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Q91V98

- CD248_MOUSE

UniProt

Q91V98 - CD248_MOUSE

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Protein

Endosialin

Gene

Cd248

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

May play a role in angiogenesis or vascular function.1 Publication

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. carbohydrate binding Source: UniProtKB-KW
  3. extracellular matrix binding Source: MGI

GO - Biological processi

  1. anatomical structure regression Source: MGI
  2. cell migration Source: MGI
  3. lymph node development Source: MGI
  4. positive regulation of cell proliferation Source: MGI
  5. positive regulation of endothelial cell apoptotic process Source: MGI
Complete GO annotation...

Keywords - Ligandi

Calcium, Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Endosialin
Alternative name(s):
Tumor endothelial marker 1
CD_antigen: CD248
Gene namesi
Name:Cd248
Synonyms:Tem1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:1917695. Cd248.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. extracellular vesicular exosome Source: Ensembl
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 765748EndosialinPRO_0000045800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi131 ↔ 147PROSITE-ProRule annotation
Disulfide bondi164 ↔ 213PROSITE-ProRule annotation
Disulfide bondi203 ↔ 230PROSITE-ProRule annotation
Disulfide bondi316 ↔ 326PROSITE-ProRule annotation
Disulfide bondi322 ↔ 335PROSITE-ProRule annotation
Disulfide bondi337 ↔ 350PROSITE-ProRule annotation
Glycosylationi401 – 4011O-linked (GalNAc...)Sequence Analysis
Glycosylationi428 – 4281O-linked (GalNAc...)Sequence Analysis
Glycosylationi448 – 4481O-linked (GalNAc...)Sequence Analysis
Glycosylationi456 – 4561O-linked (GalNAc...)Sequence Analysis
Glycosylationi459 – 4591O-linked (GalNAc...)Sequence Analysis
Glycosylationi466 – 4661O-linked (GalNAc...)Sequence Analysis
Glycosylationi467 – 4671O-linked (GalNAc...)Sequence Analysis
Glycosylationi470 – 4701O-linked (GalNAc...)Sequence Analysis
Glycosylationi472 – 4721O-linked (GalNAc...)Sequence Analysis
Glycosylationi477 – 4771O-linked (GalNAc...)Sequence Analysis
Glycosylationi488 – 4881O-linked (GalNAc...)Sequence Analysis
Glycosylationi517 – 5171O-linked (GalNAc...)Sequence Analysis
Glycosylationi520 – 5201O-linked (GalNAc...)Sequence Analysis
Glycosylationi535 – 5351O-linked (GalNAc...)Sequence Analysis
Glycosylationi552 – 5521O-linked (GalNAc...)Sequence Analysis
Glycosylationi554 – 5541O-linked (GalNAc...)Sequence Analysis
Glycosylationi556 – 5561O-linked (GalNAc...)Sequence Analysis
Glycosylationi570 – 5701O-linked (GalNAc...)Sequence Analysis
Glycosylationi571 – 5711O-linked (GalNAc...)Sequence Analysis
Glycosylationi604 – 6041O-linked (GalNAc...)Sequence Analysis
Glycosylationi613 – 6131O-linked (GalNAc...)Sequence Analysis
Glycosylationi626 – 6261O-linked (GalNAc...)Sequence Analysis
Glycosylationi627 – 6271O-linked (GalNAc...)Sequence Analysis
Glycosylationi635 – 6351O-linked (GalNAc...)Sequence Analysis
Glycosylationi638 – 6381O-linked (GalNAc...)Sequence Analysis
Glycosylationi639 – 6391O-linked (GalNAc...)Sequence Analysis
Glycosylationi640 – 6401O-linked (GalNAc...)Sequence Analysis
Glycosylationi644 – 6441O-linked (GalNAc...)Sequence Analysis
Glycosylationi663 – 6631O-linked (GalNAc...)Sequence Analysis
Glycosylationi673 – 6731O-linked (GalNAc...)Sequence Analysis

Post-translational modificationi

O-glycosylated by sialylated oligosaccharides.By similarity
May be N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ91V98.
PRIDEiQ91V98.

PTM databases

PhosphoSiteiQ91V98.

Expressioni

Tissue specificityi

Expressed in cell lines derived from endothelial cells, embryonic fibroblasts and preadipocytes.1 Publication

Developmental stagei

Detected at E19 in embryo.1 Publication

Gene expression databases

BgeeiQ91V98.
CleanExiMM_CD248.
GenevestigatoriQ91V98.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070847.

Structurei

3D structure databases

ProteinModelPortaliQ91V98.
SMRiQ91V98. Positions 34-159, 242-357.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 695678ExtracellularSequence AnalysisAdd
BLAST
Topological domaini717 – 76549CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei696 – 71621HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 156127C-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini162 – 23271SushiAdd
BLAST
Domaini312 – 35140EGF-like; calcium-bindingSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi400 – 676277Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 1 EGF-like domain.Curated
Contains 1 Sushi (CCP/SCR) domain.Curated

