ID   LYPD3_RAT               Reviewed;         352 AA.
AC   O55162;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Ly6/PLAUR domain-containing protein 3;
DE   AltName: Full=GPI-anchored metastasis-associated protein C4.4A;
DE   Flags: Precursor;
GN   Name=Lypd3; Synonyms=C4.4a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GPI-ANCHOR, AND TISSUE SPECIFICITY.
RC   STRAIN=BDIX; TISSUE=Colon carcinoma;
RX   PubMed=9788443; DOI=10.1038/sj.onc.1202079;
RA   Roesel M., Claas C., Seiter S., Herlevsen M., Zoeller M.;
RT   "Cloning and functional characterization of a new phosphatidyl-inositol
RT   anchored molecule of a metastasizing rat pancreatic tumor.";
RL   Oncogene 17:1989-2002(1998).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH LAMININ-1; LAMININ-5 AND GALECTIN-3.
RX   PubMed=15729693; DOI=10.1002/ijc.20977;
RA   Paret C., Bourouba M., Beer A., Miyazaki K., Schnoelzer M., Fiedler S.,
RA   Zoeller M.;
RT   "Ly6 family member C4.4A binds laminins 1 and 5, associates with galectin-3
RT   and supports cell migration.";
RL   Int. J. Cancer 115:724-733(2005).
CC   -!- FUNCTION: Supports cell migration. May be involved in tumor
CC       progression. {ECO:0000269|PubMed:15729693, ECO:0000269|PubMed:9788443}.
CC   -!- SUBUNIT: Interacts with AGR2 and AGR3 (By similarity). Binds laminin-1
CC       and laminin-5. Interacts with LGALS3. {ECO:0000250,
CC       ECO:0000269|PubMed:15729693}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- TISSUE SPECIFICITY: Found predominantly on the basal layers of squamous
CC       epithelium. Expressed in the gravid uterus and on epithelial of the
CC       upper gastrointestinal tract. It has been found in tumor lines which
CC       metastasize via the lymphatic system. {ECO:0000269|PubMed:9788443}.
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; AJ001043; CAA04497.1; -; mRNA.
DR   RefSeq; NP_068527.1; NM_021759.1.
DR   AlphaFoldDB; O55162; -.
DR   SMR; O55162; -.
DR   STRING; 10116.ENSRNOP00000027100; -.
DR   GlyGen; O55162; 4 sites.
DR   PaxDb; O55162; -.
DR   Ensembl; ENSRNOT00000027100; ENSRNOP00000027100; ENSRNOG00000019999.
DR   GeneID; 60378; -.
DR   KEGG; rno:60378; -.
DR   UCSC; RGD:69053; rat.
DR   CTD; 27076; -.
DR   RGD; 69053; Lypd3.
DR   eggNOG; ENOG502RYZP; Eukaryota.
DR   GeneTree; ENSGT00940000153599; -.
DR   HOGENOM; CLU_062960_0_0_1; -.
DR   InParanoid; O55162; -.
DR   OMA; RQGAEHE; -.
DR   OrthoDB; 1102918at2759; -.
DR   PhylomeDB; O55162; -.
DR   TreeFam; TF337983; -.
DR   Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   PRO; PR:O55162; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000019999; Expressed in esophagus and 17 other tissues.
DR   Genevisible; O55162; RN.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0043236; F:laminin binding; IDA:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
DR   GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; ISO:RGD.
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   Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..330
FT                   /note="Ly6/PLAUR domain-containing protein 3"
FT                   /id="PRO_0000226755"
FT   PROPEP          331..352
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000226756"
FT   DOMAIN          35..128
FT                   /note="UPAR/Ly6 1"
FT   DOMAIN          142..224
FT                   /note="UPAR/Ly6 2"
FT   REGION          236..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           330
FT                   /note="GPI-anchor amidated glycine"
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   352 AA;  36961 MW;  1894500CFCF9CAF5 CRC64;
     MDAARRGDTQ PVMWTTRWLL LLPLLLCEGA QALECYSCVQ KADDGCSPHK MKTVKCGPGV
     DVCTEAVGAV ESIHGQFSVA VRGCGSGIPG KNDRGLDLHG LLAFIQLQQC TEDRCNAKLN
     LTLRGLNPAG NESAYEHNGA ECYSCMGLSR EKCQGAMPPV VNCYNASGRV YKGCFDGNVT
     LTAANVTVSL PVRGCVQDEA CTRDGVTGPG FTLSGSCCQG PRCNSDLRNK TYFSPRIPPL
     VLLPPPTTPA PSTRTQNSSS TTSTTAPTTA TTTIKPTTVQ ASHTSSTHET EHEVIQEEGS
     HLSGGATGHQ DRSNMGKFPE KGGAQIPSKG GSDALGSWLS AILLTVVAGA ML