P30922 (CH3L1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chitinase-3-like protein 1

Alternative name(s):
39 kDa whey protein
Cartilage glycoprotein 39
Short name=CGP-39
Short name=GP-39
Chitinase-like protein 1
Short name=CLP-1
SPC-40
Signal-processing protein

Gene names

Name:

CHI3L1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	383 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Carbohydrate-binding lectin with a preference for chitin. May play a role in defense against pathogens, or in tissue remodeling. May play an important role in the capacity of cells to respond to and cope with changes in their environment By similarity. Ref.5
Subunit structure	Monomer.
Subcellular location	Secreted › extracellular space.
Tissue specificity	Mammary secretions collected during the non-lactating period.
Post-translational modification	Glycosylated. Ref.5
Sequence similarities	Belongs to the glycosyl hydrolase 18 family.
Sequence caution	The sequence AAX46682.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Lectin
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chitin catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro chitinase activity Inferred from electronic annotation. Source: InterPro sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Ref.3

Chain

22 – 383

362

Chitinase-3-like protein 1

PRO_0000042787

Regions

Region

70 – 71

2

Chitooligosaccharide binding By similarity

Region

97 – 100

4

Chitooligosaccharide binding By similarity

Region

204 – 207

4

Chitooligosaccharide By similarity

Sites

Binding site

141

1

Chitooligosaccharide By similarity

Binding site

263

1

Chitooligosaccharide By similarity

Binding site

352

1

Chitooligosaccharide By similarity

Amino acid modifications

Glycosylation

60

1

N-linked (GlcNAc...) Ref.5

Glycosylation

367

1

N-linked (GlcNAc...) Potential

Disulfide bond

26 ↔ 51

Ref.5

Disulfide bond

300 ↔ 364

Ref.5

Experimental info

Sequence conflict

25

1

I → V in AAB64304. Ref.4

Sequence conflict

104

1

Q → E in AAP41220. Ref.2

Sequence conflict

164

1

E → G in AAB64304. Ref.4

Sequence conflict

179

1

P → T in AAP41220. Ref.2

Sequence conflict

211

1

A → G in AAP41220. Ref.2

Sequence conflict

214

1

Q → G in AAP41220. Ref.2

Sequence conflict

226 – 232

7

QEDASSD → NSDGSS in AAP41220. Ref.2

Sequence conflict

271 – 273

3

KTD → STR in AAP41220. Ref.2

Sequence conflict

307

1

T → I in AAX46682. Ref.1

Sequence conflict

369

1

T → A in AAX46682. Ref.1

Sequence conflict

382

1

R → E in AAX46682. Ref.1

Secondary structure

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383

Helix Strand Turn

Details...

Beta strand

23 – 29

7

Helix

30 – 34

5

Helix

37 – 39

3

Helix

43 – 45

3

Turn

48 – 50

3

Beta strand

52 – 62

11

Beta strand

65 – 67

3

Helix

73 – 81

9

Helix

82 – 85

4

Beta strand

91 – 97

7

Helix

103 – 111

9

Helix

113 – 130

18

Beta strand

133 – 138

6

Turn

144 – 146

3

Helix

147 – 164

18

Helix

165 – 167

3

Beta strand

173 – 179

7

Helix

182 – 188

7

Helix

191 – 195

5

Beta strand

199 – 204

6

Beta strand

211 – 215

5

Turn

230 – 234

5

Helix

237 – 246

10

Helix

251 – 253

3

Beta strand

254 – 270

17

Beta strand

277 – 281

5

Turn

286 – 288

3

Beta strand

293 – 295

3

Helix

296 – 302

7

Turn

303 – 305

3

Beta strand

307 – 311

5

Turn

312 – 315

4

Beta strand

316 – 321

6

Beta strand

324 – 327

4

Helix

331 – 343

13

Beta strand

347 – 352

6

Helix

354 – 356

3

Beta strand

359 – 361

3

Beta strand

363 – 366

4

Helix

371 – 382

12

Sequences

	Sequence		Length	Mass (Da)
	P30922 [UniParc]. Last modified November 8, 2005. Version 3. Checksum: 391561804C371A10	FASTA	383	43,032
	10 20 30 40 50 60 MGLRAAHTGF VVLVLLQSCA AYKLICYYTS WSQYREGDGS CFPDAIDPFL CTHVIYSFAN 70 80 90 100 110 120 ISNNEIDTWE WNDVTLYDTL NTLKNRNPNL KTLLSVGGWN FGSQRFSKIA SKTQSRRTFI 130 140 150 160 170 180 KSVPPFLRTH GFDGLDLAWL YPGWRDKRHL TTLVKEMKAE FVREAQAGTE QLLLSAAVPA 190 200 210 220 230 240 GKIAIDRGYD IAQISRHLDF ISLLTYDFHG AWRQTVGHHS PLFRGQEDAS SDRFSNADYA 250 260 270 280 290 300 VSYMLRLGAP ANKLVMGIPT FGRSYTLASS KTDVGAPISG PGIPGQFTKE KGILAYYEIC 310 320 330 340 350 360 DFLHGATTHR FRDQQVPYAT KGNQWVAYDD QESVKNKARY LKNRQLAGAM VWALDLDDFR 370 380 GTFCGQNLTF PLTSAIKDVL ARV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	"Signal processing protein from bovine mammary gland." Srinivasan A., Kumar J., Singh T.P. Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-383. Tissue: Mammary gland.
[3]	"Isolation and characterization of a novel 39 kilodalton whey protein from bovine mammary secretions collected during the nonlactating period." Rejman J.J., Hurley W.L. Biochem. Biophys. Res. Commun. 150:329-334(1988) [PubMed: 3122754] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-57.
[4]	"Expression of chitinase-like protein 1 (CLP-1) in bovine chondrocytes." Recklies A.D., White C. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-356.
[5]	"Structure of a bovine secretory signalling glycoprotein (SPC-40) at 2.1 Angstrom resolution." Kumar J., Ethayathulla A.S., Srivastava D.B., Sharma S., Singh S.B., Srinivasan A., Yadav M.P., Singh T.P. Acta Crystallogr. D 62:953-963(2006) [PubMed: 16929095] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-383, GLYCOSYLATION AT ASN-60, DISULFIDE BONDS, FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BT021835 mRNA. Translation: AAX46682.1. Different initiation.
AY291312 mRNA. Translation: AAP41220.2.
AF011373 mRNA. Translation: AAB64304.1.

IPI

IPI00717764.

PIR

A27682.

RefSeq

NP_001073688.1. NM_001080219.1.

UniGene

Bt.60417.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OWQ	X-ray	2.00	A	22-383	[»]
2ESC	X-ray	2.10	A	22-383	[»]

ProteinModelPortal

P30922.

SMR

P30922. Positions 22-383.

ModBase

Search...

Protein family/group databases

CAZy

GH18. Glycoside Hydrolase Family 18.

Proteomic databases

PRIDE

P30922.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

286869.

KEGG

bta:286869.

Organism-specific databases

CTD

1116.

Phylogenomic databases

eggNOG

maNOG04955.

GeneTree

ENSGT00550000074323.

HOVERGEN

HBG011684.

InParanoid

P30922.

OrthoDB

EOG40K7ZX.

PhylomeDB

P30922.

Family and domain databases

InterPro

IPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.

KO

K01183.

Pfam

PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]

SMART

SM00636. Glyco_18. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS01095. CHITINASE_18. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CH3L1_BOVIN

Accession

Primary (citable) accession number: P30922
Secondary accession number(s): O18949, Q58CW2, Q7YSE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	November 8, 2005
Last modified:	November 16, 2011
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program