MESD_HUMAN
ID MESD_HUMAN Reviewed; 234 AA.
AC Q14696; B4DW84; D3DW96; Q969U1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=LRP chaperone MESD {ECO:0000305};
DE AltName: Full=LDLR chaperone MESD;
DE AltName: Full=Mesoderm development LRP chaperone MESD {ECO:0000312|HGNC:HGNC:13520};
DE AltName: Full=Mesoderm development candidate 2;
DE AltName: Full=Mesoderm development protein;
DE AltName: Full=Renal carcinoma antigen NY-REN-61;
DE Flags: Precursor;
GN Name=MESD {ECO:0000312|HGNC:HGNC:13520}; Synonyms=KIAA0081, MESDC2, MESDM;
GN ORFNames=UNQ1911/PRO4369;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
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 2).
RC TISSUE=Synovium;
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 GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Skin;
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 [8]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15014448; DOI=10.1038/sj.emboj.7600132;
RA Culi J., Springer T.A., Mann R.S.;
RT "Boca-dependent maturation of beta-propeller/EGF modules in low-density
RT lipoprotein receptor proteins.";
RL EMBO J. 23:1372-1380(2004).
RN [10]
RP FUNCTION, INTERACTION WITH LRP5 AND LRP6, AND SUBCELLULAR LOCATION.
RX PubMed=17488095; DOI=10.1021/bi700049g;
RA Koduri V., Blacklow S.C.;
RT "Requirement for natively unstructured regions of mesoderm development
RT candidate 2 in promoting low-density lipoprotein receptor-related protein 6
RT maturation.";
RL Biochemistry 46:6570-6577(2007).
RN [11]
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 [12]
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 [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 OI20, AND VARIANT OI20 226-ARG--LEU-234.
RX PubMed=31564437; DOI=10.1016/j.ajhg.2019.08.008;
RA Moosa S., Yamamoto G.L., Garbes L., Keupp K., Beleza-Meireles A.,
RA Moreno C.A., Valadares E.R., de Sousa S.B., Maia S., Saraiva J.,
RA Honjo R.S., Kim C.A., Cabral de Menezes H., Lausch E., Lorini P.V.,
RA Lamounier A. Jr., Carniero T.C.B., Giunta C., Rohrbach M., Janner M.,
RA Semler O., Beleggia F., Li Y., Yigit G., Reintjes N., Altmueller J.,
RA Nuernberg P., Cavalcanti D.P., Zabel B., Warman M.L., Bertola D.R.,
RA Wollnik B., Netzer C.;
RT "Autosomal-recessive mutations in MESD cause osteogenesis imperfecta.";
RL Am. J. Hum. Genet. 105:836-843(2019).
CC -!- FUNCTION: Chaperone specifically assisting the folding of beta-
CC propeller/EGF modules within the family of low-density lipoprotein
CC receptors (LDLRs) (PubMed:15014448). Acts as a modulator of the Wnt
CC pathway through chaperoning the coreceptors of the canonical Wnt
CC pathway, LRP5 and LRP6, to the plasma membrane (PubMed:17488095).
CC Essential for specification of embryonic polarity and mesoderm
CC induction. Plays an essential role in neuromuscular junction (NMJ)
CC formation by promoting cell-surface expression of LRP4 (By similarity).
CC May regulate phagocytosis of apoptotic retinal pigment epithelium (RPE)
CC cells (By similarity). {ECO:0000250|UniProtKB:Q9ERE7,
CC ECO:0000269|PubMed:15014448, ECO:0000269|PubMed:17488095}.
CC -!- SUBUNIT: Monomer. Interacts with LRP5; the interaction prevents LRP5
CC from forming aggregates and chaperones LRP6 to the plasma membrane
CC (PubMed:17488095). Interacts with LRP6; the interaction prevents LRP6
CC from forming aggregates and chaperones LRP6 to the plasma membrane
CC (PubMed:17488095). Interacts with LRP4; the interaction promotes
CC glycosylation of LRP4 and its cell-surface expression (By similarity).
