H2A0L6 (HEX_PINMG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Putative beta-hexosaminidase EC=3.2.1.52 Alternative name(s): Beta-N-acetylhexosaminidase Chitobiase N-acetyl-beta-glucosaminidase
Organism	Pinctada margaritifera (Black-lipped pearl oyster)
Taxonomic identifier	102329 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Mollusca › Bivalvia › Pteriomorphia › Pterioida › Pterioidea › Pteriidae › Pinctada

Protein attributes

Sequence length	1135 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)

Catalytic activity	Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. UniProtKB Q04786
Pathway	Glycan degradation; chitin degradation. UniProtKB Q04786
Subcellular location	Secreted Ref.2.
Tissue specificity	Prismatic layer of shell (at protein level). Ref.2
Sequence similarities	Belongs to the glycosyl hydrolase 20 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: EC polysaccharide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 1135	1112	Putative beta-hexosaminidase		PRO_0000418019
Regions
	Compositional bias	937 – 1004	68	Pro-rich
	Compositional bias	1006 – 1133	128	Gln-rich

Sequences

	Sequence		Length	Mass (Da)
	H2A0L6 [UniParc]. Last modified March 21, 2012. Version 1. Checksum: 208E25A2E93AA61E	FASTA	1,135	126,661
	10 20 30 40 50 60 MKWVKSGVGI LGILLTICHA VTSQGHILDI TDSLKITFKT LSNFGPRAQS IQNVTIENVG 70 80 90 100 110 120 IKDIPDSGWR CYFCHDQLLF PGTFNLARNQ YFLRPILDNY VVLSDGFLLE FIKGCMYRIT 130 140 150 160 170 180 PIPRNAPIKT RDKREFTLLA EQFSVSKYDS FPKWYCETIS GGNTEVGIIR NTENLKYVED 190 200 210 220 230 240 FDSSYNWFRI PHDFRSVPLQ PQDRFSANHK ASSVDECKYK VIPTPVKASV SKVQRNFGTT 250 260 270 280 290 300 VYYGTTDTSI RGREKLFKVA EQLALKHNLG LVEITPGLTV NNGISLVVTG NYVERNIPSP 310 320 330 340 350 360 DEAYSLTVTA DLISIEAPAL PGLINGIETI HSLSAWDMAL PYGGIKDFPR FPFRGIFLDI 370 380 390 400 410 420 ASNFPGYNYI KKFLTVMAQY KLNKLVLPMY NNEGFRLQLN DSPRYEFQAL HMIGGKRCHD 430 440 450 460 470 480 LKEEKCLFSQ LGSGPDSSGG YLTKAQMTDL IKTADLLNIE IIMSMNIGES ARGAIVPLKQ 490 500 510 520 530 540 SPHSRLLYDP DDTDFVDRFY PQKDTSMNPC REETTYFYDH MLKQLKDIYN AASVPLKTIM 550 560 570 580 590 600 IGSKVNFDQV LNSKYCYASN LNSTQRLMAR GNLERNINGF KLNFTKRLVK TAHDNGIKEV 610 620 630 640 650 660 MAIDDVFTTE FDAEGNTPNT VYDTKNSDNS TRFNATVTAV HSRYDTVRDE RLWKRGDRFA 670 680 690 700 710 720 ELGYKVILSP PILDFNYAVE PDPDRPGDYD SVIRNISFSK LFRFVPDSRC CNIPNAIQHD 730 740 750 760 770 780 CALESDCTTA GAKDSYIGTL GKLDTRKLRS LKDWNELLFP RLLIFAERSW HKSSWEDSFG 790 800 810 820 830 840 PHRASVNNIT RQLITNYTVP NWNDINNEES KVLGCISRKE KLRLMHEDGL KPYVEPPGAR 850 860 870 880 890 900 LLGGNTMRIA ASTTEDSFWV QASVNGNPWT DNVKILDVNP TDSVRLRTVH PAKAELRSKE 910 920 930 940 950 960 VKLNLTSLPT PRERFRKIAQ DALSRRIGID IQRARMPPMP VNPAYRPPVP LPSFDPADDR 970 980 990 1000 1010 1020 APDLAAIAAA HPPPLPPGMP SHMMPNMPPP FPPRPPFGPP MLPPGQMRAL GQQAGQALRG 1030 1040 1050 1060 1070 1080 QGTALGPQTG QQPMPAQPRG PLTGQAAGTG VAGQTGQQPS TAGQGTQQGL PGQQRGGVLP 1090 1100 1110 1120 1130 GQWPFFPGMP AAQFPPMFNP QMQRALQMRG QGQIPQRTQG AAAGAGQSRI PQQAG

References

[1]	"Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization." Joubert C., Piquemal D., Marie B., Manchon L., Pierrat F., Zanella-Cleon I., Cochennec-Laureau N., Gueguen Y., Montagnani C. BMC Genomics 11:613-613(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION. Tissue: Mantle.
[2]	"Dissimilar protein secretions control the deposition of nacreous and prismatic shell layers by the pearl oyster mantle epithelia." Marie B., Zanella-cleon I., Jackson D., Marin F. Submitted (OCT-2011) to UniProtKB Cited for: PROTEIN SEQUENCE OF 259-266, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Shell.

Cross-references

Sequence databases
EMBL GenBank DDBJ	HE610383 mRNA. Translation: CCE46157.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00349.
Family and domain databases
Gene3D	2.60.40.290. 1 hit. 3.20.20.80. 1 hit.
InterPro	IPR025705. Beta_hexosaminidase_sua/sub. IPR008965. Carb-bd_dom. IPR012291. CBD_carb-bd_dom. IPR004866. CHB/HEX_N_dom. IPR015883. Glyco_hydro_20_cat-core. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF03173. CHB_HEX. 1 hit. PF00728. Glyco_hydro_20. 1 hit. [Graphical view]
PRINTS	PR00738. GLHYDRLASE20.
SUPFAM	SSF49384. Cellul_bind. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HEX_PINMG

Accession

Primary (citable) accession number: H2A0L6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2012
Last sequence update:	March 21, 2012
Last modified:	May 1, 2013
This is version 10 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)