Q29411 (CH3L1_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chitinase-3-like protein 1

Alternative name(s):
38 kDa heparin-binding glycoprotein
Signal-processing protein
gp38k

Gene names

Name:

CHI3L1

Organism

Sus scrofa (Pig) [Complete proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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. Stimulates migration and adhesion of cultured vascular smooth muscle cells. 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.4
Subunit structure	Monomer By similarity.
Subcellular location	Secreted › extracellular space Ref.1 Ref.3.
Tissue specificity	Detected in smooth muscle cells in atherosclerotic plaques. Detected in regions of vascular occlusion in the aorta. Ref.1 Ref.4
Induction	Up-regulated in cultured aortic smooth muscle cells upon transition to a nodular, multilayered culture. Ref.1
Sequence similarities	Belongs to the glycosyl hydrolase 18 family.
Sequence caution	The sequence AAV30548.1 differs from that shown. Reason: Sequencing errors.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Lectin
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
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.1

Chain

22 – 383

362

Chitinase-3-like protein 1

PRO_0000011967

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...)

Disulfide bond

26 ↔ 51

Disulfide bond

300 ↔ 364

Experimental info

Sequence conflict

69

1

W → L in AAA86482. Ref.1

Sequence conflict

69

1

W → L in CAA87764. Ref.1

Sequence conflict

112

1

K → N in AAA86482. Ref.1

Sequence conflict

112

1

K → N in CAA87764. Ref.1

Sequence conflict

140 – 141

2

LY → IS in AAA86482. Ref.1

Sequence conflict

140 – 141

2

LY → IS in CAA87764. Ref.1

Sequence conflict

162

1

I → V in AAA86482. Ref.1

Sequence conflict

162

1

I → V in CAA87764. Ref.1

Sequence conflict

166 – 167

2

QA → LP in AAA86482. Ref.1

Sequence conflict

166 – 167

2

QA → LP in CAA87764. Ref.1

Sequence conflict

171

1

Q → R in AAA86482. Ref.1

Sequence conflict

171

1

Q → R in CAA87764. Ref.1

Sequence conflict

176

1

A → G in AAA86482. Ref.1

Sequence conflict

176

1

A → G in CAA87764. Ref.1

Sequence conflict

227

1

E → G in AAA86482. Ref.1

Sequence conflict

227

1

E → G in CAA87764. Ref.1

Sequence conflict

278

1

V → A in AAA86482. Ref.1

Sequence conflict

278

1

V → A in CAA87764. Ref.1

Sequence conflict

308 – 313

6

THRFRD → VRRPLG in AAA86482. Ref.1

Sequence conflict

353

1

A → T in AAA86482. Ref.1

Sequence conflict

353

1

A → T in CAA87764. Ref.1

Secondary structure

1

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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 – 178

6

Helix

182 – 188

7

Helix

191 – 195

5

Beta strand

199 – 203

5

Beta strand

213 – 215

3

Helix

237 – 247

11

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 – 303

8

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

Turn

354 – 356

3

Beta strand

359 – 361

3

Beta strand

363 – 367

5

Helix

371 – 381

11

Sequences

	Sequence		Length	Mass (Da)
	Q29411 [UniParc]. Last modified November 8, 2005. Version 2. Checksum: FC6F637E1FD8886E	FASTA	383	42,800
	10 20 30 40 50 60 MGLRVAQTGF VALVLLQSCA AYKLVCYYTS WSQYREGDGS CFPDAIDPFL CTHIIYSFAN 70 80 90 100 110 120 ISNNEIDTWE WNDVTLYDTL NTLKNRNPNL KTLLSVGGWN FGSQRFSKIA SKTQSRRTFI 130 140 150 160 170 180 KSVPPFLRTH GFDGLDLAWL YPGRRDKRHL TTLVKEMKAE FIREAQAGTE QLLLSAAVSA 190 200 210 220 230 240 GKVAIDRGYD IAQISQHLDF ISLLTYDFHG AWRQTTGHHS PLFRGQEDAS SDRFSNADYA 250 260 270 280 290 300 VSYVLRLGAP ANKLVMGIPT FGRSFTLASS KTDVGAPVSG PGIPGRFTKE KGILAYYEIC 310 320 330 340 350 360 DFLQGATTHR FRDQQVPYAT KGNQWVGYDD QESVKNKAKY LKSRQLAGAM VWALDLDDFR 370 380 GNFCGQNLRF PLTSAIKDVL AAA

References

[1]	"Identification of a 38-kDa heparin-binding glycoprotein (gp38k) in differentiating vascular smooth muscle cells as a member of a group of proteins associated with tissue remodeling." Shackelton L.M., Mann D.M., Millis A.J.T. J. Biol. Chem. 270:13076-13083(1995) [PubMed: 7768902] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-36; 92-105; 183-201; 272-278; 292-206 AND 343-362, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Smooth muscle.
[2]	"Crystal structure of a porcine 40 kDa signalling protein at 2.89A resolution." Baskar Singh S., Srivastava D.B., Ethayathulla A.S., Sharma S., Srinivasan A., Singh T.P. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-383, X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 22-383. Tissue: Mammary gland.
[3]	"In vitro expression of a 38,000 dalton heparin-binding glycoprotein by morphologically differentiated smooth muscle cells." Millis A.J.T., Hoyle M., Kent L. J. Cell. Physiol. 127:366-372(1986) [PubMed: 3086326] [Abstract] Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION.
[4]	"gp38k (CHI3L1) is a novel adhesion and migration factor for vascular cells." Nishikawa K.C., Millis A.J.T. Exp. Cell Res. 287:79-87(2003) [PubMed: 12799184] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U19900 mRNA. Translation: AAA86482.1.
Z47803 mRNA. Translation: CAA87764.1.
AY762599 mRNA. Translation: AAV30548.1. Sequence problems.

PIR

S51327.

RefSeq

NP_001001540.1. NM_001001540.1.

UniGene

Ssc.90.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XHG	X-ray	2.90	A	22-381	[»]
1XRV	X-ray	2.10	A	22-381	[»]
1ZB5	X-ray	2.45	A	22-381	[»]
1ZBC	X-ray	2.29	A	22-381	[»]

ProteinModelPortal

Q29411.

SMR

Q29411. Positions 22-383.

ModBase

Search...

Protein family/group databases

CAZy

GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

396865.

KEGG

ssc:396865.

Organism-specific databases

CTD

1116.

Phylogenomic databases

GeneTree

ENSGT00550000074323.

HOVERGEN

HBG011684.

OrthoDB

EOG40K7ZX.

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_PIG

Accession

Primary (citable) accession number: Q29411
Secondary accession number(s): Q5UC99

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	November 8, 2005
Last modified:	November 16, 2011
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program