ID CH3L1_MOUSE Reviewed; 381 AA.
AC Q61362; Q4FJW9; Q8BKL8; Q99J84;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 01-MAY-2013, entry version 110.
DE RecName: Full=Chitinase-3-like protein 1;
DE AltName: Full=BRP39 protein;
DE AltName: Full=Cartilage glycoprotein 39;
DE Short=CGP-39;
DE Short=GP-39;
DE Flags: Precursor;
GN Name=Chi3l1; Synonyms=Brp39;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=7970700;
RA Morrison B.W., Leder P.;
RT "neu and ras initiate murine mammary tumors that share genetic markers
RT generally absent in c-myc and int-2-initiated tumors.";
RL Oncogene 9:3417-3426(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
RA Mollenhauer J., Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Carbohydrate-binding lectin with a preference for
CC chitin. May play a role in defense against pathogens, or in tissue
CC remodeling. May play an important role in the capacity of cells to
CC respond to and cope with changes in their environment (By
CC similarity).
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space (By
CC similarity).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC -!- CAUTION: Although it belongs to the glycosyl hydrolase 18 family,
CC Leu-141 is present instead of the conserved Glu which is an active
CC site residue. Therefore this protein lacks chitinase activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC34654.1; Type=Erroneous initiation;
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DR EMBL; X93035; CAA63603.1; -; mRNA.
DR EMBL; AK051475; BAC34654.1; ALT_INIT; mRNA.
DR EMBL; CT010283; CAJ18491.1; -; mRNA.
DR EMBL; BC003780; AAH03780.1; -; mRNA.
DR EMBL; BC004734; AAH04734.1; -; mRNA.
DR EMBL; BC005611; AAH05611.1; -; mRNA.
DR IPI; IPI00277478; -.
DR PIR; S61551; S61551.
DR RefSeq; NP_031721.2; NM_007695.3.
DR UniGene; Mm.38274; -.
DR ProteinModelPortal; Q61362; -.
DR SMR; Q61362; 22-381.
DR STRING; 10090.ENSMUSP00000080717; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PhosphoSite; Q61362; -.
DR PaxDb; Q61362; -.
DR PRIDE; Q61362; -.
DR Ensembl; ENSMUST00000082060; ENSMUSP00000080717; ENSMUSG00000064246.
DR Ensembl; ENSMUST00000153856; ENSMUSP00000117117; ENSMUSG00000064246.
DR GeneID; 12654; -.
DR KEGG; mmu:12654; -.
DR UCSC; uc007crg.2; mouse.
DR CTD; 1116; -.
DR MGI; MGI:1340899; Chi3l1.
DR eggNOG; COG3325; -.
DR GeneTree; ENSGT00550000074323; -.
DR HOVERGEN; HBG011684; -.
DR InParanoid; Q4FJW9; -.
DR KO; K01183; -.
DR NextBio; 281872; -.
DR ArrayExpress; Q61362; -.
DR Bgee; Q61362; -.
DR CleanEx; MM_CHI3L1; -.
DR Genevestigator; Q61362; -.
DR GermOnline; ENSMUSG00000064246; Mus musculus.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0008061; F:chitin binding; ISS:UniProtKB.
DR GO; GO:0004568; F:chitinase activity; IEA:InterPro.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0072606; P:interleukin-8 secretion; IDA:UniProtKB.
DR GO; GO:0030324; P:lung development; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling cascade; IDA:UniProtKB.
DR GO; GO:0070555; P:response to interleukin-1; ISS:UniProtKB.
DR GO; GO:0070741; P:response to interleukin-6; ISS:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; ISS:UniProtKB.
DR Gene3D; 3.20.20.80; -; 2.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR001223; Glyco_hydro18cat.
DR InterPro; IPR013781; Glyco_hydro_catalytic_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; Glyco_hydro_cat; 1.
DR PROSITE; PS01095; CHITINASE_18; FALSE_NEG.
PE 2: Evidence at transcript level;
KW Complete proteome; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1 21 Potential.
FT CHAIN 22 381 Chitinase-3-like protein 1.
FT /FTId=PRO_0000011966.
FT REGION 71 72 Chitooligosaccharide binding (By
FT similarity).
FT REGION 98 101 Chitooligosaccharide binding (By
FT similarity).
FT REGION 205 208 Chitooligosaccharide (By similarity).
FT BINDING 142 142 Chitooligosaccharide (By similarity).
FT BINDING 353 353 Chitooligosaccharide (By similarity).
FT CARBOHYD 60 60 N-linked (GlcNAc...) (By similarity).
FT DISULFID 26 51 By similarity.
FT DISULFID 301 364 By similarity.
FT CONFLICT 331 331 D -> H (in Ref. 1; CAA63603).
SQ SEQUENCE 381 AA; 42979 MW; EF6588C5AE9D4450 CRC64;
MGMRAALTGF AVLMLLQSCS AYKLVCYFTS WSQYREGVGS FLPDAIQPFL CTHIIYSFAN
ISSDNMLSTW EWNDESNYDK LNKLKTRNTN LKTLLSVGGW KFGEKRFSEI ASNTERRTAF
VRSVAPFLRS YGFDGLDLAW LYPRLRDKQY FSTLIKELNA EFTKEVQPGR EKLLLSAALS
AGKVAIDTGY DIAQIAQHLD FINLMTYDFH GVWRQITGHH SPLFQGQKDT RFDRYSNVNY
AVQYMIRLGA QASKLLMGIP TFGKSFTLAS SENQLGAPIS GEGLPGRFTK EAGTLAYYEI
CDFLKGAEVH RLSNEKVPFA TKGNQWVGYE DKESVKNKVG FLKEKKLAGA MVWALDLDDF
QGTCQPKEFF PLTNAIKDAL A
//
