MXRA8_RAT
ID MXRA8_RAT Reviewed; 382 AA.
AC Q5XI43;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Matrix remodeling-associated protein 8;
DE AltName: Full=Limitrin;
DE Flags: Precursor;
GN Name=Mxra8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [2]
RP CLEAVAGE AFTER SER-324, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT "Peptidomics for studying limited proteolysis.";
RL J. Proteome Res. 14:4921-4931(2015).
CC -!- FUNCTION: Transmembrane protein which can modulate activity of various
CC signaling pathways, probably via binding to integrin ITGAV:ITGB3.
CC Mediates heterophilic cell-cell interactions in vitro. Inhibits
CC osteoclastogenesis downstream of TNFSF11/RANKL and CSF1, where it may
CC function by attenuating signaling via integrin ITGB3 and MAP kinase
CC p38. Plays a role in cartilage formation where it promotes
CC proliferation and maturation of growth plate chondrocytes. Stimulates
CC formation of primary cilia in chondrocytes. Enhances expression of
CC genes involved in the hedgehog signaling pathway in chondrocytes,
CC including the hedgehog signaling molecule IHH; may also promote
CC signaling via the PTHLH/PTHrP pathway. Plays a role in angiogenesis
CC where it suppresses migration of endothelial cells and also promotes
CC their apoptosis. Inhibits VEGF-induced activation of AKT and p38 MAP
CC kinase in endothelial cells. Also inhibits VTN (vitronectin)-mediated
CC integrin ITGAV:ITGB3 signaling and activation of PTK2/FAK. May play a
CC role in the maturation and maintenance of the blood-brain barrier.
CC {ECO:0000250|UniProtKB:Q9BRK3, ECO:0000250|UniProtKB:Q9DBV4}.
CC -!- SUBUNIT: Homodimer in cis. Does not appear to form trans-homodimers.
CC Interacts with ITGB3; the interaction inhibits ITGAV:ITGB3 heterodimer
CC formation. {ECO:0000250|UniProtKB:Q9DBV4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9DBV4};
CC Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight
CC junction {ECO:0000250|UniProtKB:Q9DBV4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9DBV4}. Cell projection, cilium membrane
CC {ECO:0000250|UniProtKB:Q9DBV4}. Nucleus {ECO:0000250|UniProtKB:Q9DBV4}.
CC Note=Primarily localizes to the cell membrane. Detected in the cilium
CC of primary chondrocytes. Highly expressed at areas of cell-cell contact
CC and may localize to tight junctions. Also found in the nucleus where it
CC is detected in the soluble (as opposed to chromatin-bound) fraction.
CC {ECO:0000250|UniProtKB:Q9DBV4}.
CC -!- DOMAIN: RGD motif 2 (but not RGD motif 1) is involved in integrin
CC ITGAV:ITGB3 binding. {ECO:0000250|UniProtKB:Q9DBV4}.
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DR EMBL; BC083849; AAH83849.1; -; mRNA.
DR RefSeq; NP_001007003.1; NM_001007002.1.
DR AlphaFoldDB; Q5XI43; -.
DR SMR; Q5XI43; -.
DR IntAct; Q5XI43; 1.
DR STRING; 10116.ENSRNOP00000058800; -.
DR GlyGen; Q5XI43; 2 sites.
DR PaxDb; Q5XI43; -.
DR Ensembl; ENSRNOT00000067252; ENSRNOP00000058800; ENSRNOG00000019244.
DR GeneID; 313770; -.
DR KEGG; rno:313770; -.
DR CTD; 54587; -.
DR RGD; 1359356; Mxra8.
DR eggNOG; ENOG502QRZ7; Eukaryota.
DR GeneTree; ENSGT00390000001509; -.
DR HOGENOM; CLU_062248_1_0_1; -.
DR InParanoid; Q5XI43; -.
DR PhylomeDB; Q5XI43; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q5XI43; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000019244; Expressed in ovary and 18 other tissues.
DR ExpressionAtlas; Q5XI43; baseline and differential.
DR Genevisible; Q5XI43; RN.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0060857; P:establishment of glial blood-brain barrier; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR042472; MXRA8.
DR PANTHER; PTHR44793; PTHR44793; 1.
DR Pfam; PF07686; V-set; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00406; IGv; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell membrane; Cell projection; Cytoplasm;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Tight junction;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..382
FT /note="Matrix remodeling-associated protein 8"
FT /id="PRO_0000298667"
FT TOPO_DOM 20..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..156
FT /note="Ig-like V-type 1"
FT DOMAIN 159..291
FT /note="Ig-like V-type 2"
FT REGION 297..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 128..130
FT /note="RGD 1"
FT /evidence="ECO:0000250|UniProtKB:Q9DBV4"
FT MOTIF 251..253
FT /note="RGD 2"
FT /evidence="ECO:0000250|UniProtKB:Q9DBV4"
FT SITE 324..325
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:26479776"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRK3"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 185..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 382 AA; 42735 MW; CC4192489450F0D1 CRC64;
MELLSRVLLW KLVLLQSSAV LSSGSPGTAA ASSSVVSESA VSWAAGTQAV LRCQSPRMVW
TQDRLHDRQR VVHWDLSGGP GSQGRRLVDM YSAGEQRVYQ PRDRDRLLLS PSAFHDGNFS
LLIRAVERGD EGVYTCNLHH HYCHLYESLA VRLEVTDDPL LSRAYWDGEK EVLVVALGAP
ALMTCVNREH LWTDRHLEEA QQVVHWDRQL PGVPHDRADR LLDLYASGER RAYGPPFLRD
RVSVNTNAFA RGDFSLRIDD LEPADEGIYS CHLHHHYCGL HERRVFHLRV TEPVFEPPAR
ASPGNGSGHN SVPSPDPTMA RGHSIINVIV PEDHTHFFQQ LGYVLATLLL FILLLITVVL
ATRHRHSGGC KTSDRKAGKS KG
