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Deleted in malignant brain tumors 1 protein (Apactin) (CRP-ductin) (Glycoprotein 300) (gp300) (Hensin) (Mucin-like glycoprotein) (Muclin) (Vomeroglandin) (p80)

 DMBT1_MOUSE             Reviewed;        2085 AA.
Q60997; Q80YC6; Q9JMJ9;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
10-JAN-2006, sequence version 2.
22-NOV-2017, entry version 138.
RecName: Full=Deleted in malignant brain tumors 1 protein;
AltName: Full=Apactin;
AltName: Full=CRP-ductin;
AltName: Full=Glycoprotein 300;
Short=gp300;
AltName: Full=Hensin;
AltName: Full=Mucin-like glycoprotein;
Short=Muclin;
AltName: Full=Vomeroglandin;
AltName: Full=p80;
Flags: Precursor;
Name=Dmbt1; Synonyms=Crpd;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION IN EPITHELIAL
DIFFERENTIATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
STRAIN=BALB/cJ; TISSUE=Jejunal epithelium;
PubMed=8742698;
DOI=10.1002/(SICI)1097-0185(199603)244:3<327::AID-AR5>3.3.CO;2-A;
Cheng H., Bjerknes M., Chen H.;
"CRP-ductin: a gene expressed in intestinal crypts and in pancreatic
and hepatic ducts.";
Anat. Rec. 244:327-343(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PROTEIN SEQUENCE OF 22-40 AND
1942-1957, AND TISSUE SPECIFICITY.
STRAIN=ddY;
PubMed=10679193; DOI=10.1006/bbrc.2000.2104;
Matsushita F., Miyawaki A., Mikoshiba K.;
"Vomeroglandin/CRP-ductin is strongly expressed in the glands
associated with the mouse vomeronasal organ: identification and
characterization of mouse vomeroglandin.";
Biochem. Biophys. Res. Commun. 268:275-281(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=FVB/N; TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=7876332; DOI=10.1002/jcb.240560315;
De Lisle R.C.;
"Characterization of the major sulfated protein of mouse pancreatic
acinar cells: a high molecular weight peripheral membrane glycoprotein
of zymogen granules.";
J. Cell. Biochem. 56:385-396(1994).
[5]
TISSUE SPECIFICITY.
PubMed=7537458;
De Lisle R.C.;
"Increased expression of sulfated gp300 and acinar tissue pathology in
pancreas of CFTR(-/-) mice.";
Am. J. Physiol. 268:G717-G723(1995).
[6]
DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
PubMed=8543783; DOI=10.1177/44.1.8543783;
De Lisle R.C., Isom K.S.;
"Expression of sulfated gp300 and changes in glycosylation during
pancreatic development.";
J. Histochem. Cytochem. 44:57-66(1996).
[7]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9247472;
De Lisle R.C., Petitt M., Huff J., Isom K.S., Agbas A.;
"Muclin expression in the cystic fibrosis transmembrane conductance
regulator knockout mouse.";
Gastroenterology 113:521-532(1997).
[8]
TISSUE SPECIFICITY.
PubMed=9688648;
De Lisle R.C., Petitt M., Isom K.S., Ziemer D.;
"Developmental expression of a mucinlike glycoprotein (MUCLIN) in
pancreas and small intestine of CF mice.";
Am. J. Physiol. 275:G219-G227(1998).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11152281; DOI=10.1078/0171-9335-00121;
De Lisle R.C., Ziemer D.;
"Processing of pro-muclin and divergent trafficking of its products to
zymogen granules and the apical plasma membrane of pancreatic acinar
cells.";
Eur. J. Cell Biol. 79:892-904(2000).
[10]
FUNCTION.
PubMed=12082154;
De Lisle R.C.;
"Role of sulfated O-linked glycoproteins in zymogen granule
formation.";
J. Cell Sci. 115:2941-2952(2002).
[11]
FUNCTION, INTERACTION WITH SFTPD, AND TISSUE SPECIFICITY.
