ID   LYPD3_MOUSE             Reviewed;         363 AA.
AC   Q91YK8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   14-DEC-2022, entry version 128.
DE   RecName: Full=Ly6/PLAUR domain-containing protein 3;
DE   AltName: Full=GPI-anchored metastasis-associated protein C4.4A homolog;
DE   Flags: Precursor;
GN   Name=Lypd3; Synonyms=C4.4a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   INDUCTION.
RX   PubMed=15012588; DOI=10.1042/bj20031478;
RA   Hansen L.V., Gaardsvoll H., Nielsen B.S., Lund L.R., Danoe K., Jensen O.N.,
RA   Ploug M.;
RT   "Structural analysis and tissue localization of human C4.4A: a protein
RT   homologue of the urokinase receptor.";
RL   Biochem. Eng. J. 380:845-857(2004).
CC   -!- FUNCTION: Supports cell migration. May be involved in tumor progression
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds laminin-1 and laminin-5. Interacts with LGALS3.
CC       Interacts with AGR2 and AGR3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated in suprabasal keratinocytes of hyperplastic
CC       skin induced by phorbol-ester. {ECO:0000269|PubMed:15012588}.
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DR   EMBL; BC016549; AAH16549.1; -; mRNA.
DR   EMBL; BC094282; AAH94282.1; -; mRNA.
DR   CCDS; CCDS20958.1; -.
DR   RefSeq; NP_598504.1; NM_133743.1.
DR   AlphaFoldDB; Q91YK8; -.
DR   SMR; Q91YK8; -.
DR   STRING; 10090.ENSMUSP00000079543; -.
DR   GlyGen; Q91YK8; 4 sites.
DR   iPTMnet; Q91YK8; -.
DR   PhosphoSitePlus; Q91YK8; -.
DR   PaxDb; Q91YK8; -.
DR   PeptideAtlas; Q91YK8; -.
DR   ProteomicsDB; 291978; -.
DR   Antibodypedia; 45382; 286 antibodies from 26 providers.
DR   Ensembl; ENSMUST00000080718; ENSMUSP00000079543; ENSMUSG00000057454.
DR   GeneID; 72434; -.
DR   KEGG; mmu:72434; -.
DR   UCSC; uc009fqe.1; mouse.
DR   AGR; MGI:1919684; -.
DR   CTD; 27076; -.
DR   MGI; MGI:1919684; Lypd3.
DR   VEuPathDB; HostDB:ENSMUSG00000057454; -.
DR   eggNOG; ENOG502RYZP; Eukaryota.
DR   GeneTree; ENSGT00940000153599; -.
DR   HOGENOM; CLU_062960_0_0_1; -.
DR   InParanoid; Q91YK8; -.
DR   OMA; RQGAEHE; -.
DR   OrthoDB; 1102918at2759; -.
DR   PhylomeDB; Q91YK8; -.
DR   TreeFam; TF337983; -.
DR   Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   BioGRID-ORCS; 72434; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Lypd3; mouse.
DR   PRO; PR:Q91YK8; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q91YK8; protein.
DR   Bgee; ENSMUSG00000057454; Expressed in lip and 53 other tissues.
DR   Genevisible; Q91YK8; MM.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0043236; F:laminin binding; ISO:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; ISO:MGI.
DR   CDD; cd00117; LU; 2.
DR   Gene3D; 2.10.60.10; -; 2.
DR   InterPro; IPR016054; LY6_UPA_recep-like.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   Pfam; PF00021; UPAR_LY6; 2.
DR   SMART; SM00134; LU; 1.
DR   SUPFAM; SSF57302; Snake toxin-like; 2.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..343
FT                   /note="Ly6/PLAUR domain-containing protein 3"
FT                   /id="PRO_0000226753"
FT   PROPEP          344..363
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000226754"
FT   DOMAIN          35..128
FT                   /note="UPAR/Ly6 1"
FT   DOMAIN          142..224
FT                   /note="UPAR/Ly6 2"
FT   REGION          238..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           343
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   363 AA;  37489 MW;  D6CE5139A17CC5FA CRC64;
     MDAARRGDTQ PVMWTTGWLL LLPLLLCEGA QALECYSCVQ KADDGCSPHR MKTVKCGPGV
     DVCTEAVGAV ETIHGQFSVA VRGCGSGIPG KNDRGLDLHG LLAFFQLQQC SEDRCNAKLN
     LTLRGLNPAG NESAYEPNGA ECYSCVGLSR EKCQGSMPPV VNCYNASGRV YKGCFDGNVT
     LTAANVTVSL PVRGCVQDET CTRDGVTGPG FTLSGSCCQG PRCNADLRNK TYFSPRIPPL
     VLLPPPTTAA PSTRAQNSSS TTSTAAPTTT TSIIKPTTAQ ASHTSPHEMD LEVIQEEGAS
     LSGGAAGHGG TAGHGGAAGH QDRSNMEKYP GKGGAQIPAK GGSGTLGSWL SAVLLTVVAG
     AML
//