LMA2L_HUMAN
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 03-AUG-2022, entry version 184.
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).
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.
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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_001142292.1. [Q9H0V9-2]
DR RefSeq; NP_001309275.1; NM_001322346.1. [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_001322354.1. [Q9H0V9-3]
DR RefSeq; NP_110432.1; NM_030805.3. [Q9H0V9-1]
DR AlphaFoldDB; Q9H0V9; -.
DR SMR; Q9H0V9; -.
DR BioGRID; 123525; 125.
DR IntAct; Q9H0V9; 41.
DR STRING; 9606.ENSP00000366280; -.
DR GlyGen; Q9H0V9; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H0V9; -.
DR PhosphoSitePlus; Q9H0V9; -.
DR SwissPalm; Q9H0V9; -.
DR BioMuta; LMAN2L; -.
DR DMDM; 29611906; -.
DR EPD; Q9H0V9; -.
DR jPOST; Q9H0V9; -.
DR MassIVE; Q9H0V9; -.
DR MaxQB; Q9H0V9; -.
DR PaxDb; Q9H0V9; -.
DR PeptideAtlas; Q9H0V9; -.
DR PRIDE; Q9H0V9; -.
DR ProteomicsDB; 5026; -.
DR ProteomicsDB; 80329; -. [Q9H0V9-1]
DR ProteomicsDB; 80330; -. [Q9H0V9-2]
DR TopDownProteomics; Q9H0V9-1; -. [Q9H0V9-1]
DR TopDownProteomics; Q9H0V9-2; -. [Q9H0V9-2]
DR Antibodypedia; 17473; 65 antibodies from 17 providers.
DR DNASU; 81562; -.
DR Ensembl; ENST00000264963.9; ENSP00000264963.4; ENSG00000114988.12. [Q9H0V9-1]
DR Ensembl; ENST00000377079.8; ENSP00000366280.4; ENSG00000114988.12. [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 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 neXtProt; NX_Q9H0V9; -.
DR OpenTargets; ENSG00000114988; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA134937652; -.
DR VEuPathDB; HostDB:ENSG00000114988; -.
DR eggNOG; KOG3839; Eukaryota.
DR GeneTree; ENSGT00940000155596; -.
DR HOGENOM; CLU_041093_0_0_1; -.
DR InParanoid; Q9H0V9; -.
DR OMA; MGWATGR; -.
DR OrthoDB; 1377709at2759; -.
DR PhylomeDB; Q9H0V9; -.
DR TreeFam; TF313311; -.
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 BioGRID-ORCS; 81562; 19 hits in 1077 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 188 other tissues.
DR ExpressionAtlas; Q9H0V9; baseline and differential.
DR Genevisible; Q9H0V9; HS.
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:0016021; C:integral component of membrane; TAS:UniProtKB.
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:0006457; P:protein folding; NAS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IMP: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 Alternative splicing; Disease variant; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Intellectual disability; Lectin; Membrane; Metal-binding;
KW Reference proteome; Signal; Transmembrane; 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