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG147482.
GeneTreeiENSGT00530000063403.
HOGENOMiHOG000111482.
HOVERGENiHBG081065.
InParanoidiQ91V98.
KOiK06706.
OMAiEASGEHR.
OrthoDBiEOG7ZGX2D.
PhylomeDBiQ91V98.
TreeFamiTF330714.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view]
PfamiPF07645. EGF_CA. 1 hit.
PF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS01187. EGF_CA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91V98-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLRLLLAWV AAVPALGQVP WTPEPRAACG PSSCYALFPR RRTFLEAWRA
60 70 80 90 100
CRELGGNLAT PRTPEEAQRV DSLVGVGPAN GLLWIGLQRQ ARQCQPQRPL
110 120 130 140 150
RGFIWTTGDQ DTAFTNWAQP ATEGPCPAQR CAALEASGEH RWLEGSCTLA
160 170 180 190 200
VDGYLCQFGF EGACPALPLE VGQAGPAVYT TPFNLVSSEF EWLPFGSVAA
210 220 230 240 250
VQCQAGRGAS LLCVKQPSGG VGWSQTGPLC PGTGCGPDNG GCEHECVEEV
260 270 280 290 300
DGAVSCRCSE GFRLAADGHS CEDPCAQAPC EQQCEPGGPQ GYSCHCRLGF
310 320 330 340 350
RPAEDDPHRC VDTDECQIAG VCQQMCVNYV GGFECYCSEG HELEADGISC
360 370 380 390 400
SPAGAMGAQA SQDLRDELLD DGEEGEDEEE PWEDFDGTWT EEQGILWLAP
410 420 430 440 450
THPPDFGLPY RPNFPQDGEP QRLHLEPTWP PPLSAPRGPY HSSVVSATRP
460 470 480 490 500
MVISATRPTL PSAHKTSVIS ATRPPLSPVH PPAMAPATPP AVFSEHQIPK
510 520 530 540 550
IKANYPDLPF GHKPGITSAT HPARSPPYQP PIISTNYPQV FPPHQAPMSP
560 570 580 590 600
DTHTITYLPP VPPHLDPGDT TSKAHQHPLL PDAPGIRTQA PQLSVSALQP
610 620 630 640 650
PLPTNSRSSV HETPVPAANQ PPAFPSSPLP PQRPTNQTSS ISPTHSYSRA
660 670 680 690 700
PLVPREGVPS PKSVPQLPSV PSTAAPTALA ESGLAGQSQR DDRWLLVALL
710 720 730 740 750
VPTCVFLVVL LALGIVYCTR CGSHAPNKRI TDCYRWVTHA GNKSSTEPMP
760
PRGSLTGVQT CRTSV
Length:765
Mass (Da):81,813
Last modified:December 1, 2001 - v1
Checksum:i572A06CC15BC8CD8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti525 – 5251S → P in AAK84664. (PubMed:11489895)Curated
Sequence conflicti751 – 7511P → T in BAE25992. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF378758 mRNA. Translation: AAL11995.1.
AF388572 mRNA. Translation: AAK84664.1.
AF388573 Genomic DNA. Translation: AAK84665.1.
AK144655 mRNA. Translation: BAE25992.1.
BC046318 mRNA. Translation: AAH46318.1.
CCDSiCCDS29448.1.
RefSeqiNP_473383.1. NM_054042.2.
UniGeneiMm.29597.

Genome annotation databases

EnsembliENSMUST00000070630; ENSMUSP00000070847; ENSMUSG00000056481.
GeneIDi70445.
KEGGimmu:70445.
UCSCiuc008gcb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF378758 mRNA. Translation: AAL11995.1 .
AF388572 mRNA. Translation: AAK84664.1 .
AF388573 Genomic DNA. Translation: AAK84665.1 .
AK144655 mRNA. Translation: BAE25992.1 .
BC046318 mRNA. Translation: AAH46318.1 .
CCDSi CCDS29448.1.
RefSeqi NP_473383.1. NM_054042.2.
UniGenei Mm.29597.

3D structure databases

ProteinModelPortali Q91V98.
SMRi Q91V98. Positions 34-159, 242-357.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000070847.

PTM databases

PhosphoSitei Q91V98.

Proteomic databases

PaxDbi Q91V98.
PRIDEi Q91V98.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000070630 ; ENSMUSP00000070847 ; ENSMUSG00000056481 .
GeneIDi 70445.
KEGGi mmu:70445.
UCSCi uc008gcb.1. mouse.

Organism-specific databases

CTDi 57124.
MGIi MGI:1917695. Cd248.

Phylogenomic databases

eggNOGi NOG147482.
GeneTreei ENSGT00530000063403.
HOGENOMi HOG000111482.
HOVERGENi HBG081065.
InParanoidi Q91V98.
KOi K06706.
OMAi EASGEHR.
OrthoDBi EOG7ZGX2D.
PhylomeDBi Q91V98.
TreeFami TF330714.

Miscellaneous databases

ChiTaRSi CD248. mouse.
NextBioi 331635.
PROi Q91V98.
SOURCEi Search...

Gene expression databases

Bgeei Q91V98.
CleanExi MM_CD248.
Genevestigatori Q91V98.

Family and domain databases

Gene3Di 3.10.100.10. 1 hit.
InterProi IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view ]
Pfami PF07645. EGF_CA. 1 hit.
PF00059. Lectin_C. 1 hit.
[Graphical view ]
SMARTi SM00034. CLECT. 1 hit.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEi PS50041. C_TYPE_LECTIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS01187. EGF_CA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cell surface tumor endothelial markers are conserved in mice and humans."
    Carson-Walter E.B., Watkins D.N., Nanda A., Vogelstein B., Kinzler K.W., St Croix B.
    Cancer Res. 61:6649-6655(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular characterization of the mouse Tem1/endosialin gene regulated by cell density in vitro and expressed in normal tissues in vivo."
    Opavsky R., Haviernik P., Jurkovicova D., Garin M.T., Copeland N.G., Gilbert D.J., Jenkins N.A., Bies J., Garfield S., Pastorekova S., Oue A., Wolff L.
    J. Biol. Chem. 276:38795-38807(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, FUNCTION.
    Strain: 129S6/SvEvTac.
    Tissue: Spleen and Thymus.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Olfactory epithelium.

Entry informationi

Entry nameiCD248_MOUSE
AccessioniPrimary (citable) accession number: Q91V98
Secondary accession number(s): Q3UMV6, Q91ZV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3