LYPD3_HUMAN
ID LYPD3_HUMAN Reviewed; 346 AA.
AC O95274; Q9UJ74;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ly6/PLAUR domain-containing protein 3;
DE AltName: Full=GPI-anchored metastasis-associated protein C4.4A homolog;
DE AltName: Full=Matrigel-induced gene C4 protein;
DE Short=MIG-C4;
DE Flags: Precursor;
GN Name=LYPD3; Synonyms=C4.4A; ORFNames=UNQ491/PRO1007;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Urothelium;
RX PubMed=11245483;
RA Smith B.A., Kennedy W.J., Harnden P., Selby P.J., Trejdosiewicz L.K.,
RA Southgate J.;
RT "Identification of genes involved in human urothelial cell-matrix
RT interactions: implications for the progression pathways of malignant
RT urothelium.";
RL Cancer Res. 61:1678-1685(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=11179665; DOI=10.1016/s0378-1119(00)00515-1;
RA Wuerfel J., Seiter S., Stassar M., Claas A., Klaes R., Roesel M.,
RA Marhaba R., Savelyeva L., Schwab M., Matzku S., Zoeller M.;
RT "Cloning of the human homologue of the metastasis-associated rat C4.4A.";
RL Gene 262:35-41(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [6]
RP PROTEIN SEQUENCE OF 196-216, FUNCTION, TISSUE SPECIFICITY, GLYCOSYLATION,
RP AND GPI-ANCHOR.
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).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH AGR2 AND AGR3.
RX PubMed=12592373; DOI=10.1038/sj.bjc.6600740;
RA Fletcher G.C., Patel S., Tyson K., Adam P.J., Schenker M., Loader J.A.,
RA Daviet L., Legrain P., Parekh R., Harris A.L., Terrett J.A.;
RT "hAG-2 and hAG-3, human homologues of genes involved in differentiation,
RT are associated with oestrogen receptor-positive breast tumours and interact
RT with metastasis gene C4.4a and dystroglycan.";
RL Br. J. Cancer 88:579-585(2003).
CC -!- FUNCTION: Supports cell migration. May be involved in urothelial cell-
CC matrix interactions. May be involved in tumor progression.
CC {ECO:0000269|PubMed:11179665, ECO:0000269|PubMed:11245483,
CC ECO:0000269|PubMed:12592373, ECO:0000269|PubMed:15012588}.
CC -!- SUBUNIT: Binds laminin-1 and laminin-5. Interacts with LGALS3 (By
CC similarity). Interacts with AGR2 and AGR3. {ECO:0000250,
CC ECO:0000269|PubMed:12592373}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Expressed in placenta, skin and urothelium. Found
CC in suprabasal keratinocytes of chronic wounds. Weak expression is found
CC in esophagus and peripheral blood mononuclear cells. Found in the
CC majority of primary and metastatic transitional cell carcinomas (TCCs)
CC and as well in breast cancer tissues, but not in adjacent normal
CC tissues. High expression is found in the tumor component of some
CC noninvasive superficial lesions and in invasive and metastatic
CC urothelial cancers. {ECO:0000269|PubMed:11179665,
CC ECO:0000269|PubMed:12592373, ECO:0000269|PubMed:15012588}.
CC -!- INDUCTION: Up-regulated in migrating keratinocytes during
CC epithelization of incisional skin wounds.
CC -!- PTM: N-glycosylated and O-glycosylated. {ECO:0000269|PubMed:15012588}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LYPD3ID44245ch19q13.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF082889; AAD13751.1; -; mRNA.
DR EMBL; AJ223603; CAA11469.2; -; mRNA.
DR EMBL; AY359006; AAQ89365.1; -; mRNA.
DR EMBL; AC018758; AAG09062.1; -; Genomic_DNA.
DR EMBL; BC039167; AAH39167.1; -; mRNA.
DR CCDS; CCDS12620.1; -.
DR RefSeq; NP_055215.2; NM_014400.2.
DR PDB; 6IOM; X-ray; 2.59 A; A/B=31-231.
DR PDB; 6ION; X-ray; 2.75 A; A=31-231.
DR PDBsum; 6IOM; -.
DR PDBsum; 6ION; -.
DR AlphaFoldDB; O95274; -.
DR SMR; O95274; -.
DR BioGRID; 117985; 138.
DR IntAct; O95274; 89.
DR MINT; O95274; -.
DR STRING; 9606.ENSP00000244333; -.
DR GlyGen; O95274; 5 sites.