PubMed=12884308; DOI=10.1002/eji.200323972;
Madsen J., Tornoee I., Nielsen O., Lausen M., Krebs I.,
Mollenhauer J., Kollender G., Poustka A., Skjodt K., Holmskov U.;
"CRP-ductin, the mouse homologue of gp-340/deleted in malignant brain
tumors 1 (DMBT1), binds gram-positive and gram-negative bacteria and
interacts with lung surfactant protein D.";
Eur. J. Immunol. 33:2327-2336(2003).
[12]
FUNCTION, PHOSPHORYLATION AT THR-2073 AND SER-2082, AND MUTAGENESIS OF
THR-2073 AND SER-2082.
PubMed=15146979; DOI=10.1078/0171-9335-00361;
Tandon C., De Lisle R.C.;
"Apactin is involved in remodeling of the actin cytoskeleton during
regulated exocytosis.";
Eur. J. Cell Biol. 83:79-89(2004).
[13]
FUNCTION.
PubMed=15292166; DOI=10.1074/jbc.M406213200;
Boulatnikov I., De Lisle R.C.;
"Binding of the Golgi sorting receptor muclin to pancreatic zymogens
through sulfated O-linked oligosaccharides.";
J. Biol. Chem. 279:40918-40926(2004).
[14]
DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=15452149; DOI=10.1083/jcb.200405159;
Takito J., Al-Awqati Q.;
"Conversion of ES cells to columnar epithelia by hensin and to
squamous epithelia by laminin.";
J. Cell Biol. 166:1093-1102(2004).
[15]
FUNCTION.
PubMed=15987769; DOI=10.1152/ajpcell.00099.2005;
De Lisle R.C., Norkina O., Roach E., Ziemer D.;
"Expression of pro-muclin in pancreatic AR42J cells induces functional
regulated secretory granules.";
Am. J. Physiol. 289:C1169-C1178(2005).
[16]
DISRUPTION PHENOTYPE.
PubMed=17983803; DOI=10.1053/j.gastro.2007.08.007;
Renner M., Bergmann G., Krebs I., End C., Lyer S., Hilberg F.,
Helmke B., Gassler N., Autschbach F., Bikker F.,
Strobel-Freidekind O., Gronert-Sum S., Benner A., Blaich S.,
Wittig R., Hudler M., Ligtenberg A.J., Madsen J., Holmskov U.,
Annese V., Latiano A., Schirmacher P., Amerongen A.V.N., D'Amato M.,
Kioschis P., Hafner M., Poustka A., Mollenhauer J.;
"DMBT1 confers mucosal protection in vivo and a deletion variant is
associated with Crohn's disease.";
Gastroenterology 133:1499-1509(2007).
[17]
DISRUPTION PHENOTYPE.
PubMed=18202109; DOI=10.1152/ajpgi.00525.2007;
De Lisle R.C., Xu W., Roe B.A., Ziemer D.;
"Effects of muclin (Dmbt1) deficiency on the gastrointestinal
system.";
Am. J. Physiol. 294:G717-G727(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: May play roles in mucosal defense system and cellular
immune defense. May play a role in liver regeneration. May be an
important factor in fate decision and differentiation of transit-
amplifying ductular (oval) cells within the hepatic lineage. May
function as a binding protein in saliva for the regulation of
taste sensation. May play a role as an opsonin receptor for SFTPD
and SPAR in macrophage tissues throughout the body, including
epithelial cells lining the gastrointestinal tract (By
similarity). Required for terminal differentiation of columnar
epithelial cells during early embryogenesis. Displays a broad
calcium-dependent binding spectrum against both Gram-positive and
Gram-negative bacteria, suggesting a role in defense against
bacterial pathogens. Binds to a range of poly-sulfated and poly-
phosphorylated ligands which may explain its broad bacterial-
binding specificity. Inhibits cytoinvasion of S.enterica.
