CHID1_MOUSE
ID CHID1_MOUSE Reviewed; 393 AA.
AC Q922Q9; Q3TVF7; Q6P8U4; Q8C7C5; Q9CXR7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Chitinase domain-containing protein 1;
DE Flags: Precursor;
GN Name=Chid1;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Head, Pancreas, 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 MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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: Saccharide- and LPS-binding protein with possible roles in
CC pathogen sensing and endotoxin neutralization. Ligand-binding
CC specificity relates to the length of the oligosaccharides, with
CC preference for chitotetraose (in vitro) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with STAB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Lysosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q922Q9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q922Q9-2; Sequence=VSP_023827;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61063.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB29142.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC34365.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE35662.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK014071; BAB29142.1; ALT_SEQ; mRNA.
DR EMBL; AK050655; BAC34365.1; ALT_INIT; mRNA.
DR EMBL; AK160156; BAE35662.1; ALT_INIT; mRNA.
DR EMBL; BC006876; AAH06876.1; -; mRNA.
DR EMBL; BC061063; AAH61063.1; ALT_INIT; mRNA.
DR CCDS; CCDS22019.2; -. [Q922Q9-2]
DR CCDS; CCDS52447.2; -. [Q922Q9-1]
DR RefSeq; NP_001136153.1; NM_001142681.1. [Q922Q9-1]
DR RefSeq; NP_080798.2; NM_026522.5. [Q922Q9-2]
DR AlphaFoldDB; Q922Q9; -.
DR SMR; Q922Q9; -.
DR BioGRID; 212618; 3.
DR STRING; 10090.ENSMUSP00000130360; -.
DR iPTMnet; Q922Q9; -.
DR PhosphoSitePlus; Q922Q9; -.
DR SwissPalm; Q922Q9; -.
DR EPD; Q922Q9; -.
DR MaxQB; Q922Q9; -.
DR PaxDb; Q922Q9; -.
DR PeptideAtlas; Q922Q9; -.
DR PRIDE; Q922Q9; -.
DR ProteomicsDB; 281663; -. [Q922Q9-1]
DR ProteomicsDB; 281664; -. [Q922Q9-2]
DR Antibodypedia; 10139; 210 antibodies from 24 providers.
DR DNASU; 68038; -.
DR Ensembl; ENSMUST00000118694; ENSMUSP00000112891; ENSMUSG00000025512. [Q922Q9-2]
DR Ensembl; ENSMUST00000153191; ENSMUSP00000114693; ENSMUSG00000025512. [Q922Q9-1]
DR GeneID; 68038; -.
DR KEGG; mmu:68038; -.
DR UCSC; uc009klp.2; mouse. [Q922Q9-2]
DR UCSC; uc009klq.2; mouse. [Q922Q9-1]
DR CTD; 66005; -.
DR MGI; MGI:1915288; Chid1.
DR VEuPathDB; HostDB:ENSMUSG00000025512; -.
DR eggNOG; KOG2091; Eukaryota.
DR GeneTree; ENSGT00390000012069; -.
DR HOGENOM; CLU_035132_2_0_1; -.
DR InParanoid; Q922Q9; -.
DR OMA; YSINERI; -.
DR OrthoDB; 1067925at2759; -.
DR PhylomeDB; Q922Q9; -.
DR TreeFam; TF319271; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 68038; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Chid1; mouse.
DR PRO; PR:Q922Q9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q922Q9; protein.
DR Bgee; ENSMUSG00000025512; Expressed in spermatid and 249 other tissues.
DR ExpressionAtlas; Q922Q9; baseline and differential.
DR Genevisible; Q922Q9; MM.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0070492; F:oligosaccharide binding; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISO:MGI.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Immunity; Innate immunity; Lysosome;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..393
FT /note="Chitinase domain-containing protein 1"
FT /id="PRO_0000280609"
FT DOMAIN 79..393
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT VAR_SEQ 235..320
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023827"
FT CONFLICT 334
FT /note="W -> R (in Ref. 1; BAE35662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 44906 MW; 492C5C84288B1DDC CRC64;
MWPLLHVLWL ALVCGSVHTT LSKSDAKKAA SKMLLEKTQF SDKPVQDRGL VVTDIKAEDV
VLEHRSYCSS RARERNFAGE VLGYVTPWNS HGYDVAKVFG SKFTQISPVW LQLKRRGREM
FEITGLHDVD QGWMRAVKKH AKGVRIVPRL LFEDWTYDDF RNVLDSEDEI EELSKTVAQV
AKNQHFDGFV VEVWSQLLSQ KHVGLIHMLT HLAEALHQAR LLVILVIPPA VTPGTDQLGM
FTHKEFEQLA PILDGFSLMT YDYSTSQQPG PNAPLSWIRA CVQVLDPKSQ WRSKILLGLN
FYGMDYAASK DAREPVIGAR YVQTLKDHRP RVVWDSQAAE HFFEYKKNRG GRHVVFYPTL
KSLQVRLELA RELGVGVSIW ELGQGLDYFY DLL
