ID   LMAN2_HUMAN             Reviewed;         356 AA.
AC   Q12907; Q53HH1;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   10-JUN-2026, entry version 197.
DE   RecName: Full=Vesicular integral-membrane protein VIP36;
DE   AltName: Full=Glycoprotein GP36b;
DE   AltName: Full=Lectin mannose-binding 2;
DE   AltName: Full=Vesicular integral-membrane protein 36;
DE            Short=VIP36;
DE   Flags: Precursor;
GN   Name=LMAN2; Synonyms=C5orf8;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hartmann E., Reimann B., Goerlich D., Rapoport T.A., Prehn S.;
RT   "Human GP36b glycoprotein of the endoplasmic reticulum.";
RL   Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Smooth muscle;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10444376; DOI=10.1242/jcs.112.17.2813;
RA   Fullekrug J., Scheiffele P., Simons K.;
RT   "VIP36 localisation to the early secretory pathway.";
RL   J. Cell Sci. 112:2813-2821(1999).
RN   [5]
RP   GLYCOSYLATION AT ASN-183.
RX   PubMed=12754519; DOI=10.1038/nbt827;
RA   Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT   "Identification and quantification of N-linked glycoproteins using
RT   hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL   Nat. Biotechnol. 21:660-666(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-44, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Plays a role as an intracellular lectin in the early
CC       secretory pathway. Interacts with N-acetyl-D-galactosamine and high-
CC       mannose type glycans and may also bind to O-linked glycans. Involved in
CC       the transport and sorting of glycoproteins carrying high mannose-type
CC       glycans (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC       compartment membrane {ECO:0000269|PubMed:10444376}; Single-pass type I
CC       membrane protein {ECO:0000269|PubMed:10444376}. Golgi apparatus
CC       membrane {ECO:0000269|PubMed:10444376}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:10444376}. Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:10444376}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:10444376}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
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DR   EMBL; U10362; AAA19572.1; -; mRNA.
DR   EMBL; AK222609; BAD96329.1; -; mRNA.
DR   EMBL; BC017263; AAH17263.1; -; mRNA.
DR   CCDS; CCDS4417.1; -.
DR   PIR; G01447; G01447.
DR   RefSeq; NP_006807.1; NM_006816.3.
DR   AlphaFoldDB; Q12907; -.
DR   SMR; Q12907; -.
DR   BioGRID; 116159; 173.
DR   FunCoup; Q12907; 2159.
DR   IntAct; Q12907; 90.
DR   MINT; Q12907; -.
DR   NDEx; IQUERY-CP-LMAN2; 4 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000303366; -.
DR   ChEMBL; CHEMBL6066356; -.
DR   TCDB; 9.B.417.1.2; the mcfd2/lman1 complex receptor (mlm-cr) family.
DR   GlyConnect; Q12907; 10 N-Linked glycans (1 site).
DR   GlyCosmos; Q12907; 1 site, 8 glycans.
DR   GlyGen; Q12907; 5 sites, 46 N-linked glycans (1 site), 2 O-linked glycans (2 sites).
DR   iPTMnet; Q12907; -.
DR   PhosphoSitePlus; Q12907; -.
DR   SwissPalm; Q12907; -.
DR   BioMuta; LMAN2; -.
DR   DMDM; 21264108; -.
DR   jPOST; Q12907; -.
DR   MassIVE; Q12907; -.
DR   PaxDb; 9606-ENSP00000303366; -.
DR   PeptideAtlas; Q12907; -.
DR   PRIDE; Q12907; -.
DR   ProteomicsDB; 59020; -.
DR   Pumba; Q12907; -.
DR   TopDownProteomics; Q12907; -.
DR   Antibodypedia; 1119; 160 antibodies from 24 providers.
DR   DNASU; 10960; -.
DR   Ensembl; ENST00000303127.12; ENSP00000303366.7; ENSG00000169223.17.
DR   GeneID; 10960; -.
DR   KEGG; hsa:10960; -.
DR   MANE-Select; ENST00000303127.12; ENSP00000303366.7; NM_006816.3; NP_006807.1.
DR   UCSC; uc003mge.4; human.
DR   AGR; HGNC:16986; -.