Associates with the actin cytoskeleton and is involved in its
remodeling during regulated exocytosis. Interacts with pancreatic
zymogens in a pH-dependent manner and may act as a Golgi cargo
receptor in the regulated secretory pathway of the pancreatic
acinar cell. {ECO:0000250, ECO:0000269|PubMed:11152281,
ECO:0000269|PubMed:12082154, ECO:0000269|PubMed:12884308,
ECO:0000269|PubMed:15146979, ECO:0000269|PubMed:15292166,
ECO:0000269|PubMed:15452149, ECO:0000269|PubMed:15987769,
ECO:0000269|PubMed:8742698}.
-!- SUBUNIT: Interacts with LGALS3. Binds SPAR in a calcium-dependent
manner (By similarity). Binds SFTPD in a calcium-dependent manner.
{ECO:0000250, ECO:0000269|PubMed:12884308}.
-!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory
vesicle membrane; Single-pass membrane protein; Lumenal side.
Note=Localized to the lumenal aspect of crypt cells in the small
intestine. In the colon, seen in the lumenal aspect of surface
epithelial cells. Formed in the ducts of von Ebner gland and
released into the fluid bathing the taste buds contained in the
taste papillae. In the CFTR knockout mouse, enhanced on the acinar
luminar surface.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=CPR-ductin alpha;
IsoId=Q60997-1; Sequence=Displayed;
Name=2; Synonyms=CPR-ductin beta;
IsoId=Q60997-2; Sequence=VSP_016853;
Name=3;
IsoId=Q60997-3; Sequence=VSP_016851, VSP_016852;
Name=4;
IsoId=Q60997-4; Sequence=VSP_016852;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Strongly expressed in acini and duct
epithelial cells of the exocrine pancreas but not in the islets of
Langerhans. Expressed in gall bladder, salivary glands and in the
epithelium lining larger hepatic ducts, but not in the liver
parenchyma, stomach or lung. Expressed along the intestinal tract
including duodenum, jejunum, ileum and colon (at protein level).
Expressed in glands associated with vomeronasal tissues. Expressed
in the vomeronasal gland and posterior gland of nasal septum.
Weakly expressed in lateral nasal gland. CFTR knockout mice show
increased expression in pancreas, duodenum and small intestine but
not in gall bladder. In pancreas and small intestine, increased
expression occurs after the appearance of dilated lumina.
{ECO:0000269|PubMed:10679193, ECO:0000269|PubMed:12884308,
ECO:0000269|PubMed:7537458, ECO:0000269|PubMed:8742698,
ECO:0000269|PubMed:9247472, ECO:0000269|PubMed:9688648}.
-!- DEVELOPMENTAL STAGE: Present in the E3.5 blastocyst. Levels
increase to a maximum between E18.5 and birth and decrease
gradually between birth and adulthood with the greatest decreases
occurring between neonate and P1 and between P9 and P16 (at
protein level). Expressed in the primitive endoderm at E4.5. At
E9.5, expressed in midbrain, notochord, liver primordium, midgut
and hindgut. {ECO:0000269|PubMed:15452149,
ECO:0000269|PubMed:8543783}.
-!- DOMAIN: The SRCR domains mediate binding to bacteria.
{ECO:0000250}.
-!- PTM: Highly N- and O-glycosylated. The O-glycans are heavily
sulfated. O-glycosylation and sulfation in pancreatic acinar cells
are required for zymogen granule maturation. Glycoconjugate
composition changes during development with fucose only acquired
post-natally during weaning. {ECO:0000269|PubMed:7876332,
ECO:0000269|PubMed:8543783}.
-!- DISRUPTION PHENOTYPE: Variable phenotypes have been reported. In
some studies mice display normal development and viability with
impaired exocrine pancreatic function and no development of
gastrointestinal tumors (PubMed:17983803 and PubMed:18202109). In
other studies mice die between E4.5 and E5.5 due to defects in the
differentiation of the primitive endoderm layer (PubMed:15452149).
