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Mesencephalic astrocyte-derived neurotrophic factor (Arginine-rich protein) (Protein ARMET)

 MANF_HUMAN              Reviewed;         182 AA.
P55145; Q14CX4; Q86U67; Q96IS4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
03-MAY-2011, sequence version 3.
12-SEP-2018, entry version 153.
RecName: Full=Mesencephalic astrocyte-derived neurotrophic factor;
AltName: Full=Arginine-rich protein;
AltName: Full=Protein ARMET;
Flags: Precursor;
Name=MANF; Synonyms=ARMET, ARP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DISCUSSION OF A PUTATIVE CANCER
VARIANT.
PubMed=8649854;
Shridhar V., Rivard S., Shridhar R., Mullins C., Bostick L., Sakr W.,
Grignon D., Miller O.J., Smith D.I.;
"A gene from human chromosomal band 3p21.1 encodes a highly conserved
arginine-rich protein and is mutated in renal cell carcinomas.";
Oncogene 12:1931-1939(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
PROTEIN SEQUENCE OF 25-39.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[6]
PROTEIN SEQUENCE OF 25-29, FUNCTION, SUBCELLULAR LOCATION, AND
GLYCOSYLATION.
PubMed=12794311; DOI=10.1385/JMN:20:2:173;
Petrova P., Raibekas A., Pevsner J., Vigo N., Anafi M., Moore M.K.,
Peaire A.E., Shridhar V., Smith D.I., Kelly J., Durocher Y.,
Commissiong J.W.;
"MANF: a new mesencephalic, astrocyte-derived neurotrophic factor with
selectivity for dopaminergic neurons.";
J. Mol. Neurosci. 20:173-188(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=18561914; DOI=10.1016/j.yexcr.2008.05.001;
Apostolou A., Shen Y., Liang Y., Luo J., Fang S.;
"Armet, a UPR-upregulated protein, inhibits cell proliferation and ER
stress-induced cell death.";
Exp. Cell Res. 314:2454-2467(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
FUNCTION, INTERACTION WITH HSPA5, SUBCELLULAR LOCATION, INDUCTION, AND
MUTAGENESIS OF 179-ARG--LYS-182 AND ARG-179.
PubMed=22637475; DOI=10.1074/jbc.M112.356345;
Glembotski C.C., Thuerauf D.J., Huang C., Vekich J.A., Gottlieb R.A.,
Doroudgar S.;
"Mesencephalic astrocyte-derived neurotrophic factor protects the
heart from ischemic damage and is selectively secreted upon
sarco/endoplasmic reticulum calcium depletion.";
J. Biol. Chem. 287:25893-25904(2012).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DOMAIN, AND MUTAGENESIS OF
LYS-112.
PubMed=29497057; DOI=10.1038/s41467-018-03355-0;
Bai M., Vozdek R., Hnizda A., Jiang C., Wang B., Kuchar L., Li T.,
Zhang Y., Wood C., Feng L., Dang Y., Ma D.K.;
"Conserved roles of C. elegans and human MANFs in sulfatide binding
and cytoprotection.";
Nat. Commun. 9:897-897(2018).
[14]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 25-182, DOMAIN, AND
DISULFIDE BONDS.
PubMed=19258449; DOI=10.1093/protein/gzn080;
Parkash V., Lindholm P., Peranen J., Kalkkinen N., Oksanen E.,
Saarma M., Leppanen V.-M., Goldman A.;
"The structure of the conserved neurotrophic factors MANF and CDNF
explains why they are bifunctional.";
Protein Eng. Des. Sel. 22:233-241(2009).
[15]
DISCUSSION OF A PUTATIVE CANCER VARIANT.
PubMed=8971156;
Shridhar R., Shridhar V., Rivard S., Siegfried J.M.,
Pietraszkiewicz H., Ensley J., Pauley R., Grignon D., Sakr W.,
Miller O.J., Smith D.I.;
"Mutations in the arginine-rich protein gene, in lung, breast, and
prostate cancers, and in squamous cell carcinoma of the head and
neck.";
Cancer Res. 56:5576-5578(1996).
[16]
DISCUSSION OF PUTATIVE CANCER VARIANTS.
PubMed=9174057; DOI=10.1038/sj.onc.1201054;
Shridhar V., Rivard S., Wang X., Shridhar R., Paisley C., Mullins C.,
Beirnat L., Dugan M., Sarkar F., Miller O.J., Vaitkevicius V.K.,
Smith D.I.;
"Mutations in the arginine-rich protein gene (ARP) in pancreatic
cancer.";
Oncogene 14:2213-2216(1997).