CC {ECO:0000250|UniProtKB:Q9ERE7, ECO:0000269|PubMed:17488095}.
CC -!- INTERACTION:
CC Q14696; Q9H221: ABCG8; NbExp=3; IntAct=EBI-6165891, EBI-3908684;
CC Q14696; Q9NX38: ABITRAM; NbExp=3; IntAct=EBI-6165891, EBI-9105722;
CC Q14696; Q8N6N7: ACBD7; NbExp=3; IntAct=EBI-6165891, EBI-18657673;
CC Q14696; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-6165891, EBI-18899653;
CC Q14696; Q53H80: AKIRIN2; NbExp=3; IntAct=EBI-6165891, EBI-742928;
CC Q14696; Q5T1N1-2: AKNAD1; NbExp=3; IntAct=EBI-6165891, EBI-18898519;
CC Q14696; P31749: AKT1; NbExp=3; IntAct=EBI-6165891, EBI-296087;
CC Q14696; Q9UBL3: ASH2L; NbExp=3; IntAct=EBI-6165891, EBI-540797;
CC Q14696; Q96A05: ATP6V1E2; NbExp=3; IntAct=EBI-6165891, EBI-8650380;
CC Q14696; P46379-2: BAG6; NbExp=3; IntAct=EBI-6165891, EBI-10988864;
CC Q14696; Q96FH0: BORCS8; NbExp=3; IntAct=EBI-6165891, EBI-744076;
CC Q14696; Q9HAS0: C17orf75; NbExp=3; IntAct=EBI-6165891, EBI-12954949;
CC Q14696; Q8IYK2: CCDC105; NbExp=3; IntAct=EBI-6165891, EBI-10818513;
CC Q14696; Q86X02: CDR2L; NbExp=3; IntAct=EBI-6165891, EBI-11063830;
CC Q14696; Q86UT8: CENATAC; NbExp=3; IntAct=EBI-6165891, EBI-11028020;
CC Q14696; Q9H3R5: CENPH; NbExp=3; IntAct=EBI-6165891, EBI-1003700;
CC Q14696; Q96BP2: CHCHD1; NbExp=3; IntAct=EBI-6165891, EBI-5454898;
CC Q14696; Q92989: CLP1; NbExp=3; IntAct=EBI-6165891, EBI-2559831;
CC Q14696; Q92600-3: CNOT9; NbExp=3; IntAct=EBI-6165891, EBI-12907584;
CC Q14696; Q03692: COL10A1; NbExp=3; IntAct=EBI-6165891, EBI-2528309;
CC Q14696; P08123: COL1A2; NbExp=3; IntAct=EBI-6165891, EBI-983038;
CC Q14696; Q96I36: COX14; NbExp=3; IntAct=EBI-6165891, EBI-6570698;
CC Q14696; P20674: COX5A; NbExp=3; IntAct=EBI-6165891, EBI-715032;
CC Q14696; Q9NTM9: CUTC; NbExp=3; IntAct=EBI-6165891, EBI-714918;
CC Q14696; Q9HBI6: CYP4F11; NbExp=3; IntAct=EBI-6165891, EBI-3924028;
CC Q14696; P26196: DDX6; NbExp=3; IntAct=EBI-6165891, EBI-351257;
CC Q14696; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-6165891, EBI-744099;
CC Q14696; Q8NE31: FAM13C; NbExp=3; IntAct=EBI-6165891, EBI-751248;
CC Q14696; Q8WUF8: FAM172A; NbExp=3; IntAct=EBI-6165891, EBI-2556079;
CC Q14696; O95363: FARS2; NbExp=3; IntAct=EBI-6165891, EBI-2513774;
CC Q14696; P12319: FCER1A; NbExp=3; IntAct=EBI-6165891, EBI-3908910;
CC Q14696; P55040: GEM; NbExp=3; IntAct=EBI-6165891, EBI-744104;
CC Q14696; Q7Z5G4: GOLGA7; NbExp=3; IntAct=EBI-6165891, EBI-4403685;