{ECO:0000269|PubMed:15452149, ECO:0000269|PubMed:17983803,
ECO:0000269|PubMed:18202109}.
-!- SIMILARITY: Belongs to the DMBT1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC52505.1; Type=Frameshift; Positions=227, 233, 236, 240; Evidence={ECO:0000305};
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EMBL; U37438; AAC52505.1; ALT_FRAME; mRNA.
EMBL; AB005909; BAA92266.1; -; mRNA.
EMBL; BC049835; AAH49835.1; -; mRNA.
PIR; T42721; T42721.
RefSeq; NP_001334561.1; NM_001347632.1.
RefSeq; NP_031795.2; NM_007769.2.
UniGene; Mm.4138; -.
ProteinModelPortal; Q60997; -.
SMR; Q60997; -.
STRING; 10090.ENSMUSP00000081556; -.
iPTMnet; Q60997; -.
PhosphoSitePlus; Q60997; -.
PaxDb; Q60997; -.
PRIDE; Q60997; -.
GeneID; 12945; -.
KEGG; mmu:12945; -.
CTD; 1755; -.
MGI; MGI:106210; Dmbt1.
eggNOG; ENOG410IHBC; Eukaryota.
eggNOG; ENOG410XQVR; LUCA.
HOGENOM; HOG000290652; -.
HOVERGEN; HBG060122; -.
InParanoid; Q60997; -.
KO; K13912; -.
PhylomeDB; Q60997; -.
PRO; PR:Q60997; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_DMBT1; -.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0030670; C:phagocytic vesicle membrane; ISO:MGI.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0042589; C:zymogen granule membrane; IDA:UniProtKB.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0035375; F:zymogen binding; IDA:UniProtKB.
GO; GO:0001824; P:blastocyst development; IMP:MGI.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0001833; P:inner cell mass cell proliferation; IDA:MGI.
GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IDA:MGI.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
CDD; cd00041; CUB; 5.
Gene3D; 2.60.120.290; -; 5.
InterPro; IPR000859; CUB_dom.
InterPro; IPR035914; Sperma_CUB_dom_sf.
InterPro; IPR001190; SRCR.
InterPro; IPR017448; SRCR-like_dom.
InterPro; IPR036772; SRCR-like_dom_sf.
InterPro; IPR001507; ZP_dom.
InterPro; IPR017977; ZP_dom_CS.
Pfam; PF00431; CUB; 5.
Pfam; PF00530; SRCR; 8.
Pfam; PF00100; Zona_pellucida; 1.
PRINTS; PR00258; SPERACTRCPTR.
SMART; SM00042; CUB; 5.
SMART; SM00202; SR; 8.
SMART; SM00241; ZP; 1.
SUPFAM; SSF49854; SSF49854; 5.
SUPFAM; SSF56487; SSF56487; 8.
PROSITE; PS01180; CUB; 5.
PROSITE; PS00420; SRCR_1; 8.
PROSITE; PS50287; SRCR_2; 8.
PROSITE; PS00682; ZP_1; 1.
PROSITE; PS51034; ZP_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasmic vesicle;
Developmental protein; Differentiation; Direct protein sequencing;
Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
Protein transport; Reference proteome; Repeat; Secreted; Signal;
Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 2085 Deleted in malignant brain tumors 1
protein.
/FTId=PRO_0000045388.
TRANSMEM 2050 2070 Helical. {ECO:0000255}.
DOMAIN 37 137 SRCR 1. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 186 286 SRCR 2. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 324 424 SRCR 3. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 463 563 SRCR 4. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 602 702 SRCR 5. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 741 841 SRCR 6. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 880 980 SRCR 7. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 1023 1132 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1139 1248 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1265 1374 CUB 3. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1381 1490 CUB 4. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1510 1610 SRCR 8. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 1633 1742 CUB 5. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1751 1999 ZP. {ECO:0000255|PROSITE-
ProRule:PRU00375}.