-!- FUNCTION: Selectively promotes the survival of dopaminergic
neurons of the ventral mid-brain (PubMed:12794311). Modulates
GABAergic transmission to the dopaminergic neurons of the
substantia nigra (By similarity). Enhances spontaneous, as well as
evoked, GABAergic inhibitory postsynaptic currents in dopaminergic
neurons (By similarity). Inhibits cell proliferation and
endoplasmic reticulum (ER) stress-induced cell death
(PubMed:18561914, PubMed:22637475, PubMed:29497057). Retained in
the ER/sarcoplasmic reticulum (SR) through association with the
endoplasmic reticulum chaperone protein HSPA5 under normal
conditions (PubMed:22637475). Up-regulated and secreted by the
ER/SR in response to ER stress and hypoxia (PubMed:22637475).
Following secretion by the ER/SR, directly binds to 3-O-
sulfogalactosylceramide, a lipid sulfatide in the outer cell
membrane of target cells (PubMed:29497057). Sulfatide binding
promotes its cellular uptake by endocytosis, and is required for
its role in alleviating ER stress and cell toxicity under hypoxic
and ER stress conditions (PubMed:29497057).
{ECO:0000250|UniProtKB:P0C5H9, ECO:0000269|PubMed:12794311,
ECO:0000269|PubMed:18561914, ECO:0000269|PubMed:22637475,
ECO:0000269|PubMed:29497057}.
-!- SUBUNIT: Interacts with HSPA5; the interaction is direct.
{ECO:0000269|PubMed:22637475}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12794311,
ECO:0000269|PubMed:18561914, ECO:0000269|PubMed:22637475,
ECO:0000269|PubMed:29497057}. Endoplasmic reticulum lumen
{ECO:0000305|PubMed:29497057}. Sarcoplasmic reticulum lumen
{ECO:0000269|PubMed:22637475}. Note=Retained in the endoplasmic
reticulum (ER), and sarcoplasmic reticulum (SR) under normal
conditions (PubMed:22637475). Up-regulated and secreted by the
ER/SR in response to ER stress and hypoxia (PubMed:22637475,
PubMed:29497057). {ECO:0000269|PubMed:22637475,
ECO:0000269|PubMed:29497057}.
-!- INDUCTION: By endoplasmic reticulum stress (PubMed:18561914,
PubMed:22637475, PubMed:29497057). By hypoxia (PubMed:29497057).
{ECO:0000269|PubMed:18561914, ECO:0000269|PubMed:22637475,
ECO:0000269|PubMed:29497057}.
-!- DOMAIN: The N-terminal region may be responsible for neurotrophic
activity while the C-terminal region may play a role in the ER
stress response. {ECO:0000269|PubMed:19258449}.
-!- DOMAIN: The N-terminal region may be required for lipid sulfatide
binding. {ECO:0000269|PubMed:29497057}.
-!- PTM: May contain sialic acid residues.
-!- SIMILARITY: Belongs to the ARMET family. {ECO:0000305}.
-!- CAUTION: Was originally (PubMed:8649854, PubMed:8971156 and
PubMed:9174057) thought to be much longer and included an
arginine-rich region thought to be the target of cancer-causing
mutations. All these mutations are in what is now thought to be
the 5'-UTR of the mRNA. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB08753.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAI13589.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAI13591.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M83751; AAB08753.1; ALT_INIT; mRNA.
EMBL; BT007110; AAP35774.1; -; mRNA.
EMBL; AC092037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007282; AAH07282.1; -; mRNA.
EMBL; BC113588; AAI13589.1; ALT_INIT; mRNA.
EMBL; BC113590; AAI13591.1; ALT_INIT; mRNA.
RefSeq; NP_006001.4; NM_006010.5.
UniGene; Hs.436446; -.
PDB; 2KVD; NMR; -; A=25-182.
PDB; 2KVE; NMR; -; A=120-182.
PDB; 2W51; X-ray; 2.80 A; A=25-182.
PDBsum; 2KVD; -.
PDBsum; 2KVE; -.
PDBsum; 2W51; -.
ProteinModelPortal; P55145; -.
SMR; P55145; -.
BioGrid; 113621; 12.
IntAct; P55145; 4.
MINT; P55145; -.
STRING; 9606.ENSP00000432799; -.
iPTMnet; P55145; -.
PhosphoSitePlus; P55145; -.
BioMuta; MANF; -.
DMDM; 332278201; -.
OGP; P55145; -.
EPD; P55145; -.
MaxQB; P55145; -.
PaxDb; P55145; -.
PeptideAtlas; P55145; -.
PRIDE; P55145; -.
ProteomicsDB; 56793; -.
DNASU; 7873; -.
