ID LMA2L_HUMAN Reviewed; 348 AA. AC Q9H0V9; B4DSH3; D3DXH6; Q53GV3; Q53S67; Q63HN6; Q8NBQ6; Q9BQ14; DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 10-JUN-2026, entry version 202. 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; ORFNames=PSEC0028, UNQ368/PRO704; 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] (ISOFORM 1), CHARACTERIZATION, STRUCTURE OF RP CARBOHYDRATES, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 344-ARG--ARG-346. RC TISSUE=Liver; RX PubMed=12609988; DOI=10.1074/jbc.m211199200; RA Nufer O., Mitrovic S., Hauri H.-P.; RT "Profile-based data base scanning for animal L-type lectins and RT characterization of VIPL, a novel VIP36-like endoplasmic reticulum RT protein."; RL J. Biol. Chem. 278:15886-15896(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Liver; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Teratocarcinoma; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle, and Uterus; 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 [11] RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP GLYCOSYLATION. RX PubMed=12878160; DOI=10.1016/s0014-4827(03)00161-7; RA Neve E.P.A., Svensson K., Fuxe J., Pettersson R.F.; RT "VIPL, a VIP36-like membrane protein with a putative function in the export RT of glycoproteins from the endoplasmic reticulum."; RL Exp. Cell Res. 288:70-83(2003). RN [12] 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 [13] 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). RN [14] RP INVOLVEMENT IN MRT52, VARIANT MRT52 GLN-53, AND CHARACTERIZATION OF VARIANT RP MRT52 GLN-53. RX PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179; RA Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G., RA Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.; RT "Homozygous missense mutation in the LMAN2L gene segregates with RT intellectual disability in a large consanguineous Pakistani family."; RL J. Med. Genet. 53:138-144(2016). RN [15] RP INVOLVEMENT IN MRD69. RX PubMed=31020005; DOI=10.1002/acn3.727; RA Alkhater R.A., Wang P., Ruggieri A., Israelian L., Walker S., Scherer S.W., RA Smith M.L., Minassian B.A.; RT "Dominant LMAN2L mutation causes intellectual disability with remitting RT epilepsy."; RL Ann. Clin. Transl. Neurol. 6:807-811(2019). 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. {ECO:0000269|PubMed:12878160}. CC -!- INTERACTION: CC Q9H0V9; P42858: HTT; NbExp=3; IntAct=EBI-9091707, EBI-466029; CC Q9H0V9; P21145: MAL; NbExp=3; IntAct=EBI-9091707, EBI-3932027; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type CC I membrane protein. Golgi apparatus membrane; Single-pass type I CC membrane protein. Note=Predominantly found in the endoplasmic CC reticulum. Partly found in the Golgi. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9H0V9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H0V9-2; Sequence=VSP_017940; CC Name=3; CC IsoId=Q9H0V9-3; Sequence=VSP_054439, VSP_054440; CC -!- TISSUE SPECIFICITY: Expressed in numerous tissues. Highest expression CC in skeletal muscle and kidney, intermediate levels in heart, liver and CC placenta, low levels in brain, thymus, spleen, small intestine and CC lung. {ECO:0000269|PubMed:12878160}. CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 52 CC (MRT52) [MIM:616887]: A disorder characterized by significantly below CC average general intellectual functioning associated with impairments in CC adaptive behavior and manifested during the developmental period. MRT52 CC clinical features include global developmental delay, severe CC intellectual disability with poor speech, and mild seizures in early CC childhood. {ECO:0000269|PubMed:26566883}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 