MXRA8_BOVIN
ID MXRA8_BOVIN Reviewed; 463 AA.
AC Q148M6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Matrix remodeling-associated protein 8;
DE AltName: Full=Limitrin;
DE Flags: Precursor;
GN Name=MXRA8;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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: The RGD motif is involved in integrin ITGAV:ITGB3 binding.
CC {ECO:0000250|UniProtKB:Q9DBV4}.
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DR EMBL; BC118137; AAI18138.1; -; mRNA.
DR RefSeq; NP_001069298.1; NM_001075830.1.
DR PDB; 6ORT; X-ray; 2.30 A; A=24-309.
DR PDBsum; 6ORT; -.
DR AlphaFoldDB; Q148M6; -.
DR SMR; Q148M6; -.
DR STRING; 9913.ENSBTAP00000016253; -.
DR PaxDb; Q148M6; -.
DR PRIDE; Q148M6; -.
DR GeneID; 522392; -.
DR KEGG; bta:522392; -.
DR CTD; 54587; -.
DR eggNOG; ENOG502QRZ7; Eukaryota.
DR HOGENOM; CLU_062248_1_0_1; -.
DR InParanoid; Q148M6; -.
DR OrthoDB; 634484at2759; -.
DR TreeFam; TF332884; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
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 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; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell junction; Cell membrane; Cell projection;
KW Cytoplasm; Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..463
FT /note="Matrix remodeling-associated protein 8"
FT /id="PRO_0000298664"
FT TOPO_DOM 20..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..173
FT /note="Ig-like V-type 1"
FT DOMAIN 176..308
FT /note="Ig-like V-type 2"
FT REGION 309..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 268..270
FT /note="RGD"
FT /evidence="ECO:0000250|UniProtKB:Q9DBV4"
FT SITE 346..347
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q5XI43"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRK3"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 202..288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6ORT"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6ORT"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:6ORT"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 86..100
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 103..117
FT /evidence="ECO:0007829|PDB:6ORT"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6ORT"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:6ORT"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:6ORT"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:6ORT"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 162..174
FT /evidence="ECO:0007829|PDB:6ORT"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6ORT"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:6ORT"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6ORT"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:6ORT"
FT TURN 265..269
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:6ORT"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 284..292
FT /evidence="ECO:0007829|PDB:6ORT"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:6ORT"
FT STRAND 297..308
FT /evidence="ECO:0007829|PDB:6ORT"
SQ SEQUENCE 463 AA; 52034 MW; 9A01D961F0C78B21 CRC64;
MELRAWVLLW RLVLLQSSAV LLSSGPSGPA TSDRSVVSES TVSWAAGARA VLRCQSPRMV
WTQDRLHDRQ RVVHWDLSGS KAGGPARRLV DMYSTGEQRV GEQRLGEQRV GEQRVYEPRD
RGRLLLPPSA FHDGNFSLFI RAVEETDEGL YTCNLHHHYC HLYESLAVSL EVTDDPRAAG
AHWDGEKEVL AVERGAPALL TCVNRAHVWT DRHLEEAQQV VHWDRQPPGV PHDRADRLLD
LYASGERRAY GPPFLRDRVA VEADAFARGD FSLLIDPVEP ADEGTYSCHL HHHYCGLHER
RVFHLRVTEP AARPPPPPRD SPGNGSSHSG APGPGARDPT LTRGRSVINV IVPEGRAHFF
QQLGYVLATL LLFILLLITV VLATRQRRRG GYEYSNKKSK SKGKDINMAE FAVASGDQSL
YRSEDIRLDY KNNILKERAE VAHSLPPAKN IDLDKEFRKE YCK
