ID PXDC2_HUMAN Reviewed; 529 AA. AC Q6UX71; Q96E59; Q96PD9; Q96SU9; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 02-SEP-2026, entry version 156. DE RecName: Full=Plexin domain-containing protein 2; DE AltName: Full=Tumor endothelial marker 7-related protein; DE Flags: Precursor; GN Name=PLXDC2; Synonyms=TEM7R; ORFNames=UNQ2514/PRO6003; 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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND RP VARIANTS ILE-396 AND VAL-458. RX PubMed=11559528; RA Carson-Walter E.B., Watkins D.N., Nanda A., Vogelstein B., Kinzler K.W., RA St Croix B.; RT "Cell surface tumor endothelial markers are conserved in mice and humans."; RL Cancer Res. 61:6649-6655(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS ILE-396 RP AND VAL-458. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Ovary; 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [7] RP INTERACTION WITH CTTN. RX PubMed=15574754; DOI=10.1158/0008-5472.can-04-2716; RA Nanda A., Buckhaults P., Seaman S., Agrawal N., Boutin P., Shankara S., RA Nacht M., Teicher B., Stampfl J., Singh S., Vogelstein B., Kinzler K.W., RA St Croix B.; RT "Identification of a binding partner for the endothelial cell surface RT proteins TEM7 and TEM7R."; RL Cancer Res. 64:8507-8511(2004). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). CC -!- FUNCTION: May play a role in tumor angiogenesis. CC {ECO:0000269|PubMed:11559528}. CC -!- SUBUNIT: Interacts with CTTN. {ECO:0000269|PubMed:15574754}. CC -!- INTERACTION: CC Q6UX71; P17516: AKR1C4; NbExp=2; IntAct=EBI-6115410, EBI-21734635; CC Q6UX71; A2APF7: Zbp1; Xeno; NbExp=2; IntAct=EBI-6115410, EBI-6115394; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q6UX71-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6UX71-2; Sequence=VSP_018378; CC Name=3; CC IsoId=Q6UX71-3; Sequence=VSP_018377; CC -!- TISSUE SPECIFICITY: Expressed in the endothelial cells of the stroma CC but not in the endothelial cells of normal colonic tissue. CC {ECO:0000269|PubMed:11559528}. CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}. 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; AF378757; AAL11994.1; -; mRNA. DR EMBL; AY358486; AAQ88850.1; -; mRNA. DR EMBL; AK027529; BAB55178.1; -; mRNA. DR EMBL; AC067743; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC069549; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL353147; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC012885; AAH12885.1; -; mRNA. DR CCDS; CCDS60497.1; -. [Q6UX71-2] DR CCDS; CCDS7132.1; -. [Q6UX71-1] DR RefSeq; NP_001269665.1; NM_001282736.2. [Q6UX71-2] DR RefSeq; NP_116201.7; NM_032812.9. [Q6UX71-1] DR AlphaFoldDB; Q6UX71; -. DR SMR; Q6UX71; -. DR BioGRID; 124338; 112. DR DIP; DIP-46251N; -. DR FunCoup; Q6UX71; 772. DR IntAct; Q6UX71; 72. DR MINT; Q6UX71; -. DR NDEx; MUSIC2-C5372-PLXDC2; Osteosarcoma (U2OS) cell map - C5372 (4 proteins). DR STRING; 9606.ENSP00000366460; -. DR GlyConnect; Q6UX71; 6 N-Linked glycans (4 sites). DR GlyCosmos; Q6UX71; 6 sites, 7 glycans. DR GlyGen; Q6UX71; 8 sites, 26 N-linked glycans (3 sites), 4 O-linked glycans (4 sites). DR iPTMnet; Q6UX71; -. DR PhosphoSitePlus; Q6UX71; -. DR BioMuta; PLXDC2; -. DR DMDM; 74749416; -. DR jPOST; Q6UX71; -. DR MassIVE; Q6UX71; -. DR PaxDb; 9606-ENSP00000366460; -. DR PeptideAtlas; Q6UX71; -. DR ProteomicsDB; 67571; -. [Q6UX71-1] DR ProteomicsDB; 67572; -. [Q6UX71-2] DR ProteomicsDB; 67573; -. [Q6UX71-3] DR Pumba; Q6UX71; -. DR Antibodypedia; 25453; 174 antibodies from 33 providers. DR DNASU; 84898; -. DR Ensembl; ENST00000377242.7; ENSP00000366450.3; ENSG00000120594.18. [Q6UX71-2] DR