COMPBIAS 987 1018 Thr-rich.
MOD_RES 2073 2073 Phosphothreonine.
{ECO:0000269|PubMed:15146979}.
MOD_RES 2082 2082 Phosphoserine.
{ECO:0000269|PubMed:15146979}.
CARBOHYD 1088 1088 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1100 1100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1136 1136 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1204 1204 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1216 1216 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1330 1330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1342 1342 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1378 1378 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1446 1446 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1458 1458 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1500 1500 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1504 1504 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1514 1514 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1630 1630 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1745 1745 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1746 1746 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1782 1782 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1813 1813 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1817 1817 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1858 1858 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1874 1874 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 62 126 {ECO:0000250}.
DISULFID 75 136 {ECO:0000250}.
DISULFID 106 116 {ECO:0000250}.
DISULFID 211 275 {ECO:0000250}.
DISULFID 224 285 {ECO:0000250}.
DISULFID 255 265 {ECO:0000250}.
DISULFID 349 413 {ECO:0000250}.
DISULFID 362 423 {ECO:0000250}.
DISULFID 393 403 {ECO:0000250}.
DISULFID 488 552 {ECO:0000250}.
DISULFID 501 562 {ECO:0000250}.
DISULFID 532 542 {ECO:0000250}.
DISULFID 627 691 {ECO:0000250}.
DISULFID 640 701 {ECO:0000250}.
DISULFID 671 681 {ECO:0000250}.
DISULFID 766 830 {ECO:0000250}.
DISULFID 779 840 {ECO:0000250}.
DISULFID 810 820 {ECO:0000250}.
DISULFID 905 969 {ECO:0000250}.
DISULFID 918 979 {ECO:0000250}.
DISULFID 949 959 {ECO:0000250}.
DISULFID 1023 1049 {ECO:0000250}.
DISULFID 1074 1096 {ECO:0000250}.
DISULFID 1139 1165 {ECO:0000250}.
DISULFID 1190 1212 {ECO:0000250}.
DISULFID 1265 1291 {ECO:0000250}.
DISULFID 1316 1338 {ECO:0000250}.
DISULFID 1381 1407 {ECO:0000250}.
DISULFID 1432 1454 {ECO:0000250}.
DISULFID 1535 1599 {ECO:0000250}.
DISULFID 1548 1609 {ECO:0000250}.
DISULFID 1579 1589 {ECO:0000250}.
DISULFID 1633 1659 {ECO:0000250}.
DISULFID 1684 1706 {ECO:0000250}.
DISULFID 1920 1978 {ECO:0000250}.
VAR_SEQ 29 29 D -> DEVSYTAEQSTE (in isoform 3).
{ECO:0000303|PubMed:10679193}.
/FTId=VSP_016851.
VAR_SEQ 397 534 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:10679193,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_016852.
VAR_SEQ 2032 2085 Missing (in isoform 2).
{ECO:0000303|PubMed:8742698}.
/FTId=VSP_016853.
MUTAGEN 2073 2073 T->A: Abolishes phosphorylation.
{ECO:0000269|PubMed:15146979}.
MUTAGEN 2082 2082 S->A: Abolishes phosphorylation.
{ECO:0000269|PubMed:15146979}.
CONFLICT 247 248 PI -> L (in Ref. 1; AAC52505).
{ECO:0000305}.
CONFLICT 1494 1497 PPSF -> SLH (in Ref. 1; AAC52505).
{ECO:0000305}.
CONFLICT 2061 2061 V -> G (in Ref. 2; BAA92266).
{ECO:0000305}.
