CD248_MOUSE
ID CD248_MOUSE Reviewed; 765 AA.
AC Q91V98; Q3UMV6; Q91ZV1;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Endosialin;
DE AltName: Full=Tumor endothelial marker 1;
DE AltName: CD_antigen=CD248;
DE Flags: Precursor;
GN Name=Cd248; Synonyms=Tem1;
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].
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 [GENOMIC DNA / MRNA], DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, AND FUNCTION.
RC STRAIN=129S6/SvEvTac; TISSUE=Spleen, and Thymus;
RX PubMed=11489895; DOI=10.1074/jbc.m105241200;
RA Opavsky R., Haviernik P., Jurkovicova D., Garin M.T., Copeland N.G.,
RA Gilbert D.J., Jenkins N.A., Bies J., Garfield S., Pastorekova S., Oue A.,
RA Wolff L.;
RT "Molecular characterization of the mouse Tem1/endosialin gene regulated by
RT cell density in vitro and expressed in normal tissues in vivo.";
RL J. Biol. Chem. 276:38795-38807(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
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 angiogenesis or vascular function.
CC {ECO:0000269|PubMed:11489895}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in cell lines derived from endothelial
CC cells, embryonic fibroblasts and preadipocytes.
CC {ECO:0000269|PubMed:11489895}.
CC -!- DEVELOPMENTAL STAGE: Detected at 19 dpc in embryo.
CC {ECO:0000269|PubMed:11489895}.
CC -!- PTM: O-glycosylated by sialylated oligosaccharides. {ECO:0000250}.
CC -!- PTM: May be N-glycosylated. {ECO:0000250}.
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; AF378758; AAL11995.1; -; mRNA.
DR EMBL; AF388572; AAK84664.1; -; mRNA.
DR EMBL; AF388573; AAK84665.1; -; Genomic_DNA.
DR EMBL; AK144655; BAE25992.1; -; mRNA.
DR EMBL; BC046318; AAH46318.1; -; mRNA.
DR CCDS; CCDS29448.1; -.
DR RefSeq; NP_473383.1; NM_054042.2.
DR AlphaFoldDB; Q91V98; -.
DR SMR; Q91V98; -.
DR BioGRID; 214055; 4.
DR STRING; 10090.ENSMUSP00000070847; -.
DR GlyGen; Q91V98; 30 sites.
DR iPTMnet; Q91V98; -.
DR PhosphoSitePlus; Q91V98; -.
DR CPTAC; non-CPTAC-3350; -.
DR jPOST; Q91V98; -.
DR MaxQB; Q91V98; -.
DR PaxDb; Q91V98; -.
DR PeptideAtlas; Q91V98; -.
DR PRIDE; Q91V98; -.
DR ProteomicsDB; 281349; -.
DR Antibodypedia; 30126; 380 antibodies from 38 providers.
DR DNASU; 70445; -.
DR Ensembl; ENSMUST00000070630; ENSMUSP00000070847; ENSMUSG00000056481.
DR GeneID; 70445; -.
DR KEGG; mmu:70445; -.
DR UCSC; uc008gcb.1; mouse.
DR CTD; 57124; -.
DR MGI; MGI:1917695; Cd248.
DR VEuPathDB; HostDB:ENSMUSG00000056481; -.
DR eggNOG; ENOG502QQKI; Eukaryota.
DR GeneTree; ENSGT00940000162405; -.
DR HOGENOM; CLU_027075_0_0_1; -.
DR InParanoid; Q91V98; -.
DR OMA; NWAQPAT; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; Q91V98; -.
DR TreeFam; TF330714; -.
DR BioGRID-ORCS; 70445; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Cd248; mouse.
DR PRO; PR:Q91V98; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91V98; protein.
DR Bgee; ENSMUSG00000056481; Expressed in external carotid artery and 186 other tissues.
DR Genevisible; Q91V98; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:1990430; F:extracellular matrix protein binding; IBA:GO_Central.
DR GO; GO:0060033; P:anatomical structure regression; IMP:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0072577; P:endothelial cell apoptotic process; IMP:MGI.
DR GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0048535; P:lymph node development; IMP:MGI.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IMP:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; EGF-like domain; Glycoprotein; Lectin; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..765
FT /note="Endosialin"
FT /id="PRO_0000045800"
FT TOPO_DOM 18..695
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 696..716
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 717..765
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..156
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 162..232
FT /note="Sushi"
FT DOMAIN 312..351
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255"
FT REGION 548..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..632
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 401
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 639
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 673
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT DISULFID 131..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 164..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 203..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 316..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 322..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 337..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 525
FT /note="S -> P (in Ref. 2; AAK84664)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="P -> T (in Ref. 3; BAE25992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 765 AA; 81813 MW; 572A06CC15BC8CD8 CRC64;
MLLRLLLAWV AAVPALGQVP WTPEPRAACG PSSCYALFPR RRTFLEAWRA CRELGGNLAT
PRTPEEAQRV DSLVGVGPAN GLLWIGLQRQ ARQCQPQRPL RGFIWTTGDQ DTAFTNWAQP
ATEGPCPAQR CAALEASGEH RWLEGSCTLA VDGYLCQFGF EGACPALPLE VGQAGPAVYT
TPFNLVSSEF EWLPFGSVAA VQCQAGRGAS LLCVKQPSGG VGWSQTGPLC PGTGCGPDNG
GCEHECVEEV DGAVSCRCSE GFRLAADGHS CEDPCAQAPC EQQCEPGGPQ GYSCHCRLGF
RPAEDDPHRC VDTDECQIAG VCQQMCVNYV GGFECYCSEG HELEADGISC SPAGAMGAQA
SQDLRDELLD DGEEGEDEEE PWEDFDGTWT EEQGILWLAP THPPDFGLPY RPNFPQDGEP
QRLHLEPTWP PPLSAPRGPY HSSVVSATRP MVISATRPTL PSAHKTSVIS ATRPPLSPVH
PPAMAPATPP AVFSEHQIPK IKANYPDLPF GHKPGITSAT HPARSPPYQP PIISTNYPQV
FPPHQAPMSP DTHTITYLPP VPPHLDPGDT TSKAHQHPLL PDAPGIRTQA PQLSVSALQP
PLPTNSRSSV HETPVPAANQ PPAFPSSPLP PQRPTNQTSS ISPTHSYSRA PLVPREGVPS
PKSVPQLPSV PSTAAPTALA ESGLAGQSQR DDRWLLVALL VPTCVFLVVL LALGIVYCTR
CGSHAPNKRI TDCYRWVTHA GNKSSTEPMP PRGSLTGVQT CRTSV
