ID   C3YV77_BRAFL            Unreviewed;       570 AA.
AC   C3YV77;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   02-SEP-2026, entry version 81.
DE   RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
GN   Name=LOC118415987 {ECO:0000313|RefSeq:XP_035676889.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554, ECO:0000313|RefSeq:XP_035676889.1};
RN   [1] {ECO:0000313|Proteomes:UP000001554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|Proteomes:UP000001554};
RX   PubMed=32313176;
RA   Simakov O., Marletaz F., Yue J.X., O'Connell B., Jenkins J., Brandt A.,
RA   Calef R., Tung C.H., Huang T.K., Schmutz J., Satoh N., Yu J.K.,
RA   Putnam N.H., Green R.E., Rokhsar D.S.;
RT   "Deeply conserved synteny resolves early events in vertebrate evolution.";
RL   Nat. Ecol. Evol. 0:0-0(2020).
RN   [2] {ECO:0000313|RefSeq:XP_035676889.1}
RP   IDENTIFICATION.
RC   STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035676889.1};
RC   TISSUE=Testes {ECO:0000313|RefSeq:XP_035676889.1};
RG   RefSeq;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- FUNCTION: Extracts misfolded glycoproteins, but not glycoproteins
CC       undergoing productive folding, from the calnexin cycle. It is directly
CC       involved in endoplasmic reticulum-associated degradation (ERAD) and
CC       targets misfolded glycoproteins for degradation in an N-glycan-
CC       independent manner, probably by forming a complex with SEL1L. It has
CC       low mannosidase activity, catalyzing mannose trimming from Man8GlcNAc2
CC       to Man7GlcNAc2. {ECO:0000256|ARBA:ARBA00060207}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601382-2};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004648}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family.
CC       {ECO:0000256|ARBA:ARBA00007658, ECO:0000256|RuleBase:RU361193}.
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DR   RefSeq; XP_035676889.1; XM_035820996.1.
DR   AlphaFoldDB; C3YV77; -.
DR   STRING; 7739.C3YV77; -.
DR   GeneID; 118415987; -.
DR   eggNOG; KOG2429; Eukaryota.
DR   Proteomes; UP000001554; Chromosome 5.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1904380; P:endoplasmic reticulum mannose trimming; IEA:InterPro.
DR   GO; GO:0036503; P:ERAD pathway; IEA:UniProtKB-ARBA.
DR   GO; GO:1904154; P:positive regulation of retrograde protein transport, ER to cytosol; IEA:UniProtKB-ARBA.
DR   FunFam; 1.50.10.10:FF:000016; alpha-1,2-Mannosidase; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR044674; EDEM1/2/3.
DR   InterPro; IPR001382; Glyco_hydro_47.
DR   InterPro; IPR036026; Seven-hairpin_glycosidases.
DR   PANTHER; PTHR45679:SF5; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR45679; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 2; 1.
DR   Pfam; PF01532; Glyco_hydro_47; 1.
DR   PRINTS; PR00747; GLYHDRLASE47.
DR   SUPFAM; SSF48225; Seven-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR601382-2};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|RuleBase:RU361193};
KW   Hydrolase {ECO:0000256|RuleBase:RU361193};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601382-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001554};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..570
FT                   /note="alpha-1,2-Mannosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5048113701"
FT   ACT_SITE        141
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        390
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        409
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   BINDING         495
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-2"
SQ   SEQUENCE   570 AA;  65264 MW;  E0A37ED33A1CFCC0 CRC64;
     MDWYLWFLCF ISLAVSALDW RDVLTDEDAY NGRKYGHFPD SLRLEMREEA RKMFYFGYDN
     YMRYAFPKDE LNPHACSGRG PDVDNPANIN INDVLGDYSL TLVDTLDTLA IMGNASEFKH
     AVQLVLDNVS FERNTTVQVF EATIRVLGAL LSAHLIITDP LQPFGDLQPD GYENDLLELA
     HDLGTRLLPA FENTPTGLPY PRVNLKHGLP SNPRNDTCTA GAGSLLLEFG MLSRLVGDPT
     YESIARRAVK ALWRYRHAST GLVGNTINIQ TGEWMGPWAG LGAGSDSFYE YLFKGYIMYG
     DPEDLKMFRE IYTSVKENLR KGRDRCNSGQ GNPPMYVNVN IGDGSLASTW VDSLQAFWAG
     LQVLNGDIEE AICHHAVYYA IWRRYGALPE RFNWHLKAPD VRFYPLRPEL VESTYLLYQA
     TKNPFYLHVG TDILKSLEQH AKAKCGYATL HCVINKTQED RMESFFLSET CKYLYLLFDK
     DNHVNQHARR YLFTTEGHLL RVDKTFRRSP WEWEGLSQPK RSKVEEQLSV VDALSMNGTN
     CHKIPIERRY LLPLQSQYQH QLDSFMGLNT
//