LMA2L_MOUSE
ID LMA2L_MOUSE Reviewed; 347 AA.
AC P59481; Q3TZ91;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=VIP36-like protein;
DE AltName: Full=Lectin mannose-binding 2-like;
DE Short=LMAN2-like protein;
DE Flags: Precursor;
GN Name=Lman2l; Synonyms=Vipl;
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=Inner ear;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory epithelium;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
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: May be involved in the regulation of export from the
CC endoplasmic reticulum of a subset of glycoproteins. May function as a
CC regulator of ERGIC-53 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus
CC membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}. Note=Predominantly found in the endoplasmic reticulum.
CC Partly found in the Golgi. {ECO:0000250}.
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DR EMBL; AK158015; BAE34318.1; -; mRNA.
DR EMBL; BC046969; AAH46969.1; -; mRNA.
DR CCDS; CCDS14878.1; -.
DR RefSeq; NP_001013392.1; NM_001013374.2.
DR RefSeq; NP_001297446.1; NM_001310517.1.
DR AlphaFoldDB; P59481; -.
DR SMR; P59481; -.
DR BioGRID; 229570; 17.
DR STRING; 10090.ENSMUSP00000117200; -.
DR GlyConnect; 2820; 6 N-Linked glycans (1 site).
DR GlyGen; P59481; 1 site, 6 N-linked glycans (1 site).
DR iPTMnet; P59481; -.
DR PhosphoSitePlus; P59481; -.
DR SwissPalm; P59481; -.
DR MaxQB; P59481; -.
DR PaxDb; P59481; -.
DR PeptideAtlas; P59481; -.
DR PRIDE; P59481; -.
DR ProteomicsDB; 290040; -.
DR Antibodypedia; 17473; 65 antibodies from 17 providers.
DR DNASU; 214895; -.
DR Ensembl; ENSMUST00000125304; ENSMUSP00000117200; ENSMUSG00000001143.
DR GeneID; 214895; -.
DR KEGG; mmu:214895; -.
DR UCSC; uc007aqc.1; mouse.
DR CTD; 81562; -.
DR MGI; MGI:2443010; Lman2l.
DR VEuPathDB; HostDB:ENSMUSG00000001143; -.
DR eggNOG; KOG3839; Eukaryota.
DR GeneTree; ENSGT00940000155596; -.
DR InParanoid; P59481; -.
DR OrthoDB; 1377709at2759; -.
DR PhylomeDB; P59481; -.
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; 214895; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Lman2l; mouse.
DR PRO; PR:P59481; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P59481; protein.
DR Bgee; ENSMUSG00000001143; Expressed in otolith organ and 227 other tissues.
DR ExpressionAtlas; P59481; baseline and differential.
DR Genevisible; P59481; MM.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005537; F:mannose binding; IBA:GO_Central.
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:0015031; P:protein transport; ISS:UniProtKB.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR005052; Lectin_leg.
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 Disulfide bond; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Lectin; Membrane; Metal-binding; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..347
FT /note="VIP36-like protein"
FT /id="PRO_0000017669"
FT TOPO_DOM 44..312
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..273
FT /note="L-type lectin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT MOTIF 343..345
FT /note="Endoplasmic reticulum retention signal"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 127
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 160..162
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 187
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 257..259
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 199..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT CONFLICT 16
FT /note="R -> H (in Ref. 1; BAE34318)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 39881 MW; B5DD3287F86E4C23 CRC64;
MAAASRPSWW QRWRRRAWAR DGAKLLLFLL LLGSGPGPRH VRAGQAVEYL KREHSLSKPY
QGVGTSSSSL WNLMGNAMVM TQYIRLTPDM QSKQGALWNR VPCFLKDWEL QVHFKIHGQG
KKNLHGDGLA IWYTKDRMQP GPVFGNMDKF VGLGVFVDTY PNEEKQHERV FPYISAMVNN
GSLSYDHERD GRPTELGGCT AIVRNIRYDT FLVIRYVKRH LTIMMDIDGK HEWRDCIEMP
GVRLPRGYYF GTSSITGDLS DNHDVISLKL FELTGVRTPE EEKLHRDVFL PSVDNLKLPE
MTVPPTPLSG LALFLIVFFS LVFSVFAIVI GIILYNKWQD QSRKRFY
