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Database: UniProt
Entry: Q61362
LinkDB: Q61362
Original site: Q61362 
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   16-APR-2014, entry version 117.
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   PIR; S61551; S61551.
DR   RefSeq; NP_031721.2; NM_007695.3.
DR   UniGene; Mm.38274; -.
DR   ProteinModelPortal; Q61362; -.
DR   SMR; Q61362; 22-381.
DR   IntAct; Q61362; 1.
DR   MINT; MINT-4090719; -.
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; 12654; -.
DR   MGI; MGI:1340899; Chi3l1.
DR   eggNOG; COG3325; -.
DR   GeneTree; ENSGT00550000074323; -.
DR   HOVERGEN; HBG011684; -.
DR   InParanoid; Q4FJW9; -.
DR   KO; K17523; -.
DR   PhylomeDB; Q61362; -.
DR   TreeFam; TF315610; -.
DR   NextBio; 281872; -.
DR   PRO; PR:Q61362; -.
DR   ArrayExpress; Q61362; -.
DR   Bgee; Q61362; -.
DR   CleanEx; MM_CHI3L1; -.
DR   Genevestigator; Q61362; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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; 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   GO; GO:0034612; P:response to tumor necrosis factor; ISS:UniProtKB.
DR   Gene3D; 3.20.20.80; -; 2.
DR   InterPro; IPR028538; CHI3L1.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR001223; Glyco_hydro18cat.
DR   InterPro; IPR013781; Glyco_hydro_catalytic_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11177:SF81; PTHR11177:SF81; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 2.
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
//
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