METRN_MOUSE
ID METRN_MOUSE Reviewed; 291 AA.
AC Q8C1Q4; Q45G31; Q6P6N6; Q8CI64; Q922A8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Meteorin;
DE AltName: Full=Hypoxia/reoxygenation regulatory factor;
DE Flags: Precursor;
GN Name=Metrn; Synonyms=Hyrac;
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 [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15085178; DOI=10.1038/sj.emboj.7600202;
RA Nishino J., Yamashita K., Hashiguchi H., Fujii H., Shimazaki T., Hamada H.;
RT "Meteorin: a secreted protein that regulates glial cell differentiation and
RT promotes axonal extension.";
RL EMBO J. 23:1998-2008(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RA Park J.A., Kim K.-W.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 6-291 (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Kidney, and Mammary gland;
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 [4]
RP PROTEIN SEQUENCE OF 22-31, TISSUE SPECIFICITY, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=19259827; DOI=10.1007/s12031-009-9189-4;
RA Jorgensen J.R., Thompson L., Fjord-Larsen L., Krabbe C., Torp M.,
RA Kalkkinen N., Hansen C., Wahlberg L.;
RT "Characterization of Meteorin--an evolutionary conserved neurotrophic
RT factor.";
RL J. Mol. Neurosci. 39:104-116(2009).
RN [5]
RP DISULFIDE BONDS.
RX PubMed=28245108; DOI=10.1021/acs.analchem.6b04600;
RA Wen D., Xiao Y., Vecchi M.M., Gong B.J., Dolnikova J., Pepinsky R.B.;
RT "Determination of the disulfide structure of murine Meteorin, a
RT neurotrophic factor, by LC-MS and electron transfer dissociation-high-
RT energy collisional dissociation analysis of proteolytic fragments.";
RL Anal. Chem. 89:4021-4030(2017).
CC -!- FUNCTION: Involved in both glial cell differentiation and axonal
CC network formation during neurogenesis. Promotes astrocyte
CC differentiation and transforms cerebellar astrocytes into radial glia.
CC Also induces axonal extension in small and intermediate neurons of
CC sensory ganglia by activating nearby satellite glia.
CC {ECO:0000269|PubMed:15085178}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19259827}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15085178}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C1Q4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C1Q4-2; Sequence=VSP_010844, VSP_010845;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Expressed in
CC undifferentiated neural progenitors and in astrocyte lineage,
CC particulary in Bergmann glia, a subtype of radial glia, and a few
CC discrete neuronal populations residing in the superior colliculus, the
CC ocular motor nucleus, the raphe and pontine nuclei, and in various
CC thalamic nuclei. Weakly expressed in heart, kidney, skeletal muscle,
CC spleen, testis, gut and lung. {ECO:0000269|PubMed:15085178,
CC ECO:0000269|PubMed:19259827}.
CC -!- INDUCTION: By all-trans retinoic acid (ATRA).
CC {ECO:0000269|PubMed:15085178}.
CC -!- MISCELLANEOUS: Was called meteorin because it can transform glial cells
CC into cells with an elongated trail.
CC -!- SIMILARITY: Belongs to the meteorin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37181.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ133462; AAZ41748.1; -; mRNA.
DR EMBL; BC008695; AAH08695.1; -; mRNA.
DR EMBL; BC037181; AAH37181.1; ALT_INIT; mRNA.
DR EMBL; BC062118; AAH62118.1; -; mRNA.
DR CCDS; CCDS28529.1; -. [Q8C1Q4-1]
DR RefSeq; NP_598480.1; NM_133719.2. [Q8C1Q4-1]
DR AlphaFoldDB; Q8C1Q4; -.
DR STRING; 10090.ENSMUSP00000127275; -.
DR PhosphoSitePlus; Q8C1Q4; -.
DR PaxDb; Q8C1Q4; -.
DR PRIDE; Q8C1Q4; -.
DR ProteomicsDB; 295886; -. [Q8C1Q4-1]
DR ProteomicsDB; 295887; -. [Q8C1Q4-2]
DR Antibodypedia; 22849; 108 antibodies from 16 providers.
DR Ensembl; ENSMUST00000002344; ENSMUSP00000002344; ENSMUSG00000002274. [Q8C1Q4-1]
DR Ensembl; ENSMUST00000165838; ENSMUSP00000127275; ENSMUSG00000002274. [Q8C1Q4-1]
DR GeneID; 70083; -.
DR KEGG; mmu:70083; -.
DR UCSC; uc008bbz.1; mouse. [Q8C1Q4-1]
DR CTD; 79006; -.
DR MGI; MGI:1917333; Metrn.
DR VEuPathDB; HostDB:ENSMUSG00000002274; -.
DR eggNOG; ENOG502QUQB; Eukaryota.
DR GeneTree; ENSGT00390000001390; -.
DR HOGENOM; CLU_069970_0_0_1; -.
DR InParanoid; Q8C1Q4; -.
DR OMA; EACRPCN; -.
DR PhylomeDB; Q8C1Q4; -.
DR TreeFam; TF330918; -.
DR BioGRID-ORCS; 70083; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q8C1Q4; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8C1Q4; protein.
DR Bgee; ENSMUSG00000002274; Expressed in floor plate of midbrain and 249 other tissues.
DR ExpressionAtlas; Q8C1Q4; baseline and differential.
DR Genevisible; Q8C1Q4; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR GO; GO:0010001; P:glial cell differentiation; IBA:GO_Central.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IDA:MGI.
DR GO; GO:0060019; P:radial glial cell differentiation; IDA:MGI.
DR InterPro; IPR039229; Meteorin.
DR PANTHER; PTHR28593:SF2; PTHR28593:SF2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation;
KW Direct protein sequencing; Disulfide bond; Neurogenesis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:19259827"
FT CHAIN 22..291
FT /note="Meteorin"
FT /id="PRO_0000021681"
FT DISULFID 28..49
FT /evidence="ECO:0000269|PubMed:28245108"
FT DISULFID 80..116
FT /evidence="ECO:0000269|PubMed:28245108"
FT DISULFID 169..240
FT /evidence="ECO:0000269|PubMed:28245108"
FT DISULFID 172..264
FT /evidence="ECO:0000269|PubMed:28245108"
FT DISULFID 182..286
FT /evidence="ECO:0000269|PubMed:28245108"
FT VAR_SEQ 1..164
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010844"
FT VAR_SEQ 165..166
FT /note="VD -> ML (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010845"
SQ SEQUENCE 291 AA; 31469 MW; 643B933B7D127973 CRC64;
MLVATLLCAL CCGLLAASAH AGYSEDRCSW RGSGLTQEPG SVGQLTLDCT EGAIEWLYPA
GALRLTLGGP DPGTRPSIVC LRPERPFAGA QVFAERMTGN LELLLAEGPD LAGGRCMRWG
PRERRALFLQ ATPHRDISRR VAAFRFELHE DQRAEMSPQA QGLGVDGACR PCSDAELLLA
ACTSDFVIHG TIHGVAHDTE LQESVITVVV ARVIRQTLPL FKEGSSEGQG RASIRTLLRC
GVRPGPGSFL FMGWSRFGEA WLGCAPRFQE FSRVYSAALT THLNPCEMAL D
