PLDX1_MOUSE
ID PLDX1_MOUSE Reviewed; 500 AA.
AC Q91ZV7; A2A537; A2A538; Q29R73; Q8BM20; Q9CWV5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Plexin domain-containing protein 1;
DE AltName: Full=Tumor endothelial marker 7;
DE Flags: Precursor;
GN Name=Plxdc1; Synonyms=Tem7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryonic stem cell, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 SUBUNIT.
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 [7]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=16202431; DOI=10.1016/j.mvr.2005.08.004;
RA Wang X.Q., Sheibani N., Watson J.C.;
RT "Modulation of tumor endothelial cell marker 7 expression during
RT endothelial cell capillary morphogenesis.";
RL Microvasc. Res. 70:189-197(2005).
RN [8]
RP INTERACTION WITH NID1.
RX PubMed=16574105; DOI=10.1016/j.febslet.2006.03.033;
RA Lee H.K., Seo I.A., Park H.K., Park H.T.;
RT "Identification of the basement membrane protein nidogen as a candidate
RT ligand for tumor endothelial marker 7 in vitro and in vivo.";
RL FEBS Lett. 580:2253-2257(2006).
CC -!- FUNCTION: Plays a critical role in endothelial cell capillary
CC morphogenesis. {ECO:0000269|PubMed:16202431}.
CC -!- SUBUNIT: Interacts with NID1. May interact with CTTN.
CC {ECO:0000269|PubMed:15574754, ECO:0000269|PubMed:16574105}.
CC -!- INTERACTION:
CC Q91ZV7; P08460: Nid1; Xeno; NbExp=2; IntAct=EBI-8280807, EBI-8280787;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell junction, tight junction
CC {ECO:0000250}. Note=Localized predominantly at the tight junctions of
CC vascular endothelial cells and to a lesser extent at the luminal
CC surface of vascular endothelial cells. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91ZV7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91ZV7-2; Sequence=VSP_017975;
CC -!- TISSUE SPECIFICITY: Detected in brain. Highly expressed in Purkinje
CC cells of the cerebellum. {ECO:0000269|PubMed:11559528}.
CC -!- DEVELOPMENTAL STAGE: Expression increases in endothelial cells
CC undergoing capillary morphogenesis. {ECO:0000269|PubMed:16202431}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; AF378760; AAL11997.1; -; mRNA.
DR EMBL; AK010361; BAB26881.1; -; mRNA.
DR EMBL; AK036144; BAC29318.1; -; mRNA.
DR EMBL; AK153684; BAE32144.1; -; mRNA.
DR EMBL; AL591209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466556; EDL16106.1; -; Genomic_DNA.
DR EMBL; BC114352; AAI14353.1; -; mRNA.
DR CCDS; CCDS25333.1; -. [Q91ZV7-1]
DR CCDS; CCDS48897.1; -. [Q91ZV7-2]
DR RefSeq; NP_001157080.1; NM_001163608.1. [Q91ZV7-2]
DR RefSeq; NP_082475.3; NM_028199.3. [Q91ZV7-1]
DR AlphaFoldDB; Q91ZV7; -.
DR IntAct; Q91ZV7; 1.
DR MINT; Q91ZV7; -.
DR STRING; 10090.ENSMUSP00000103191; -.
DR GlyGen; Q91ZV7; 6 sites.
DR iPTMnet; Q91ZV7; -.
DR PhosphoSitePlus; Q91ZV7; -.
DR MaxQB; Q91ZV7; -.
DR PaxDb; Q91ZV7; -.
DR PeptideAtlas; Q91ZV7; -.
DR PRIDE; Q91ZV7; -.
DR ProteomicsDB; 289929; -. [Q91ZV7-1]
DR ProteomicsDB; 289930; -. [Q91ZV7-2]
DR Antibodypedia; 2551; 357 antibodies from 29 providers.
DR DNASU; 72324; -.
DR Ensembl; ENSMUST00000017561; ENSMUSP00000017561; ENSMUSG00000017417. [Q91ZV7-1]
DR Ensembl; ENSMUST00000107565; ENSMUSP00000103191; ENSMUSG00000017417. [Q91ZV7-2]
DR GeneID; 72324; -.
DR KEGG; mmu:72324; -.
DR UCSC; uc007lfc.2; mouse. [Q91ZV7-1]
DR UCSC; uc011ydx.1; mouse. [Q91ZV7-2]
DR CTD; 57125; -.
DR MGI; MGI:1919574; Plxdc1.
DR VEuPathDB; HostDB:ENSMUSG00000017417; -.
DR eggNOG; KOG3848; Eukaryota.
DR GeneTree; ENSGT00440000033408; -.
DR HOGENOM; CLU_029494_3_1_1; -.
DR InParanoid; Q91ZV7; -.
DR OMA; GFLFMGD; -.
DR OrthoDB; 1361987at2759; -.
DR PhylomeDB; Q91ZV7; -.
DR TreeFam; TF314400; -.
DR BioGRID-ORCS; 72324; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Plxdc1; mouse.
DR PRO; PR:Q91ZV7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91ZV7; protein.
DR Bgee; ENSMUSG00000017417; Expressed in motor neuron and 129 other tissues.
DR ExpressionAtlas; Q91ZV7; baseline and differential.
DR Genevisible; Q91ZV7; MM.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:InterPro.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR031152; PLXDC.
DR InterPro; IPR031153; PLXDC1.
DR PANTHER; PTHR13055; PTHR13055; 1.
DR PANTHER; PTHR13055:SF10; PTHR13055:SF10; 1.
DR Pfam; PF01437; PSI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Signal; Tight junction; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..500
FT /note="Plexin domain-containing protein 1"
FT /id="PRO_0000232752"
FT TOPO_DOM 20..426
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 22..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 86
FT /note="V -> VALSLSPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017975"
FT CONFLICT 104
FT /note="Q -> R (in Ref. 5; AAI14353)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="S -> P (in Ref. 5; AAI14353)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="A -> E (in Ref. 1; AAL11997 and 5; AAI14353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 55635 MW; 802D6865F8CA18BD CRC64;
MRAQLWLLQL LLLRGAARAL SPATPAGHNE GQDSAWTAKR TRQGWSRRPR ESPAQVLKPG
KTQLSQDLGG GSLAIDTLPD NRTRVVEDNH NYYVSRVYGP GEKQSQDLWV DLAVANRSHV
KIHRILSSSH RQASRVVLSF DFPFYGHPLR QITIATGGFI FMGDMLHRML TATQYVAPLM
ANFNPGYSDN STVAYFDNGT VFVVQWDHVY LQDREDRGSF TFQAALHRDG RIVFGYKEIP
MAVLDISSAQ HPVKAGLSDA FMILNSSPEV PASQRRTIFE YHRVELDSSK ITTTSAVEFT
PLPTCLQHQS CDTCVSSNLT FNCSWCHVLQ RCSSGFDRYR QEWLTYGCAQ EAEGKTCEDF
QDDSHYSASP DSSFSPFNGD STTSSSLFID SLTTEDDTKL NPYAEGDGLP DHSSPKSKGP
PVHLGTIVGI VLAVLLVAAI ILAGIYISGH PNSNAALFFI ERRPHHWPAM KFHNHPNHST
YTEVEPSGHE KEGFVEAEQC