CC Q14696; Q92917: GPKOW; NbExp=3; IntAct=EBI-6165891, EBI-746309;
CC Q14696; Q969Y2: GTPBP3; NbExp=3; IntAct=EBI-6165891, EBI-740290;
CC Q14696; P0C5Z0: H2AB3; NbExp=3; IntAct=EBI-6165891, EBI-13318575;
CC Q14696; C9JCN9: HSBP1L1; NbExp=3; IntAct=EBI-6165891, EBI-2685549;
CC Q14696; P05019-2: IGF1; NbExp=3; IntAct=EBI-6165891, EBI-12837046;
CC Q14696; O14901: KLF11; NbExp=3; IntAct=EBI-6165891, EBI-948266;
CC Q14696; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-6165891, EBI-11962058;
CC Q14696; Q9Y6Y9: LY96; NbExp=3; IntAct=EBI-6165891, EBI-1539247;
CC Q14696; O15481: MAGEB4; NbExp=3; IntAct=EBI-6165891, EBI-751857;
CC Q14696; Q9GZQ8: MAP1LC3B; NbExp=3; IntAct=EBI-6165891, EBI-373144;
CC Q14696; Q9NXL9-3: MCM9; NbExp=3; IntAct=EBI-6165891, EBI-18899369;
CC Q14696; P08582-2: MELTF; NbExp=3; IntAct=EBI-6165891, EBI-10195914;
CC Q14696; Q9HBH9-2: MKNK2; NbExp=3; IntAct=EBI-6165891, EBI-14141314;
CC Q14696; Q6IN84: MRM1; NbExp=3; IntAct=EBI-6165891, EBI-5454865;
CC Q14696; Q9H7Z3: NRDE2; NbExp=3; IntAct=EBI-6165891, EBI-1042642;
CC Q14696; Q6P1K2: PMF1; NbExp=3; IntAct=EBI-6165891, EBI-713832;
CC Q14696; P47897: QARS1; NbExp=3; IntAct=EBI-6165891, EBI-347462;
CC Q14696; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-6165891, EBI-1504830;
CC Q14696; A0A0B4J2F2: SIK1B; NbExp=3; IntAct=EBI-6165891, EBI-22345187;
CC Q14696; Q12824-2: SMARCB1; NbExp=3; IntAct=EBI-6165891, EBI-358436;
CC Q14696; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-6165891, EBI-12090309;
CC Q14696; A0A1B0GUV7: TEX48; NbExp=3; IntAct=EBI-6165891, EBI-18583507;
CC Q14696; P07951-2: TPM2; NbExp=3; IntAct=EBI-6165891, EBI-10977815;
CC Q14696; Q9BQ50: TREX2; NbExp=3; IntAct=EBI-6165891, EBI-22217464;
CC Q14696; Q8IZ69: TRMT2A; NbExp=3; IntAct=EBI-6165891, EBI-2515774;
CC Q14696; A0A0B4J1Y2: TTC21A; NbExp=3; IntAct=EBI-6165891, EBI-10220701;
CC Q14696; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-6165891, EBI-9090990;
CC Q14696; P19971: TYMP; NbExp=3; IntAct=EBI-6165891, EBI-2556931;
CC Q14696; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-6165891, EBI-741480;
CC Q14696; Q6ZR52-3: ZNF493; NbExp=3; IntAct=EBI-6165891, EBI-12856290;
CC Q14696; Q17R98: ZNF827; NbExp=3; IntAct=EBI-6165891, EBI-5564776;
CC Q14696; Q08AG5: ZNF844; NbExp=3; IntAct=EBI-6165891, EBI-10225757;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:15014448, ECO:0000269|PubMed:17488095}.
