LYSM2_MOUSE
ID LYSM2_MOUSE Reviewed; 215 AA.
AC Q9D7V2; Q80ZR2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=LysM and putative peptidoglycan-binding domain-containing protein 2;
GN Name=Lysmd2;
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; TISSUE=Stomach;
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 MRNA] (ISOFORM 2).
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D7V2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D7V2-2; Sequence=VSP_020124;
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DR EMBL; AK008800; BAB25902.1; -; mRNA.
DR EMBL; BC048545; AAH48545.1; -; mRNA.
DR CCDS; CCDS40693.1; -. [Q9D7V2-1]
DR RefSeq; XP_006511494.1; XM_006511431.1. [Q9D7V2-2]
DR AlphaFoldDB; Q9D7V2; -.
DR SMR; Q9D7V2; -.
DR STRING; 10090.ENSMUSP00000034702; -.
DR iPTMnet; Q9D7V2; -.
DR PhosphoSitePlus; Q9D7V2; -.
DR EPD; Q9D7V2; -.
DR MaxQB; Q9D7V2; -.
DR PaxDb; Q9D7V2; -.
DR PeptideAtlas; Q9D7V2; -.
DR PRIDE; Q9D7V2; -.
DR ProteomicsDB; 292153; -. [Q9D7V2-1]
DR ProteomicsDB; 292154; -. [Q9D7V2-2]
DR DNASU; 70082; -.
DR GeneID; 70082; -.
DR UCSC; uc009qsr.1; mouse. [Q9D7V2-1]
DR CTD; 256586; -.
DR MGI; MGI:1917332; Lysmd2.
DR eggNOG; ENOG502S0XR; Eukaryota.
DR InParanoid; Q9D7V2; -.
DR PhylomeDB; Q9D7V2; -.
DR BioGRID-ORCS; 70082; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9D7V2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D7V2; protein.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR045030; LYSM1-4.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR20932; PTHR20932; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IV50"
FT CHAIN 2..215
FT /note="LysM and putative peptidoglycan-binding domain-
FT containing protein 2"
FT /id="PRO_0000248003"
FT DOMAIN 71..115
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..168
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8IV50"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IV50"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IV50"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IV50"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020124"
FT CONFLICT 103..106
FT /note="TNDC -> NNER (in Ref. 1; BAB25902)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="F -> L (in Ref. 1; BAB25902)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="E -> D (in Ref. 1; BAB25902)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="D -> E (in Ref. 1; BAB25902)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="P -> L (in Ref. 1; BAB25902)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="Q -> H (in Ref. 1; BAB25902)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="K -> E (in Ref. 1; BAB25902)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 215 AA; 23694 MW; 1CB7CEAC83F12276 CRC64;
MADLSPAPAL REGGPRAHRP SAPSPPPRSR STSEPEEAEL SLSLARTKTR SYGSTASVRA
PLGARVIERH VEHRVRAGDT LQGIALKYGV TMEQIKRANK LFTNDCIFLK KTLSIPILSE
KPLLFNGLNS IDSPESETVD SSFCQEEEPV VSEEELPPPS PQDPDPKPAQ PEEVSARDFL
QRLDLQIKLS TQAARKLKEE SRDEESPYAA SLYHS