Ensembl; ENST00000377252.5; ENSP00000366460.3; ENSG00000120594.18. [Q6UX71-1] DR Ensembl; ENST00000888732.1; ENSP00000558791.1; ENSG00000120594.18. [Q6UX71-1] DR GeneID; 84898; -. DR KEGG; hsa:84898; -. DR MANE-Select; ENST00000377252.5; ENSP00000366460.3; NM_032812.9; NP_116201.7. DR UCSC; uc001iqg.3; human. [Q6UX71-1] DR AGR; HGNC:21013; -. DR ClinPGx; PA134932187; -. DR CTD; 84898; -. DR DisGeNET; 84898; -. DR GeneCards; PLXDC2; -. DR HGNC; HGNC:21013; PLXDC2. DR HPA; ENSG00000120594; Low tissue specificity. DR MIM; 606827; gene. DR OpenTargets; ENSG00000120594; -. DR VEuPathDB; HostDB:ENSG00000120594; -. DR eggNOG; KOG3848; Eukaryota. DR GeneTree; ENSGT00440000033408; -. DR HOGENOM; CLU_029494_3_1_1; -. DR InParanoid; Q6UX71; -. DR OMA; LKAQPTC; -. DR OrthoDB; 6285106at2759; -. DR PAN-GO; Q6UX71; 0 GO annotations based on evolutionary models. DR PhylomeDB; Q6UX71; -. DR PathwayCommons; Q6UX71; -. DR SignaLink; Q6UX71; -. DR Agora; ENSG00000120594; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 84898; 10 hits in 1142 CRISPR screens. DR ChiTaRS; PLXDC2; human. DR GeneWiki; PLXDC2; -. DR GenomeRNAi; 84898; -. DR Pharos; Q6UX71; Tbio. DR PRO; PR:Q6UX71; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q6UX71; protein. DR Bgee; ENSG00000120594; Expressed in calcaneal tendon and 199 other cell types or tissues. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR InterPro; IPR063539; NIDO_rel. DR InterPro; IPR002165; Plexin_repeat. DR InterPro; IPR031152; PLXDC. DR InterPro; IPR016201; PSI. DR PANTHER; PTHR13055:SF11; PLEXIN DOMAIN-CONTAINING PROTEIN 2; 1. DR PANTHER; PTHR13055; TUMOR ENDOTHELIAL MARKER 7 RELATED; 1. DR Pfam; PF30706; NIDO_rel; 1. DR Pfam; PF01437; PSI; 1. DR SMART; SM00423; PSI; 1. PE 1: Evidence at protein level; KW Alternative splicing; Glycoprotein; Membrane; Phosphoprotein; KW Proteomics identification; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..30 FT /evidence="ECO:0000255" FT CHAIN 31..529 FT /note="Plexin domain-containing protein 2" FT /id="PRO_0000234574" FT TOPO_DOM 31..454 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 455..475 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 476..529 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 327..372 FT /note="PSI" FT REGION 80..104 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 506 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT CARBOHYD 103 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 160 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT VAR_SEQ 1..378 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_018377" FT VAR_SEQ 109..157 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_018378" FT VARIANT 396 FT /note="V -> I (in dbSNP:rs3817405)" FT /evidence="ECO:0000269|PubMed:11559528, FT ECO:0000269|PubMed:14702039" FT /id="VAR_026292" FT VARIANT 458 FT /note="I -> V (in dbSNP:rs2778979)" FT /evidence="ECO:0000269|PubMed:11559528, FT ECO:0000269|PubMed:14702039" FT /id="VAR_026293" SQ SEQUENCE 529 AA; 59583 MW; CCE911D6DF837B40 CRC64; MARFPKADLA AAGVMLLCHF FTDQFQFADG KPGDQILDWQ YGVTQAFPHT EEEVEVDSHA YSHRWKRNLD FLKAVDTNRA SVGQDSPEPR SFTDLLLDDG QDNNTQIEED TDHNYYISRI YGPSDSASRD LWVNIDQMEK DKVKIHGILS NTHRQAARVN LSFDFPFYGH FLREITVATG GFIYTGEVVH RMLTATQYIA PLMANFDPSV SRNSTVRYFD NGTALVVQWD HVHLQDNYNL GSFTFQATLL MDGRIIFGYK EIPVLVTQIS STNHPVKVGL SDAFVVVHRI QQIPNVRRRT IYEYHRVELQ MSKITNISAV EMTPLPTCLQ FNRCGPCVSS QIGFNCSWCS KLQRCSSGFD RHRQDWVDSG CPEESKEKMC ENTEPVETSS RTTTTVGATT TQFRVLTTTR RAVTSQFPTS LPTEDDTKIA LHLKDNGAST DDSAAEKKGG TLHAGLIIGI LILVLIVATA ILVTVYMYHH PTSAASIFFI ERRPSRWPAM KFRRGSGHPA YAEVEPVGEK EGFIVSEQC //