CC Note=Released from apoptotic cells and shed photoreceptor outer
CC segments. {ECO:0000250|UniProtKB:Q9ERE7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14696-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14696-2; Sequence=VSP_055492, VSP_055493;
CC -!- DOMAIN: The chaperone domain provides a folding template for proper
CC folding of the beta-propeller (BP) domains of LRP5/6.
CC {ECO:0000250|UniProtKB:Q9ERE7}.
CC -!- DOMAIN: The escort domain ensures LRP5/6 safe-trafficking from the ER
CC to the Golgi by preventing premature ligand-binding.
CC {ECO:0000250|UniProtKB:Q9ERE7}.
CC -!- DISEASE: Osteogenesis imperfecta 20 (OI20) [MIM:618644]: An autosomal
CC recessive form of osteogenesis imperfecta, a connective tissue disorder
CC characterized by low bone mass, bone fragility and susceptibility to
CC fractures after minimal trauma. Disease severity ranges from very mild
CC forms without fractures to intrauterine fractures and perinatal
CC lethality. Extraskeletal manifestations, which affect a variable number
CC of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI20 is a progressive deforming form characterized by
CC osteopenia, skeletal deformity, healed fractures, and newly-acquired
CC fractures. Death due to respiratory failure can occur in some patients.
CC {ECO:0000269|PubMed:31564437}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the MESD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07640.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D42039; BAA07640.2; ALT_INIT; mRNA.
DR EMBL; AY359110; AAQ89468.1; -; mRNA.
DR EMBL; AK301416; BAG62946.1; -; mRNA.
DR EMBL; AC027808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471136; EAW99109.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99110.1; -; Genomic_DNA.
DR EMBL; BC009210; AAH09210.1; -; mRNA.
DR EMBL; BC012746; AAH12746.1; -; mRNA.
DR CCDS; CCDS32308.1; -. [Q14696-1]
DR RefSeq; NP_055969.1; NM_015154.2. [Q14696-1]
DR AlphaFoldDB; Q14696; -.
DR SMR; Q14696; -.
DR BioGRID; 116794; 145.
DR IntAct; Q14696; 91.
DR MINT; Q14696; -.
DR STRING; 9606.ENSP00000261758; -.
DR GlyGen; Q14696; 1 site.
DR iPTMnet; Q14696; -.
DR PhosphoSitePlus; Q14696; -.
DR BioMuta; MESD; -.
DR DMDM; 24418861; -.
DR OGP; Q14696; -.
DR EPD; Q14696; -.
DR jPOST; Q14696; -.
DR MassIVE; Q14696; -.
DR MaxQB; Q14696; -.
DR PaxDb; Q14696; -.
DR PeptideAtlas; Q14696; -.
DR PRIDE; Q14696; -.
DR ProteomicsDB; 5321; -.
DR ProteomicsDB; 60136; -. [Q14696-1]
DR TopDownProteomics; Q14696-1; -. [Q14696-1]
DR ABCD; Q14696; 1 sequenced antibody.
DR Antibodypedia; 27911; 183 antibodies from 34 providers.
DR DNASU; 23184; -.
DR Ensembl; ENST00000261758.6; ENSP00000261758.4; ENSG00000117899.11. [Q14696-1]
DR Ensembl; ENST00000422879.3; ENSP00000403839.3; ENSG00000117899.11. [Q14696-2]
DR Ensembl; ENST00000561312.5; ENSP00000453430.1; ENSG00000117899.11. [Q14696-1]
DR Ensembl; ENST00000619987.4; ENSP00000482455.1; ENSG00000117899.11. [Q14696-1]
DR GeneID; 23184; -.
DR KEGG; hsa:23184; -.
DR MANE-Select; ENST00000261758.6; ENSP00000261758.4; NM_015154.3; NP_055969.1.
DR UCSC; uc002bfy.2; human. [Q14696-1]
DR CTD; 23184; -.
