PXDC2_HUMAN
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 03-AUG-2022, entry version 138.
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; 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_001282736.1. [Q6UX71-2]
DR RefSeq; NP_116201.7; NM_032812.8. [Q6UX71-1]
DR AlphaFoldDB; Q6UX71; -.
DR BioGRID; 124338; 95.
DR DIP; DIP-46251N; -.
DR IntAct; Q6UX71; 26.
DR MINT; Q6UX71; -.
DR STRING; 9606.ENSP00000366460; -.
DR GlyConnect; 1616; 5 N-Linked glycans (3 sites).
DR GlyGen; Q6UX71; 6 sites, 4 N-linked glycans (3 sites), 3 O-linked glycans (2 sites).
DR iPTMnet; Q6UX71; -.
DR PhosphoSitePlus; Q6UX71; -.
DR BioMuta; PLXDC2; -.
DR DMDM; 74749416; -.
DR EPD; Q6UX71; -.
DR jPOST; Q6UX71; -.
DR MassIVE; Q6UX71; -.
DR MaxQB; Q6UX71; -.
DR PaxDb; Q6UX71; -.
DR PeptideAtlas; Q6UX71; -.
DR PRIDE; Q6UX71; -.
DR ProteomicsDB; 67571; -. [Q6UX71-1]
DR ProteomicsDB; 67572; -. [Q6UX71-2]
DR ProteomicsDB; 67573; -. [Q6UX71-3]
DR Antibodypedia; 25453; 172 antibodies from 31 providers.
DR DNASU; 84898; -.
DR Ensembl; ENST00000377242.7; ENSP00000366450.3; ENSG00000120594.17. [Q6UX71-2]
DR Ensembl; ENST00000377252.5; ENSP00000366460.3; ENSG00000120594.17. [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 CTD; 84898; -.
DR DisGeNET; 84898; -.
DR GeneCards; PLXDC2; -.
DR HGNC; HGNC:21013; PLXDC2.
DR HPA; ENSG00000120594; Low tissue specificity.
DR MIM; 606827; gene.
DR neXtProt; NX_Q6UX71; -.
DR OpenTargets; ENSG00000120594; -.
DR PharmGKB; PA134932187; -.
DR VEuPathDB; HostDB:ENSG00000120594; -.
DR eggNOG; KOG3848; Eukaryota.
DR GeneTree; ENSGT00440000033408; -.
DR HOGENOM; CLU_029494_3_1_1; -.
DR InParanoid; Q6UX71; -.
DR OMA; SHVRYSA; -.
DR OrthoDB; 1361987at2759; -.
DR PhylomeDB; Q6UX71; -.
DR TreeFam; TF314400; -.
DR PathwayCommons; Q6UX71; -.
DR SignaLink; Q6UX71; -.
DR BioGRID-ORCS; 84898; 10 hits in 1063 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 197 other tissues.
DR Genevisible; Q6UX71; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR031152; PLXDC.
DR InterPro; IPR031154; PLXDC2.
DR InterPro; IPR016201; PSI.
DR PANTHER; PTHR13055; PTHR13055; 1.
DR PANTHER; PTHR13055:SF11; PTHR13055:SF11; 1.
DR Pfam; PF01437; PSI; 1.
DR SMART; SM00423; PSI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; 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