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