HEX_PINMG
ID HEX_PINMG Reviewed; 1135 AA.
AC H2A0L6;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Putative beta-hexosaminidase {ECO:0000250|UniProtKB:Q04786};
DE EC=3.2.1.52 {ECO:0000250|UniProtKB:Q04786};
DE AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000250|UniProtKB:Q04786};
DE AltName: Full=Chitobiase {ECO:0000250|UniProtKB:Q04786};
DE AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000250|UniProtKB:Q04786};
DE Flags: Precursor;
OS Margaritifera margaritifera (Freshwater pearl mussel).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX NCBI_TaxID=102329;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC TISSUE=Mantle;
RX PubMed=21040589; DOI=10.1186/1471-2164-11-613;
RA Joubert C., Piquemal D., Marie B., Manchon L., Pierrat F.,
RA Zanella-Cleon I., Cochennec-Laureau N., Gueguen Y., Montagnani C.;
RT "Transcriptome and proteome analysis of Pinctada margaritifera calcifying
RT mantle and shell: focus on biomineralization.";
RL BMC Genomics 11:613-613(2010).
RN [2]
RP PROTEIN SEQUENCE OF 259-266, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Shell;
RX PubMed=23213212; DOI=10.1073/pnas.1210552109;
RA Marie B., Joubert C., Tayale A., Zanella-Cleon I., Belliard C.,
RA Piquemal D., Cochennec-Laureau N., Marin F., Gueguen Y., Montagnani C.;
RT "Different secretory repertoires control the biomineralization processes of
RT prism and nacre deposition of the pearl oyster shell.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:20986-20991(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000250|UniProtKB:Q04786};
CC -!- PATHWAY: Glycan degradation; chitin degradation.
CC {ECO:0000250|UniProtKB:Q04786}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23213212}.
CC -!- TISSUE SPECIFICITY: Prismatic layer of shell (at protein level).
CC Expressed primarily in the mantle with highest level in the mantle edge
CC and lower level in the mantle pallium. {ECO:0000269|PubMed:23213212}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000255}.
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DR EMBL; HE610383; CCE46157.1; -; mRNA.
DR AlphaFoldDB; H2A0L6; -.
DR SMR; H2A0L6; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR PRIDE; H2A0L6; -.
DR UniPathway; UPA00349; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR004866; CHB/HEX_N_dom.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR PANTHER; PTHR22600; PTHR22600; 1.
DR Pfam; PF03173; CHB_HEX; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SMART; SM01081; CHB_HEX; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1135
FT /note="Putative beta-hexosaminidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000418019"
FT REGION 970..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..1003
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1135 AA; 126661 MW; 208E25A2E93AA61E CRC64;
MKWVKSGVGI LGILLTICHA VTSQGHILDI TDSLKITFKT LSNFGPRAQS IQNVTIENVG
IKDIPDSGWR CYFCHDQLLF PGTFNLARNQ YFLRPILDNY VVLSDGFLLE FIKGCMYRIT
PIPRNAPIKT RDKREFTLLA EQFSVSKYDS FPKWYCETIS GGNTEVGIIR NTENLKYVED
FDSSYNWFRI PHDFRSVPLQ PQDRFSANHK ASSVDECKYK VIPTPVKASV SKVQRNFGTT
VYYGTTDTSI RGREKLFKVA EQLALKHNLG LVEITPGLTV NNGISLVVTG NYVERNIPSP
DEAYSLTVTA DLISIEAPAL PGLINGIETI HSLSAWDMAL PYGGIKDFPR FPFRGIFLDI
ASNFPGYNYI KKFLTVMAQY KLNKLVLPMY NNEGFRLQLN DSPRYEFQAL HMIGGKRCHD
LKEEKCLFSQ LGSGPDSSGG YLTKAQMTDL IKTADLLNIE IIMSMNIGES ARGAIVPLKQ
SPHSRLLYDP DDTDFVDRFY PQKDTSMNPC REETTYFYDH MLKQLKDIYN AASVPLKTIM
IGSKVNFDQV LNSKYCYASN LNSTQRLMAR GNLERNINGF KLNFTKRLVK TAHDNGIKEV
MAIDDVFTTE FDAEGNTPNT VYDTKNSDNS TRFNATVTAV HSRYDTVRDE RLWKRGDRFA
ELGYKVILSP PILDFNYAVE PDPDRPGDYD SVIRNISFSK LFRFVPDSRC CNIPNAIQHD
CALESDCTTA GAKDSYIGTL GKLDTRKLRS LKDWNELLFP RLLIFAERSW HKSSWEDSFG
PHRASVNNIT RQLITNYTVP NWNDINNEES KVLGCISRKE KLRLMHEDGL KPYVEPPGAR
LLGGNTMRIA ASTTEDSFWV QASVNGNPWT DNVKILDVNP TDSVRLRTVH PAKAELRSKE
VKLNLTSLPT PRERFRKIAQ DALSRRIGID IQRARMPPMP VNPAYRPPVP LPSFDPADDR
APDLAAIAAA HPPPLPPGMP SHMMPNMPPP FPPRPPFGPP MLPPGQMRAL GQQAGQALRG
QGTALGPQTG QQPMPAQPRG PLTGQAAGTG VAGQTGQQPS TAGQGTQQGL PGQQRGGVLP
GQWPFFPGMP AAQFPPMFNP QMQRALQMRG QGQIPQRTQG AAAGAGQSRI PQQAG