DR DisGeNET; 23184; -.
DR GeneCards; MESD; -.
DR HGNC; HGNC:13520; MESD.
DR HPA; ENSG00000117899; Low tissue specificity.
DR MalaCards; MESD; -.
DR MIM; 607783; gene.
DR MIM; 618644; phenotype.
DR neXtProt; NX_Q14696; -.
DR OpenTargets; ENSG00000117899; -.
DR Orphanet; 216804; Osteogenesis imperfecta type 2.
DR PharmGKB; PA30761; -.
DR VEuPathDB; HostDB:ENSG00000117899; -.
DR eggNOG; KOG4357; Eukaryota.
DR GeneTree; ENSGT00390000000993; -.
DR HOGENOM; CLU_111621_0_0_1; -.
DR InParanoid; Q14696; -.
DR OMA; NRATKQR; -.
DR OrthoDB; 1590303at2759; -.
DR PhylomeDB; Q14696; -.
DR TreeFam; TF315614; -.
DR PathwayCommons; Q14696; -.
DR SignaLink; Q14696; -.
DR BioGRID-ORCS; 23184; 72 hits in 1074 CRISPR screens.
DR ChiTaRS; MESDC2; human.
DR GeneWiki; MESDC2; -.
DR GenomeRNAi; 23184; -.
DR Pharos; Q14696; Tbio.
DR PRO; PR:Q14696; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q14696; protein.
DR Bgee; ENSG00000117899; Expressed in epithelial cell of pancreas and 194 other tissues.
DR ExpressionAtlas; Q14696; baseline and differential.
DR Genevisible; Q14696; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IBA:GO_Central.
DR GO; GO:0007498; P:mesoderm development; NAS:UniProtKB.
DR GO; GO:0001503; P:ossification; IMP:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
DR GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IMP:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR019330; MESD.
DR PANTHER; PTHR17600; PTHR17600; 1.
DR Pfam; PF10185; Mesd; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Disease variant; Endoplasmic reticulum;
KW Glycoprotein; Osteogenesis imperfecta; Reference proteome; Signal;
KW Wnt signaling pathway.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..234
FT /note="LRP chaperone MESD"
FT /id="PRO_0000096443"
FT REGION 1..164
FT /note="Chaperone domain"
FT /evidence="ECO:0000250|UniProtKB:Q9ERE7"
FT REGION 31..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..204
FT /note="Escort domain"
FT /evidence="ECO:0000250|UniProtKB:Q9ERE7"
FT REGION 187..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 231..234
FT /note="Prevents secretion from ER"
FT COMPBIAS 45..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 72..138
FT /note="KDDDIEEGDLPEHKRPSAPVDFSKIDPSKPESILKMTKKGKTLMMFVTVSGS
FT PTEKETEEITSLWQG -> TPEPLPVLPEVPSTCACLSSASLIWTCFSHLSPHALVKRV
FT WPPAKQGLGGKESPASAWLPHRGGELK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055492"
FT VAR_SEQ 139..234
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055493"
FT VARIANT 226..234
FT /note="Missing (in OI20)"
FT /evidence="ECO:0000269|PubMed:31564437"
FT /id="VAR_083534"
SQ SEQUENCE 234 AA; 26077 MW; 7F0D796A3CC4E339 CRC64;
MAASRWARKA VVLLCASDLL LLLLLLPPPG SCAAEGSPGT PDESTPPPRK KKKDIRDYND
ADMARLLEQW EKDDDIEEGD LPEHKRPSAP VDFSKIDPSK PESILKMTKK GKTLMMFVTV
SGSPTEKETE EITSLWQGSL FNANYDVQRF IVGSDRAIFM LRDGSYAWEI KDFLVGQDRC
ADVTLEGQVY PGKGGGSKEK NKTKQDKGKK KKEGDLKSRS SKEENRAGNK REDL
