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 13-FEB-2019, entry version 116. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT 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., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics 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., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 196-216, FUNCTION, TISSUE SPECIFICITY, MASS RP SPECTROMETRY, GLYCOSYLATION, AND GPI-ANCHOR. RX PubMed=15012588; DOI=10.1042/BJ20031478; RA Hansen L.V., Gaardsvoll H., Nielsen B.S., Lund L.R., Danoe K., RA Jensen O.N., 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., RA Loader J.A., Daviet L., Legrain P., Parekh R., Harris A.L., RA Terrett J.A.; RT "hAG-2 and hAG-3, human homologues of genes involved in RT differentiation, are associated with oestrogen receptor-positive RT breast tumours and interact with metastasis gene C4.4a and RT dystroglycan."; RL Br. J. Cancer 88:579-585(2003). CC -!- FUNCTION: Supports cell migration. May be involved in urothelial CC cell-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. CC Found in suprabasal keratinocytes of chronic wounds. Weak CC expression is found in esophagus and peripheral blood mononuclear CC cells. Found in the majority of primary and metastatic CC transitional cell carcinomas (TCCs) and as well in breast cancer CC tissues, but not in adjacent normal tissues. High expression is CC found in the tumor component of some noninvasive superficial CC lesions and in invasive and metastatic urothelial cancers. CC {ECO:0000269|PubMed:11179665, ECO:0000269|PubMed:12592373, CC ECO:0000269|PubMed:15012588}. CC -!- INDUCTION: Up-regulated in migrating keratinocytes during CC epithelisation of incisional skin wounds. CC -!- PTM: N-glycosylated and O-glycosylated. CC {ECO:0000269|PubMed:15012588}. CC -!- MASS SPECTROMETRY: Mass=21442.9; Method=MALDI; Range=1-204; CC Evidence={ECO:0000269|PubMed:15012588}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and 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 UniGene; Hs.631594; -. DR ProteinModelPortal; O95274; -. DR BioGrid; 117985; 118. DR IntAct; O95274; 16. DR MINT; O95274; -. DR STRING; 9606.ENSP00000244333; -. DR iPTMnet; O95274; -. DR PhosphoSitePlus; O95274; -. DR BioMuta; LYPD3; -. DR EPD; O95274; -. DR jPOST; O95274; -. DR MaxQB; O95274; -. DR PaxDb; O95274; -. DR PeptideAtlas; O95274; -. DR PRIDE; O95274; -. DR ProteomicsDB; 50778; -. DR DNASU; 27076; -. DR Ensembl; ENST00000244333; ENSP00000244333; ENSG00000124466. DR GeneID; 27076; -. DR KEGG; hsa:27076; -. DR UCSC; uc002owl.2; human. DR CTD; 27076; -. DR DisGeNET; 27076; -. DR EuPathDB; HostDB:ENSG00000124466.8; -. DR GeneCards; LYPD3; -. DR HGNC; HGNC:24880; LYPD3. DR HPA; HPA041529; -. DR HPA; HPA041797; -. DR HPA; HPA077859; -. DR MIM; 609484; gene. DR neXtProt; NX_O95274; -. DR OpenTargets; ENSG00000124466; -. DR PharmGKB; PA142671490; -. DR eggNOG; ENOG410IIUT; Eukaryota. DR eggNOG; ENOG41116C6; LUCA. DR GeneTree; ENSGT00940000153599; -. DR HOGENOM; HOG000059631; -. DR HOVERGEN; HBG053008; -. DR InParanoid; O95274; -. DR OMA; CSPHKMK; -. DR OrthoDB; 1102918at2759; -. DR PhylomeDB; O95274; -. DR TreeFam; TF337983; -. DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins. DR ChiTaRS; LYPD3; human. DR GeneWiki; LYPD3; -. DR GenomeRNAi; 27076; -. DR PRO; PR:O95274; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000124466; Expressed in 125 organ(s), highest expression level in esophagus mucosa. DR Genevisible; O95274; HS. DR GO; GO:0046658; C:anchored component of plasma membrane; TAS:HGNC. 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; IBA:GO_Central. DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central. DR InterPro; IPR016054; LY6_UPA_recep-like. DR Pfam; PF00021; UPAR_LY6; 2. DR SMART; SM00134; LU; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Direct protein sequencing; KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome; KW Repeat; Signal. FT SIGNAL 1 30 {ECO:0000255}. FT CHAIN 31 326 Ly6/PLAUR domain-containing protein 3. FT /FTId=PRO_0000226751. FT PROPEP 327 346 Removed in mature form. {ECO:0000255}. FT /FTId=PRO_0000226752. FT DOMAIN 33 126 UPAR/Ly6 1. FT DOMAIN 140 222 UPAR/Ly6 2. FT LIPID 326 326 GPI-anchor amidated cysteine. FT {ECO:0000255}. FT CARBOHYD 118 118 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 163 163 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 176 176 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 183 183 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. 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 //