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   03-AUG-2022, entry version 74.
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   DNASU; 379565; -.
DR   GeneID; 379565; -.
DR   KEGG; xla:379565; -.
DR   CTD; 379565; -.
DR   Xenbase; XB-GENE-921685; mxra8.S.
DR   OMA; KAVLPCH; -.
DR   OrthoDB; 634484at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 379565; Expressed in lung and 15 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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   SUPFAM; SSF48726; SSF48726; 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