LMAN2_MOUSE
ID LMAN2_MOUSE Reviewed; 358 AA.
AC Q9DBH5; Q8BJL4; Q9CXG7;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Vesicular integral-membrane protein VIP36;
DE AltName: Full=Lectin mannose-binding 2;
DE AltName: Full=Vesicular integral-membrane protein 36;
DE Short=VIP36;
DE Flags: Precursor;
GN Name=Lman2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryonic head, Kidney, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type I membrane protein {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK004952; BAB23695.1; -; mRNA.
DR EMBL; AK014384; BAB29313.1; -; mRNA.
DR EMBL; AK083442; BAC38916.1; -; mRNA.
DR EMBL; AK150383; BAE29514.1; -; mRNA.
DR EMBL; AK166953; BAE39136.1; -; mRNA.
DR EMBL; AK169401; BAE41147.1; -; mRNA.
DR EMBL; CH466546; EDL41187.1; -; Genomic_DNA.
DR EMBL; BC049221; AAH49221.1; -; mRNA.
DR EMBL; BC055327; AAH55327.1; -; mRNA.
DR CCDS; CCDS26544.1; -.
DR RefSeq; NP_080104.2; NM_025828.3.
DR AlphaFoldDB; Q9DBH5; -.
DR SMR; Q9DBH5; -.
DR BioGRID; 211791; 5.
DR IntAct; Q9DBH5; 3.
DR MINT; Q9DBH5; -.
DR STRING; 10090.ENSMUSP00000021940; -.
DR GlyConnect; 2819; 5 N-Linked glycans (1 site).
DR GlyGen; Q9DBH5; 1 site, 5 N-linked glycans (1 site).
DR PhosphoSitePlus; Q9DBH5; -.
DR SwissPalm; Q9DBH5; -.
DR CPTAC; non-CPTAC-3656; -.
DR EPD; Q9DBH5; -.
DR jPOST; Q9DBH5; -.
DR MaxQB; Q9DBH5; -.
DR PaxDb; Q9DBH5; -.
DR PeptideAtlas; Q9DBH5; -.
DR PRIDE; Q9DBH5; -.
DR ProteomicsDB; 292269; -.
DR TopDownProteomics; Q9DBH5; -.
DR Antibodypedia; 1119; 159 antibodies from 24 providers.
DR DNASU; 66890; -.
DR Ensembl; ENSMUST00000021940; ENSMUSP00000021940; ENSMUSG00000021484.
DR GeneID; 66890; -.
DR KEGG; mmu:66890; -.
DR UCSC; uc007qqo.1; mouse.
DR CTD; 10960; -.
DR MGI; MGI:1914140; Lman2.
DR VEuPathDB; HostDB:ENSMUSG00000021484; -.
DR eggNOG; KOG3839; Eukaryota.
DR GeneTree; ENSGT00940000158355; -.
DR HOGENOM; CLU_041093_0_0_1; -.
DR InParanoid; Q9DBH5; -.
DR OMA; QGWIFSR; -.
DR OrthoDB; 1377709at2759; -.
DR PhylomeDB; Q9DBH5; -.
DR TreeFam; TF313311; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR BioGRID-ORCS; 66890; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Lman2; mouse.
DR PRO; PR:Q9DBH5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9DBH5; protein.
DR Bgee; ENSMUSG00000021484; Expressed in ectoplacental cone and 260 other tissues.
DR Genevisible; Q9DBH5; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0005537; F:mannose binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; 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; ISO:MGI.
DR CDD; cd06901; lectin_VIP36_VIPL; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR005052; Lectin_leg.
DR InterPro; IPR035664; VIP36_lectin.
DR Pfam; PF03388; Lectin_leg-like; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51328; L_LECTIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Glycoprotein; Golgi apparatus; Lectin; Membrane;
KW Metal-binding; Protein transport; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..46
FT /evidence="ECO:0000255"
FT CHAIN 47..358
FT /note="Vesicular integral-membrane protein VIP36"
FT /id="PRO_0000017667"
FT TOPO_DOM 47..324
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 54..278
FT /note="L-type lectin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 98
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 133
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..168
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
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 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 192
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 262..264
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 204..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT CONFLICT 219
FT /note="V -> L (in Ref. 1; BAB29313)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="L -> V (in Ref. 1; BAB23695)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 40430 MW; 14FB29BF3FDD3B54 CRC64;
MAAEAWLWRW GWGWGQRCPG RPGLPGPGPS PTTFLHLLLL LGPVAADITD GNSEHLKREH
SLIKPYQGVG SSSMPLWDFQ GSTMLTSQYV RLTPDERSKE GSIWNHQPCF LKDWEMHVHF
KVHGTGKKNL HGDGIALWYT RDRLVPGPVF GSKDNFHGLA IFLDTYPNDE TTERVFPYIS
VMVNNGSLSY DHSKDGRWSE LAGCTADFRN RDHDTFLAVR YSRGRLTVMT DLEDKNEWKN
CIDITGVRLP TGYYFGASAG TGDLSDNHDI ISIKLFQLTV ERTPEEESID WTKIEPGVNF
LKSPKDNVDD PTGNFRNGPL TGWRVFLLLL CALLGVVVCA VVGAVVFQKR QERNKRFY
