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Database: UniProt
Entry: E4YHJ8_OIKDI
LinkDB: E4YHJ8_OIKDI
Original site: E4YHJ8_OIKDI 
ID   E4YHJ8_OIKDI            Unreviewed;      1371 AA.
AC   E4YHJ8;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=beta-mannosidase {ECO:0000256|ARBA:ARBA00012754};
DE            EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE   AltName: Full=Mannanase {ECO:0000256|ARBA:ARBA00033445};
GN   ORFNames=GSOID_T00025015001 {ECO:0000313|EMBL:CBY34972.1};
OS   Oikopleura dioica (Tunicate).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC   Oikopleuridae; Oikopleura.
OX   NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY34972.1};
RN   [1] {ECO:0000313|EMBL:CBY34972.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21097902; DOI=10.1126/science.1194167;
RA   Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA   Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA   Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA   Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA   Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA   Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA   Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA   Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA   Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA   Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA   Roest Crollius H., Wincker P., Chourrout D.;
RT   "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT   pelagic tunicate.";
RL   Science 330:1381-1385(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues
CC         in beta-D-mannosides.; EC=3.2.1.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00000829};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Lysosome
CC       {ECO:0000256|ARBA:ARBA00004371}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00008715}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; FN654569; CBY34972.1; -; Genomic_DNA.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000011014; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR041625; Beta-mannosidase_Ig.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR   PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF03155; Alg6_Alg8; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF17753; Ig_mannosidase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        662..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        713..731
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        751..767
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        779..802
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        822..844
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        865..887
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        893..912
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        933..954
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        960..977
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        989..1006
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1018..1038
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          270..320
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          1300..1363
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   1371 AA;  156712 MW;  5D55572D3BE84331 CRC64;
     MLFLFFFIAF ADCFSISSIN SSNLTFTAEK KLLSCSNLPP VTIYSCFLSK FPSENINNRT
     NDANLQWIGT TKSSFEAEFG QIKPAKFAFL QLENVDTIGE IIWNGAKIGN VRNSFRKYLF
     DVSKTINPTN QLQIDLQAPV IAAKQAAEAQ YPIKQYPECP VSAQTNGQCH VNMLRKPQYS
     FSWDWGPSMP DSGIYDSPKL LVFDSSAIFD AKLQLLSAFS DDLQILQVQV LILHPNSESA
     PAGQAIVNFK PALKFSEDAM KFEKVDENLW KGTMNLQIER EEINWWWIHG MGKQNLYTAT
     ITWDSSSSEI SSIEKQFGFR TAELVQDQLQ DGLSFYFKIN EKPTFMSGSN WIPSSSYIGD
     FSDYYADNLQ SAVDAGIKML RVWGGGIYEQ DAFYSKANEL GLLIWQDFTF ACSTYENDDA
     FLDSVAKEVS DQIWRLSSNP SIVAWAGNNE NEAALATNWW SIPDEEMDFY YKQYSDLYIN
     TAQKTILSEG LTVPFVLSSP SNGKMSENSP NGIAKNPYDP NFGDVHFYDY KSDCTDWTKF
     PKTRFASEFG YQSVAKIYEK CFRMDFWDCT GIFLIFSGFK ILLAQKYDLY HSTDFDVHRN
     WLAITNSKPI SEWYFENTSE WTLDYPPFFA YFEKLLSKYA AKYDPLLVKI QKDPISTDNV
     VFFQKMTVVF TDITVLFGAY FFCKSFNSRK NNLEVAFLIS CNAALFIIDH IHFQYNGLIL
     GLLLCFLAAF MNGKLKTAAL VFSFLLHLKH LFLYVAPFAG IAFLQQINST RIRRGIKTAF
     LKLAFIASIV LFVSAASLFP FLSQLDQLAA RLFPFKRGLT HSYWAGNFWA IYNFVDLLLA
     RLFGMKSALT SGLVGEFSHQ VLPNVPPLAT FSLTFASMIP ALVKIWTKPE RKTWILSFCS
     IALSSFIFGW HVHEKAILLA LLPASGFMLL EKSLFRVFGI LMVAGVSGVL PLIFTEFEQS
     IVIPVYILYL LTTLYIFQPD FQRMNIIEKL YIISSVPLVA FVQIWSKVLL PSLPFLPLLV
     QSLYTALGVL YSFILINLEL FSVDSWGLIS SIESVTSSAD RYFGSAWAAQ RNHHQDGNEQ
     IYGFITQFFG EQPWIKNQSE EAFKNFIYLS QTVQSICTSS QANFYRSRAG LQSTMGALYW
     QLNDVWSTAS WSSLDYSKNW KPLHYQIKKN FNSELTLISK VNDNDQLEVF VISDYVATKG
     RLKVETRSWR SFDTLGEVDY GMFEIKQLEG NLILTKNVGF LLNQMNCPYG KWNECYFTIS
     FITNDGLTLF TTWESPVPIR EIKVFTELDA NVAFFGDCSI DPKDQSLEFE ISSALPQPFV
     WLETRYIGKW SDNFFMMTSS RSFLTFMPAY ELTCEEFMKD AQIYYPSKVH W
//
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