DR   ClinPGx; PA25919; -.
DR   CTD; 10960; -.
DR   DisGeNET; 10960; -.
DR   GeneCards; LMAN2; -.
DR   HGNC; HGNC:16986; LMAN2.
DR   HPA; ENSG00000169223; Low tissue specificity.
DR   MIM; 609551; gene.
DR   OpenTargets; ENSG00000169223; -.
DR   VEuPathDB; HostDB:ENSG00000169223; -.
DR   eggNOG; KOG3839; Eukaryota.
DR   GeneTree; ENSGT00940000158355; -.
DR   InParanoid; Q12907; -.
DR   OMA; GCTADIR; -.
DR   OrthoDB; 270293at2759; -.
DR   PAN-GO; Q12907; 6 GO annotations based on evolutionary models.
DR   PhylomeDB; Q12907; -.
DR   PathwayCommons; Q12907; -.
DR   Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR   Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR   SignaLink; Q12907; -.
DR   SIGNOR; Q12907; -.
DR   Agora; ENSG00000169223; -.
DR   BioGRID-ORCS; 10960; 29 hits in 1162 CRISPR screens.
DR   ChiTaRS; LMAN2; human.
DR   GeneWiki; LMAN2; -.
DR   GenomeRNAi; 10960; -.
DR   Pharos; Q12907; Tbio.
DR   PRO; PR:Q12907; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q12907; protein.
DR   Bgee; ENSG00000169223; Expressed in stromal cell of endometrium and 204 other cell types or tissues.
DR   ExpressionAtlas; Q12907; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR   GO; GO:0005537; F:D-mannose binding; IMP:UniProtKB.
DR   GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB.
DR   CDD; cd06901; lectin_VIP36_VIPL; 1.
DR   FunFam; 2.60.120.200:FF:000017; Vesicular integral-membrane protein VIP36; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR051136; Intracellular_Lectin-GPT.
DR   InterPro; IPR005052; Lectin_leg.
DR   InterPro; IPR035664; VIP36_lectin.
DR   PANTHER; PTHR12223:SF36; VESICULAR INTEGRAL-MEMBRANE PROTEIN VIP36; 1.
DR   PANTHER; PTHR12223; VESICULAR MANNOSE-BINDING LECTIN; 1.
DR   Pfam; PF03388; Lectin_leg-like; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51328; L_LECTIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Calcium; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW   Golgi apparatus; Lectin; Membrane; Metal-binding; Protein transport;
KW   Proteomics identification; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..44
FT                   /evidence="ECO:0000255, ECO:0007744|PubMed:25944712"
FT   CHAIN           45..356
FT                   /note="Vesicular integral-membrane protein VIP36"
FT                   /id="PRO_0000017666"
FT   TOPO_DOM        45..322
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        346..356
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          52..276
FT                   /note="L-type lectin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT   BINDING         96
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT   BINDING         131
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT   BINDING         162
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT   BINDING         164..166
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT   BINDING         164
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT   BINDING         166
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT   BINDING         190
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT   BINDING         193
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT   BINDING         260..262
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754519"
FT   DISULFID        202..239
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT   CONFLICT        266
FT                   /note="H -> R (in Ref. 2; BAD96329)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   356 AA;  40229 MW;  196193C8E655141C CRC64;
     MAAEGWIWRW GWGRRCLGRP GLLGPGPGPT TPLFLLLLLG SVTADITDGN SEHLKREHSL
     IKPYQGVGSS SMPLWDFQGS TMLTSQYVRL TPDERSKEGS IWNHQPCFLK DWEMHVHFKV
     HGTGKKNLHG DGIALWYTRD RLVPGPVFGS KDNFHGLAIF LDTYPNDETT ERVFPYISVM
     VNNGSLSYDH SKDGRWTELA GCTADFRNRD HDTFLAVRYS RGRLTVMTDL EDKNEWKNCI
     DITGVRLPTG YYFGASAGTG DLSDNHDIIS MKLFQLMVEH TPDEESIDWT KIEPSVNFLK
     SPKDNVDDPT GNFRSGPLTG WRVFLLLLCA LLGIVVCAVV GAVVFQKRQE RNKRFY
//