Ensembl; ENST00000627526; ENSP00000487450; ENSG00000145050.
GeneID; 7873; -.
KEGG; hsa:7873; -.
UCSC; uc003dbc.4; human.
CTD; 7873; -.
DisGeNET; 7873; -.
GeneCards; MANF; -.
HGNC; HGNC:15461; MANF.
HPA; HPA011175; -.
MIM; 601916; gene.
neXtProt; NX_P55145; -.
Orphanet; 1333; Familial pancreatic carcinoma.
PharmGKB; PA24993; -.
eggNOG; KOG4154; Eukaryota.
eggNOG; ENOG4111QMZ; LUCA.
HOGENOM; HOG000264245; -.
InParanoid; P55145; -.
KO; K22556; -.
PhylomeDB; P55145; -.
TreeFam; TF314252; -.
Reactome; R-HSA-114608; Platelet degranulation.
EvolutionaryTrace; P55145; -.
GeneWiki; ARMET; -.
GenomeRNAi; 7873; -.
PRO; PR:P55145; -.
Proteomes; UP000005640; Unplaced.
CleanEx; HS_ARMET; -.
Genevisible; P55145; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0008289; F:lipid binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0071542; P:dopaminergic neuron differentiation; IBA:GO_Central.
GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:1905897; P:regulation of response to endoplasmic reticulum stress; IMP:UniProtKB.
GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
Gene3D; 1.10.720.30; -; 1.
InterPro; IPR019345; Armet_prot.
InterPro; IPR036361; SAP_dom_sf.
PANTHER; PTHR12990; PTHR12990; 1.
Pfam; PF10208; Armet; 1.
SUPFAM; SSF68906; SSF68906; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Endoplasmic reticulum; Glycoprotein; Growth factor;
Lipid-binding; Phosphoprotein; Reference proteome;
Sarcoplasmic reticulum; Secreted; Sialic acid; Signal;
Stress response; Unfolded protein response.
SIGNAL 1 24 {ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:12794311}.
CHAIN 25 182 Mesencephalic astrocyte-derived
neurotrophic factor.
/FTId=PRO_0000002305.
MOD_RES 76 76 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9CXI5}.
DISULFID 30 117 {ECO:0000269|PubMed:19258449}.
DISULFID 33 106 {ECO:0000269|PubMed:19258449}.
DISULFID 64 75 {ECO:0000269|PubMed:19258449}.
DISULFID 151 154 {ECO:0000269|PubMed:19258449}.
MUTAGEN 112 112 K->L: Reduced sulfatide binding and
uptake by target cells. Reduces
cytoprotective effect of the wild-type
protein. Attenuates stress granule
formation in response to endoplasmic
reticulum stress.
{ECO:0000269|PubMed:29497057}.
MUTAGEN 179 182 Missing: Two-fold increase in secretion.
{ECO:0000269|PubMed:22637475}.
MUTAGEN 179 179 R->K: 14-fold decrease in secretion.
{ECO:0000269|PubMed:22637475}.
CONFLICT 13 14 AL -> RV (in Ref. 1; AAB08753).
{ECO:0000305}.
CONFLICT 179 179 R -> P (in Ref. 1; AAB08753).
{ECO:0000305}.
HELIX 31 46 {ECO:0000244|PDB:2W51}.
HELIX 53 64 {ECO:0000244|PDB:2W51}.
HELIX 69 77 {ECO:0000244|PDB:2W51}.
STRAND 81 83 {ECO:0000244|PDB:2W51}.
HELIX 87 89 {ECO:0000244|PDB:2W51}.
HELIX 90 97 {ECO:0000244|PDB:2W51}.
HELIX 102 112 {ECO:0000244|PDB:2W51}.
TURN 115 118 {ECO:0000244|PDB:2W51}.
HELIX 127 129 {ECO:0000244|PDB:2KVD}.
TURN 132 134 {ECO:0000244|PDB:2KVD}.
HELIX 136 143 {ECO:0000244|PDB:2W51}.
HELIX 155 158 {ECO:0000244|PDB:2W51}.
TURN 166 173 {ECO:0000244|PDB:2KVD}.
SEQUENCE 182 AA; 20700 MW; EE25A5D1A58D1AD7 CRC64;
MRRMWATQGL AVALALSVLP GSRALRPGDC EVCISYLGRF YQDLKDRDVT FSPATIENEL
IKFCREARGK ENRLCYYIGA TDDAATKIIN EVSKPLAHHI PVEKICEKLK KKDSQICELK
YDKQIDLSTV DLKKLRVKEL KKILDDWGET CKGCAEKSDY IRKINELMPK YAPKAASART
DL


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