ID   MXRA8_CHICK             Reviewed;         437 AA.
AC   Q90WI4;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Matrix remodeling-associated protein 8;
DE   AltName: Full=Plasma membrane protein 1B3;
DE   Flags: Precursor;
GN   Name=MXRA8;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Dong S., Halfter W.;
RT   "An anti cell adhesive protein from embryonic chick kidney.";
RL   Submitted (APR-2001) 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; AF373843; AAK55399.1; -; mRNA.
DR   RefSeq; NP_989967.1; NM_204636.2.
DR   AlphaFoldDB; Q90WI4; -.
DR   SMR; Q90WI4; -.
DR   STRING; 9031.ENSGALP00000034500; -.
DR   PaxDb; Q90WI4; -.
DR   Ensembl; ENSGALT00000104012; ENSGALP00000070479; ENSGALG00000001561.
DR   GeneID; 395347; -.
DR   KEGG; gga:395347; -.
DR   CTD; 54587; -.
DR   VEuPathDB; HostDB:geneid_395347; -.
DR   eggNOG; ENOG502QRZ7; Eukaryota.
DR   GeneTree; ENSGT00390000001509; -.
DR   HOGENOM; CLU_062248_1_0_1; -.
DR   InParanoid; Q90WI4; -.
DR   OrthoDB; 634484at2759; -.
DR   PhylomeDB; Q90WI4; -.
DR   PRO; PR:Q90WI4; -.
DR   Proteomes; UP000000539; Chromosome 21.
DR   Bgee; ENSGALG00000001561; Expressed in lung and 13 other tissues.
DR   ExpressionAtlas; Q90WI4; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
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   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   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..437
FT                   /note="Matrix remodeling-associated protein 8"
FT                   /id="PRO_0000298668"
FT   TOPO_DOM        23..339
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        361..437
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          32..159
FT                   /note="Ig-like V-type 1"
FT   DOMAIN          167..294
FT                   /note="Ig-like V-type 2"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        188..274
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   437 AA;  50704 MW;  398CC264A88D4711 CRC64;
     MEQLAKLLLW QLLLQQSSVV YLYSVPADAS NPDSVVVSVL NISATRGSQA VLPCKSYRMV
     WTQDRLNDRQ RVVHWDVYST YYGDNKMERL CDMYSAGNQR VYSSYNQGRI LMPQNAFTDG
     NFSLVIKDVA ESDAGVYSCN LHHHYCHLYE TVKIQLDITK KAKAAKEYWD GEKAVIVALE
     GSTVMLPCVN RNHIWTERHS EEEQQVVHWD RQPPGVPHDR ADRLIDLYAS GERRSYGPLF
     IRQKMNITDT AFALGDFSLR ISELENADEG TYSCHLHHHY CGLHERRIYQ VFVTEPVREK
     KVVNLTTHNT APAIDPNVVR GHNVINVIIP ESRIHFFQQL GYVLATLLLF VVLLIIVVFI
     TRKRRQRGYE YNVKKYGEKD VNLKEFTVDT TDLTQYKSED IRLDYKNNIL KEKAEQARSF
     PAKNIDLDKD FRKEYCK