位置:首页 > 蛋白库 > PXDC2_MOUSE
PXDC2_MOUSE
ID   PXDC2_MOUSE             Reviewed;         530 AA.
AC   Q9DC11; Q6PET5; Q91ZV6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 130.
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;
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], FUNCTION, 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].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Lung;
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 MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary gland;
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   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC   and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May play a role in tumor angiogenesis.
CC       {ECO:0000269|PubMed:11559528}.
CC   -!- SUBUNIT: Interacts with CTTN. {ECO:0000269|PubMed:15574754}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in tumor endothelium and in vessels of
CC       some normal tissues, such as the muscle and lung.
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; AF378761; AAL11998.1; -; mRNA.
DR   EMBL; AK004640; BAB23431.1; -; mRNA.
DR   EMBL; AK154921; BAE32927.1; -; mRNA.
DR   EMBL; BC057881; AAH57881.1; -; mRNA.
DR   CCDS; CCDS15705.1; -.
DR   RefSeq; NP_080438.2; NM_026162.6.
DR   AlphaFoldDB; Q9DC11; -.
DR   BioGRID; 212194; 3.
DR   STRING; 10090.ENSMUSP00000028081; -.
DR   GlyGen; Q9DC11; 2 sites.
DR   iPTMnet; Q9DC11; -.
DR   PhosphoSitePlus; Q9DC11; -.
DR   CPTAC; non-CPTAC-3935; -.
DR   EPD; Q9DC11; -.
DR   jPOST; Q9DC11; -.
DR   MaxQB; Q9DC11; -.
DR   PaxDb; Q9DC11; -.
DR   PeptideAtlas; Q9DC11; -.
DR   PRIDE; Q9DC11; -.
DR   ProteomicsDB; 301928; -.
DR   Antibodypedia; 25453; 172 antibodies from 31 providers.
DR   DNASU; 67448; -.
DR   Ensembl; ENSMUST00000028081; ENSMUSP00000028081; ENSMUSG00000026748.
DR   GeneID; 67448; -.
DR   KEGG; mmu:67448; -.
DR   UCSC; uc008ikz.2; mouse.
DR   CTD; 84898; -.
DR   MGI; MGI:1914698; Plxdc2.
DR   VEuPathDB; HostDB:ENSMUSG00000026748; -.
DR   eggNOG; KOG3848; Eukaryota.
DR   GeneTree; ENSGT00440000033408; -.
DR   InParanoid; Q9DC11; -.
DR   OMA; XIPVLVT; -.
DR   OrthoDB; 1361987at2759; -.
DR   PhylomeDB; Q9DC11; -.
DR   TreeFam; TF314400; -.
DR   BioGRID-ORCS; 67448; 0 hits in 71 CRISPR screens.
DR   ChiTaRS; Plxdc2; mouse.
DR   PRO; PR:Q9DC11; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9DC11; protein.
DR   Bgee; ENSMUSG00000026748; Expressed in vestibular membrane of cochlear duct and 254 other tissues.
DR   ExpressionAtlas; Q9DC11; baseline and differential.
DR   Genevisible; Q9DC11; MM.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
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   Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..530
FT                   /note="Plexin domain-containing protein 2"
FT                   /id="PRO_0000234575"
FT   TOPO_DOM        31..455
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        477..530
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          327..372
FT                   /note="PSI"
FT   REGION          378..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         507
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        5
FT                   /note="R -> W (in Ref. 3; AAH57881)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26
FT                   /note="Q -> H (in Ref. 1; AAL11998)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   530 AA;  59616 MW;  FB956C020735E36D CRC64;
     MARFRRADLA AAGVMLLCHF LTDRFQFAHG EPGHHTNDWI YEVTNAFPWN EEGVEVDSQA
     YNHRWKRNVD PFKAVDTNRA SMGQASPESK GFTDLLLDDG QDNNTQIEED TDHNYYISRI
     YGPADSASRD LWVNIDQMEK DKVKIHGILS NTHRQAARVN LSFDFPFYGH FLNEVTVATG
     GFIYTGEVVH RMLTATQYIA PLMANFDPSV SRNSTVRYFD NGTALVVQWD HVHLQDNYNL
     GSFTFQATLL MDGRIIFGYK EIPVLVTQIS STNHPVKVGL SDAFVVVHRI QQIPNVRRRT
     IYEYHRVELQ MSKITNISAV EMTPLPTCLQ FNGCGPCVSS QIGFNCSWCS KLQRCSSGFD
     RHRQDWVDSG CPEEVQSKEK MCEKTEPGET SQTTTTSHTT TMQFRVLTTT RRAVTSQMPT
     SLPTEDDTKI ALHLKDSGAS TDDSAAEKKG GTLHAGLIVG ILILVLIIAA AILVTVYMYH
     HPTSAASIFF IERRPSRWPA MKFRRGSGHP AYAEVEPVGE KEGFIVSEQC
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024