LYPD3_MOUSE
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 03-AUG-2022, entry version 126.
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 PRIDE; Q91YK8; -.
DR ProteomicsDB; 291978; -.
DR Antibodypedia; 45382; 264 antibodies from 27 providers.
DR Ensembl; ENSMUST00000080718; ENSMUSP00000079543; ENSMUSG00000057454.
DR GeneID; 72434; -.
DR KEGG; mmu:72434; -.
DR UCSC; uc009fqe.1; mouse.
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:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
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; SSF57302; 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
