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   24-JAN-2024, entry version 155.
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}.
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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   GlyCosmos; Q91V98; 30 sites, No reported glycans.
DR   GlyGen; Q91V98; 30 sites.
DR   iPTMnet; Q91V98; -.
DR   PhosphoSitePlus; Q91V98; -.
DR   SwissPalm; Q91V98; -.
DR   CPTAC; non-CPTAC-3350; -.
DR   jPOST; Q91V98; -.
DR   MaxQB; Q91V98; -.
DR   PaxDb; 10090-ENSMUSP00000070847; -.
DR   PeptideAtlas; Q91V98; -.
DR   ProteomicsDB; 281349; -.
DR   Pumba; Q91V98; -.
DR   Antibodypedia; 30126; 432 antibodies from 38 providers.
DR   DNASU; 70445; -.
DR   Ensembl; ENSMUST00000070630.8; ENSMUSP00000070847.7; ENSMUSG00000056481.8.
DR   GeneID; 70445; -.
DR   KEGG; mmu:70445; -.
DR   UCSC; uc008gcb.1; mouse.
DR   AGR; MGI:1917695; -.
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; APNKRIT; -.
DR   OrthoDB; 19806at2759; -.
DR   PhylomeDB; Q91V98; -.
DR   TreeFam; TF330714; -.
DR   BioGRID-ORCS; 70445; 5 hits in 77 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 187 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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   CDD; cd03600; CLECT_thrombomodulin_like; 1.
DR   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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   PANTHER; PTHR14789; CHONDROLECTIN VARIANT CHODLFDELTAE; 1.
DR   PANTHER; PTHR14789:SF4; ENDOSIALIN; 1.
DR   Pfam; PF14670; FXa_inhibition; 1.
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; C-type lectin-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   Genevisible; Q91V98; MM.
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
//