Reviewed, UniProtKB/Swiss-Prot Q21059 (NAS34_CAEEL)

Names and origin

Protein names

Recommended name:
    Zinc metalloproteinase nas-34
    EC=3.4.24.21
Alternative name(s):
    Nematode astacin 34
    Defective hatching protein 1

Gene names

Name:	hch-1
Synonyms:	nas-34
ORF Names:	F40E10.1

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	605 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	Probable metalloprotease required for normal hatching and migration of neuroblasts. May act by degrading eggshells proteins at hatching. Ref.1
Catalytic activity	Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Secreted Potential.
Tissue specificity	Expressed in hypodermal cells. First expressed in the dorsal and lateral surface area of the middle and posterior region of embryos. At later stages, it localizes to lateral surface regions, probably corresponding to hypodermal seam cells. In L1 larvae, it is expressed in seam cells and in a few cells anterior to the nerve ring. Ref.1
Developmental stage	In embryos, it is first expressed just before elongation. Ref.1
Sequence similarities	Belongs to the peptidase M12A family. Contains 1 CUB domain. Contains 1 EGF-like domain. Contains 1 TSP type-1 domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	EGF-like domain Signal
Ligand	Metal-binding Zinc
Molecular function	Developmental protein Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion 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 – 19	19	Potential
	Chain	20 – 605	586	Zinc metalloproteinase nas-34		PRO_0000028938
Regions
	Domain	317 – 357	41	EGF-like
	Domain	366 – 469	104	CUB
	Domain	525 – 566	42	TSP type-1
	Compositional bias	173 – 178	6	Poly-Ser
	Compositional bias	479 – 487	9	Poly-Thr
	Compositional bias	498 – 502	5	Poly-Thr
	Compositional bias	505 – 508	4	Poly-Thr
	Compositional bias	511 – 518	8	Poly-Thr
Sites
	Active site	220	1	By similarity
	Metal binding	219	1	Zinc; catalytic By similarity
	Metal binding	223	1	Zinc; catalytic By similarity
	Metal binding	229	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	322	1	N-linked (GlcNAc...) Ref.4
	Disulfide bond	321 ↔ 331		By similarity
	Disulfide bond	325 ↔ 345		By similarity
	Disulfide bond	347 ↔ 356		By similarity
	Disulfide bond	366 ↔ 388		By similarity
	Disulfide bond	415 ↔ 436		By similarity
	Disulfide bond	531 ↔ 551		By similarity
	Disulfide bond	537 ↔ 560		By similarity
	Disulfide bond	541 ↔ 565		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q21059-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E32E67A0F2674809	FASTA	605	66,259
	10 20 30 40 50 60 MVSYWPVLIV LCLLPICHAK SYFADFVNGK GPFKQADALK FMDKMTILNK LQADILGIPQ 70 80 90 100 110 120 PDEFSALDFE DKIESKPDEI PYLFEGDMVL TDEQMDLIIK NVRDQYWARK SSTNEFLYAI 130 140 150 160 170 180 RGKRSMTSFL SERWSFPVPY YIDTSSGVNT NAVLAGVAKW EQETCARFTR LNSYSSSSRQ 190 200 210 220 230 240 NALRFISGNG CYSNIGKVSR FPQDVSIGWG CTSLGTVCHE IGHALGFYHE QARYDRDDYV 250 260 270 280 290 300 SILTQNIQDM YLSQFTKQSA SSMVDYGVGY DYGSVMHYDQ AAFSSTGGNT IATRDPNFQA 310 320 330 340 350 360 TIGQRVAPSF ADVKRINFAY CNSTCSNYLD CQNGGYINPN DCNNCKCPPG FGGQLCDVAG 370 380 390 400 410 420 TNSNGCGAGD ITATSSIQTI SASGALTCNY VIKAPVGAKV YFQMTAATFS RYSPCTTNYL 430 440 450 460 470 480 EINYGRDFSR VGARFCASYP TISLSETNTL VVIYKGVNGA RFSLNYRYDP VTFSTSAPTT 490 500 510 520 530 540 TSTTTTTAPI TVPTVSPTTT TTRQTTTTAR TSTTTTTTQA PPTTTTSTSQ CASWSACSAQ 550 560 570 580 590 600 CGGCGTQSRR CGTYVETVYC NTNPCTGGYC CRPFFYVTSF GTGYCRRPGA DTPAAPQRYV EQRKG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"hch-1, a gene required for normal hatching and normal migration of a neuroblast in C. elegans, encodes a protein related to TOLLOID and BMP-1." Hishida R., Ishihara T., Kondo K., Katsura I. EMBO J. 15:4111-4122(1996) [PubMed: 8861940] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"The astacin protein family in Caenorhabditis elegans." Moehrlen F., Hutter H., Zwilling R. Eur. J. Biochem. 270:4909-4920(2003) [PubMed: 14653817] [Abstract] Cited for: NOMENCLATURE.
[4]	"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-322, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D85744 mRNA. Translation: BAA12861.1. Z69792 Genomic DNA. Translation: CAB61002.1.
PIR	S71630.
RefSeq	NP_510440.1.
UniGene	Cel.23554
3D structure databases
HSSP	HSSP built from PDB template 1IAE based on UniProtKB P07584.
ModBase	Search...
Genome annotation databases
Ensembl	F40E10.1. Caenorhabditis elegans. [Contig view]
GeneID	181564.
KEGG	cel:F40E10.1.
NMPDR	fig|6239.3.peg.25288.
Organism-specific databases
WormBase	WBGene00001828. hch-1.
WormPep	F40E10.1. CE24964. [WorfDB]
Phylogenomic databases
OMA	Q21059. CHEIGHA.
Enzyme and pathway databases
BRENDA	3.4.24.21. 672.
Gene expression databases
ArrayExpress	Q21059.
Family and domain databases
InterPro	IPR000859. CUB. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000742. EGF_3. IPR006025. Pept_M_Zn_BS. IPR006026. Peptidase_M. IPR001506. Peptidase_M12A. IPR017050. Peptidase_M12A_nem. IPR000884. Thrombospondin_1_rpt. [Graphical view]
Gene3D	G3DSA:2.60.120.290. CUB. 1 hit.
Pfam	PF01400. Astacin. 1 hit. PF00431. CUB. 1 hit. [Graphical view]
PIRSF	PIRSF036365. Astacin_nematoda. 1 hit.
PRINTS	PR00480. ASTACIN.
SMART	SM00042. CUB. 1 hit. SM00181. EGF. 1 hit. SM00235. ZnMc. 1 hit. [Graphical view]
PROSITE	PS01180. CUB. 1 hit. PS00022. EGF_1. 1 hit. PS01186. EGF_2. 1 hit. PS50026. EGF_3. 1 hit. PS50092. TSP1. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	914458.

Entry information

Entry name

NAS34_CAEEL

Accession

Primary (citable) accession number: Q21059

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project