69 CC (MRD69) [MIM:617863]: An autosomal dominant disorder characterized by CC developmental delay and variably impaired intellectual development. CC Additional features may include intention tremor in infancy and CC seizures in childhood, with remission of these in adolescence. CC {ECO:0000269|PubMed:31020005}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; AJ549957; CAD71268.1; -; mRNA. DR EMBL; AL136617; CAB66552.1; -; mRNA. DR EMBL; AY358929; AAQ89288.1; -; mRNA. DR EMBL; AK299740; BAG61635.1; -; mRNA. DR EMBL; AK222828; BAD96548.1; -; mRNA. DR EMBL; AK075347; BAC11559.1; -; mRNA. DR EMBL; BX648002; CAH56196.1; -; mRNA. DR EMBL; AC068539; AAX93211.1; -; Genomic_DNA. DR EMBL; CH471207; EAW71341.1; -; Genomic_DNA. DR EMBL; CH471207; EAW71343.1; -; Genomic_DNA. DR EMBL; BC000347; AAH00347.2; -; mRNA. DR EMBL; BC005822; AAH05822.2; -; mRNA. DR EMBL; BC005862; AAH05862.2; -; mRNA. DR EMBL; BC067265; AAH67265.1; -; mRNA. DR CCDS; CCDS2023.1; -. [Q9H0V9-1] DR CCDS; CCDS46365.1; -. [Q9H0V9-2] DR RefSeq; NP_001135764.1; NM_001142292.2. [Q9H0V9-2] DR RefSeq; NP_001309275.1; NM_001322346.2. [Q9H0V9-3] DR RefSeq; NP_001309276.1; NM_001322347.1. DR RefSeq; NP_001309279.1; NM_001322350.1. DR RefSeq; NP_001309280.1; NM_001322351.1. DR RefSeq; NP_001309283.1; NM_001322354.2. [Q9H0V9-3] DR RefSeq; NP_110432.1; NM_030805.4. [Q9H0V9-1] DR AlphaFoldDB; Q9H0V9; -. DR SMR; Q9H0V9; -. DR BioGRID; 123525; 146. DR FunCoup; Q9H0V9; 1838. DR IntAct; Q9H0V9; 110. DR MINT; Q9H0V9; -. DR NDEx; IQUERY-CP-LMAN2L; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000366280; -. DR GlyCosmos; Q9H0V9; 2 sites, 1 glycan. DR GlyGen; Q9H0V9; 3 sites, 9 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q9H0V9; -. DR PhosphoSitePlus; Q9H0V9; -. DR SwissPalm; Q9H0V9; -. DR BioMuta; LMAN2L; -. DR DMDM; 29611906; -. DR jPOST; Q9H0V9; -. DR MassIVE; Q9H0V9; -. DR PaxDb; 9606-ENSP00000366280; -. DR PeptideAtlas; Q9H0V9; -. DR ProteomicsDB; 5026; -. DR ProteomicsDB; 80329; -. [Q9H0V9-1] DR ProteomicsDB; 80330; -. [Q9H0V9-2] DR Pumba; Q9H0V9; -. DR TopDownProteomics; Q9H0V9-1; -. [Q9H0V9-1] DR TopDownProteomics; Q9H0V9-2; -. [Q9H0V9-2] DR Antibodypedia; 17473; 59 antibodies from 18 providers. DR DNASU; 81562; -. DR Ensembl; ENST00000264963.9; ENSP00000264963.4; ENSG00000114988.13. [Q9H0V9-1] DR Ensembl; ENST00000377079.8; ENSP00000366280.4; ENSG00000114988.13. [Q9H0V9-2] DR GeneID; 81562; -. DR KEGG; hsa:81562; -. DR MANE-Select; ENST00000264963.9; ENSP00000264963.4; NM_030805.4; NP_110432.1. DR UCSC; uc002swu.4; human. [Q9H0V9-1] DR AGR; HGNC:19263; -. DR ClinPGx; PA134937652; -. DR CTD; 81562; -. DR DisGeNET; 81562; -. DR GeneCards; LMAN2L; -. DR HGNC; HGNC:19263; LMAN2L. DR HPA; ENSG00000114988; Low tissue specificity. DR MalaCards; LMAN2L; -. DR MIM; 609552; gene. DR MIM; 616887; phenotype. DR MIM; 617863; phenotype. DR OpenTargets; ENSG00000114988; -. DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability. DR VEuPathDB; HostDB:ENSG00000114988; -. DR eggNOG; KOG3839; Eukaryota. DR GeneTree; ENSGT00940000155596; -. DR HOGENOM; CLU_041093_0_0_1; -. DR InParanoid; Q9H0V9; -. DR OMA; GCSIDYR; -. DR OrthoDB; 270293at2759; -. DR PAN-GO; Q9H0V9; 6 GO annotations based on evolutionary models. DR PhylomeDB; Q9H0V9; -. DR PathwayCommons; Q9H0V9; -. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR Reactome; R-HSA-5694530; Cargo concentration in the ER. DR SignaLink; Q9H0V9; -. DR Agora; ENSG00000114988; -. DR BioGRID-ORCS; 81562; 19 hits in 1155 CRISPR screens. DR ChiTaRS; LMAN2L; human. DR GeneWiki; LMAN2L; -. DR GenomeRNAi; 81562; -. DR Pharos; Q9H0V9; Tbio. DR PRO; PR:Q9H0V9; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9H0V9; protein. DR Bgee; ENSG00000114988; Expressed in islet of Langerhans and 190 other cell types or tissues. DR ExpressionAtlas; Q9H0V9; baseline and differential. DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; TAS:UniProtKB. DR GO; GO:0005537; F:D-mannose binding; IBA:GO_Central. 