
FT                   /note="Mediates direct interaction with MYO6"
FT                   /evidence="ECO:0000250|UniProtKB:Q96II8"
FT   REGION          511..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          758..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         415
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         419
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96II8"
FT   MOD_RES         608
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96II8"
FT   MOD_RES         625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        92
FT                   /note="N -> D (in Ref. 1; BAC36380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="E -> K (in Ref. 1; BAC36380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="E -> K (in Ref. 1; BAE33320)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        206
FT                   /note="N -> I (in Ref. 1; BAC36380)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   778 AA;  86341 MW;  FCB59AE20EAB096B CRC64;
     MAAAGLVAVV AAAEYSGPVA SGGNLSGATC GPSPGLGPGP GPGSWSRSVD RALEEAAVTG
     VLSLSGRKLR EFPRGAANHD LTDTTRADLS RNRLSEIPME ACHFVSLESL NLYQNCIRYI
     PEAVLNLQAL TFLNISRNQL STLPVHLCNL PLKVLIASNN KLVSLPEEIG HLRHLTELDV
     SCNEIQTVPS QIGNLEALRD FNVRRNHLLR LPEELAEVPL IRLDFSCNKI TVIPVCYRNL
     RHLQVITLDN NPLQSPPAQI CIKGKIHIFK YLNIQACKIA PDLPDYERRP LGFGSCHEEL
     YSGRPYGALD SGFNSVDSGD KRWSGNEPTD EFSDLPLRVA EITKEQRLRR ESQYQENRSS
     VAVTNGGVEH DLDQIDYIDS CTTEEEENDV KQPKSLDTNS LSSQFMAYIE QRRISHEVSP
     VKPIAVREFQ KTEDMKRYSH QNRVPVEPSL VLSMPPSHNQ LSHSDLELHQ RREQSIECTR
     REAQLAALQY EEEKIRTKQI QRDAVLDFVK QKASHNPQRQ QPPGNGECSF PSRRSQHTDD
     SALLVSLSGL DGVSCVATRP HSSAFTPLKS ENRVDVTSSF PMTETVHHSP AYSFPAATQR
     NQPQRPESFL FRAAVRAEAN KGRASPLLLS SAPATDPTDA ITRQREEELK LIDQLRKHIE
     YRLKVSLPCD LGAALTDGVV LCHLANHVRP RSVPSIHVPS PAVPKLTMAK CRRNVENFLD
     ACRKIGVPQE QLCLPLHILE EKGLGQVAVT VQALLELAPP KQPPPQQPQQ QQPQLSAV
 
 
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