DR iPTMnet; O95274; -.
DR PhosphoSitePlus; O95274; -.
DR BioMuta; LYPD3; -.
DR EPD; O95274; -.
DR jPOST; O95274; -.
DR MassIVE; O95274; -.
DR MaxQB; O95274; -.
DR PaxDb; O95274; -.
DR PeptideAtlas; O95274; -.
DR PRIDE; O95274; -.
DR ProteomicsDB; 50778; -.
DR ABCD; O95274; 2 sequenced antibodies.
DR Antibodypedia; 45382; 264 antibodies from 27 providers.
DR DNASU; 27076; -.
DR Ensembl; ENST00000244333.4; ENSP00000244333.2; ENSG00000124466.9.
DR GeneID; 27076; -.
DR KEGG; hsa:27076; -.
DR MANE-Select; ENST00000244333.4; ENSP00000244333.2; NM_014400.3; NP_055215.2.
DR UCSC; uc002owl.2; human.
DR CTD; 27076; -.
DR DisGeNET; 27076; -.
DR GeneCards; LYPD3; -.
DR HGNC; HGNC:24880; LYPD3.
DR HPA; ENSG00000124466; Group enriched (esophagus, skin, vagina).
DR MIM; 609484; gene.
DR neXtProt; NX_O95274; -.
DR OpenTargets; ENSG00000124466; -.
DR PharmGKB; PA142671490; -.
DR VEuPathDB; HostDB:ENSG00000124466; -.
DR eggNOG; ENOG502RYZP; Eukaryota.
DR GeneTree; ENSGT00940000153599; -.
DR HOGENOM; CLU_062960_0_0_1; -.
DR InParanoid; O95274; -.
DR OMA; RQGAEHE; -.
DR OrthoDB; 1102918at2759; -.
DR PhylomeDB; O95274; -.
DR TreeFam; TF337983; -.
DR PathwayCommons; O95274; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; O95274; -.
DR BioGRID-ORCS; 27076; 11 hits in 1072 CRISPR screens.
DR ChiTaRS; LYPD3; human.
DR GeneWiki; LYPD3; -.
DR GenomeRNAi; 27076; -.
DR Pharos; O95274; Tbio.
DR PRO; PR:O95274; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O95274; protein.
DR Bgee; ENSG00000124466; Expressed in gingival epithelium and 129 other tissues.
DR ExpressionAtlas; O95274; baseline and differential.
DR Genevisible; O95274; HS.
DR GO; GO:0046658; C:anchored component of plasma membrane; TAS:HGNC-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043236; F:laminin binding; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; IGI:ARUK-UCL.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Repeat; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..326
FT /note="Ly6/PLAUR domain-containing protein 3"
FT /id="PRO_0000226751"
FT PROPEP 327..346
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000226752"
FT DOMAIN 33..126
FT /note="UPAR/Ly6 1"
FT DOMAIN 140..222
FT /note="UPAR/Ly6 2"
FT REGION 233..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 326
FT /note="GPI-anchor amidated cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 32..42
FT /evidence="ECO:0007829|PDB:6IOM"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:6IOM"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:6IOM"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:6IOM"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:6IOM"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:6IOM"
FT STRAND 99..110
FT /evidence="ECO:0007829|PDB:6IOM"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6IOM"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6IOM"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6IOM"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6IOM"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:6IOM"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:6IOM"
FT STRAND 184..195
FT /evidence="ECO:0007829|PDB:6IOM"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:6IOM"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:6IOM"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:6ION"
SQ SEQUENCE 346 AA; 35971 MW; 97FF9B4A554934FF CRC64;
MDPARKAGAQ AMIWTAGWLL LLLLRGGAQA LECYSCVQKA DDGCSPNKMK TVKCAPGVDV
CTEAVGAVET IHGQFSLAVR GCGSGLPGKN DRGLDLHGLL AFIQLQQCAQ DRCNAKLNLT
SRALDPAGNE SAYPPNGVEC YSCVGLSREA CQGTSPPVVS CYNASDHVYK GCFDGNVTLT
AANVTVSLPV RGCVQDEFCT RDGVTGPGFT LSGSCCQGSR CNSDLRNKTY FSPRIPPLVR
LPPPEPTTVA STTSVTTSTS APVRPTSTTK PMPAPTSQTP RQGVEHEASR DEEPRLTGGA
AGHQDRSNSG QYPAKGGPQQ PHNKGCVAPT AGLAALLLAV AAGVLL