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:0006457; P:protein folding; NAS:UniProtKB. DR GO; GO:0015031; P:protein transport; IMP:UniProtKB. 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 PANTHER; PTHR12223; VESICULAR MANNOSE-BINDING LECTIN; 1. DR PANTHER; PTHR12223:SF20; VIP36-LIKE PROTEIN; 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 Alternative splicing; Disease variant; Disulfide bond; KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; KW Intellectual disability; Lectin; Membrane; Metal-binding; KW Proteomics identification; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..44 FT /evidence="ECO:0000255" FT CHAIN 45..348 FT /note="VIP36-like protein" FT /id="PRO_0000017668" FT TOPO_DOM 45..313 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 314..336 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 337..348 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 49..274 FT /note="L-type lectin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658" FT MOTIF 344..346 FT /note="Endoplasmic reticulum retention signal" FT BINDING 93 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658" FT BINDING 128 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658" FT BINDING 159 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658" FT BINDING 161..163 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658" FT BINDING 161 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658" FT BINDING 163 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658" FT BINDING 188 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658" FT BINDING 191 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658" FT BINDING 258..260 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658" FT CARBOHYD 181 FT /note="N-linked (GlcNAc...) (high mannose) asparagine" FT /evidence="ECO:0000269|PubMed:12878160" FT DISULFID 200..237 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658" FT VAR_SEQ 1..35 FT /note="MAATLGPLGSWQQWRRCLSARDGSRMLLLLLLLGS -> MDKERRICMGMAW FT QSGTQRIGCSQAQKRRYSPGVQ (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054439" FT VAR_SEQ 36..169 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054440" FT VAR_SEQ 169 FT /note="E -> EAQKRRYSPGVQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_017940" FT VARIANT 53 FT /note="R -> Q (in MRT52; no effect on general protein FT glycosylation; dbSNP:rs869320632)" FT /evidence="ECO:0000269|PubMed:26566883" FT /id="VAR_076429" FT MUTAGEN 344..346 FT /note="RKR->SSS: Loss of ER retention." FT /evidence="ECO:0000269|PubMed:12609988" FT CONFLICT 4 FT /note="T -> A (in Ref. 6; BAC11559)" FT /evidence="ECO:0000305" FT CONFLICT 69 FT /note="S -> P (in Ref. 5; BAD96548)" FT /evidence="ECO:0000305" FT CONFLICT 288 FT /note="D -> G (in Ref. 6; BAC11559)" FT /evidence="ECO:0000305" FT CONFLICT 345 FT /note="K -> R (in Ref. 5; BAD96548)" FT /evidence="ECO:0000305" SQ SEQUENCE 348 AA; 39711 MW; F79382E20AE67751 CRC64; MAATLGPLGS WQQWRRCLSA RDGSRMLLLL LLLGSGQGPQ QVGAGQTFEY LKREHSLSKP YQGVGTGSSS LWNLMGNAMV MTQYIRLTPD MQSKQGALWN RVPCFLRDWE LQVHFKIHGQ GKKNLHGDGL AIWYTKDRMQ PGPVFGNMDK FVGLGVFVDT YPNEEKQQER VFPYISAMVN NGSLSYDHER DGRPTELGGC TAIVRNLHYD TFLVIRYVKR HLTIMMDIDG KHEWRDCIEV PGVRLPRGYY FGTSSITGDL SDNHDVISLK LFELTVERTP EEEKLHRDVF LPSVDNMKLP EMTAPLPPLS GLALFLIVFF SLVFSVFAIV IGIILYNKWQ EQSRKRFY //