ID MXRA8_XENLA Reviewed; 435 AA.
AC Q7T0R0;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Matrix remodeling-associated protein 8;
DE Flags: Precursor;
GN Name=mxra8;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) 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.
CC {ECO:0000250|UniProtKB:Q9DBV4}.
CC -!- SUBUNIT: Homodimer in cis. Does not appear to form trans-homodimers.
CC {ECO:0000250|UniProtKB:Q9DBV4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9DBV4};
CC Single-pass type I membrane protein {ECO:0000255}.
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DR EMBL; BC056081; AAH56081.1; -; mRNA.
DR RefSeq; NP_001079875.1; NM_001086406.1.
DR AlphaFoldDB; Q7T0R0; -.
DR SMR; Q7T0R0; -.
DR GlyCosmos; Q7T0R0; 5 sites, No reported glycans.
DR DNASU; 379565; -.
DR GeneID; 379565; -.
DR KEGG; xla:379565; -.
DR AGR; Xenbase:XB-GENE-921685; -.
DR CTD; 379565; -.
DR Xenbase; XB-GENE-921685; mxra8.S.
DR OMA; WTERHDE; -.
DR OrthoDB; 4235152at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 379565; Expressed in lung and 15 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; MATRIX REMODELING-ASSOCIATED PROTEIN 8; 1.
DR PANTHER; PTHR44793:SF1; MATRIX REMODELING-ASSOCIATED PROTEIN 8; 1.
DR Pfam; PF07686; V-set; 2.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..435
FT /note="Matrix remodeling-associated protein 8"
FT /id="PRO_0000298669"
FT TOPO_DOM 23..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..158
FT /note="Ig-like V-type 1"
FT DOMAIN 156..293
FT /note="Ig-like V-type 2"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
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..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 187..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 435 AA; 50880 MW; C23E61045D39BF66 CRC64;
MEIRCKVLVC HIILLHSATV YLYSVPASQQ NPESVVVSVT NISTHVGDQG FLTCESYRMV
WTQDNLMDRQ RVVHWDLYNS QGVYRGERLL DMFSAGEQRI YKDYNQRRIS VSESAFQDGN
FSLVIKDVSM IDQGLYSCNL HHHYCHLDET VRVQLNITKS ERKVKIYWDG EKIVIVALVH
STVLLPCENH DHMWTDRHRE EDQQVVHWDR QAPGIPHDRA DRLIDMYASG ERRAYGSLFL
RRKMNVSNSA FSQGDFTLFI PYLTRGDEGT YSCHLHHHYC GLHERRIFYL SVSDRPKTEE
PSKTNSDSAP AIDSNVVQEN KVINVTIQES RLHFFQQLGY ILATLLLFIL LLTAVILITR
KHQKRGYAYN LNKPQGKEVN MQEICLRPPD LIQYKKEELR IDYKNNILKE RAEMDRVFAP
KNIDLDLELR KEYCK
//