SEQUENCE 2085 AA; 226815 MW; 8BE4E77D299B32ED CRC64;
MGISTVIFEI CLLWGQILST ASQTAVPTDG TDSGLAVRLV NGGDRCQGRV EILYQGSWGT
VCDDSWDLND ANVVCRQLGC GLAVSAPGNA RFGQGSGPIV MDDVACGGYE DYLWRCSHRG
WLSHNCGHQE DAGVICSDSQ TSSPTPGWWN PGGTNNDVFY PTEQTTAEQT TIPDYTPIGT
DSGLAVRLVN GGDRCQGRVE ILYQGSWGTV CDDSWDVSDA NVVCRQLGCG WAVSAPGNAY
FGQGQGPIVL DDVACGGYEN YLWSCSHQGW LSHNCGHQED AGVICSASQS SSPTPGWWNP
GGTNNDVFYP TEQTTAGTDS GLAVRLVNGG DRCQGRVEIL YQGSWGTVCD DSWDTNDANV
VCRQLGCGWA VSAPGNAYFG PGSGSIVLDD VACTGHEDYL WRCSHRGWLS HNCGHHEDAG
VICSASQSSS PTPDVFYPTD QTTAEQTTVP DYTPIGTDSG LAVRLVNGGD RCQGRVEILY
QGSWGTVCDD SWDLNDANVV CRQLGCGLAV SAPGSARFGQ GTGPIVMDDV ACGGYEDYLW
RCSHRGWLSH NCGHHEDAGV ICSASQSSSP TPDVFYPTDQ TTAEQTTVPD YTPIGTDSGL
AVRLVNGGDR CQGRVEILYQ GSWGTVCDDS WDLNDANVVC RQLGCGLAVS APGSARFGQG
TGPIVMDDVA CGGYEDYLWR CSHRGWLSHN CGHHEDAGVI CSASQSSSPT PDVFYPTDQT
TAEQTTVPDY TTIGTENSLA VRLENGGDRC QGRVEILYQG SWGTVCDDSW DLNDANVVCR
QLGCGLAVSA PGSARFGQGT GPIVMDDVAC GGYEDYLWRC SHRGWLSHNC GHHEDAGVIC
SASQSSSPTP DVFYPTDQTT VEQTTVPDYT PIGTENSLAV RLENGGDRCQ GRVEILYQGS
WGTVCDDSWD TKDANVVCRQ LGCGWAVSAP GNAYFGPGSG SIVLDDVACT GHEDYLWSCS
HRGWLSHNCG HHEDAGVICS DAQIQSTTRP DLWPTTTTPE TTTELLTTTP YFDWWTTTSD
YSCGGLLTQP SGQFSSPYYP SNYPNNARCS WKIVLPNMNR VTVVFTDVQL EGGCNYDYIL
VYDGPEYNSS LIARVCDGSN GSFTSTGNFM SVVFITDGSV TRRGFQAHYY STVSTNYSCG
GLLTQPSGQF SSPYYPSNYP NNARCSWEIL VPNMNRVTVV FTDVQLEGGC NYDYILVYDG
PQYNSSLIAR VCDGSNGSFT STGNFMSVVF ITDGSVTRRG FQAHYYSTVS TTPPVPIPTT
DDYSCGGLLT LPSGQFSSPH YPSNYPNNAR CSWEILVPNM NRVTVAFTDV QLEGGCNYDY
ILVYDGPEYN SSLIARVCDG SNGSFTSTGN FMSVVFITDG SVTRRGFQAH YYSTVSTNYS
CGGLLTQPSG QFSSPHYPSN YPNNVRCSWE ILVPSMNRVT VAFTDVQLEG GCSFDYILVY
DGPEYNSSLI APVCDGFNGS FTSTGNFMSV VFITDGSVTR RGFQAYYYST VSTPPSFHPN
ITGNDSSLAL RLVNGSNRCE GRVEILYRGS WGTVCDDSWG ISDANVVCRQ LGCGSALSAP
GNAWFGQGSG LIVLDDVSCS GYESHLWNCH HPGWLVHNCR HSEDAGVICA LPEVTSPSPG
WWTTSPSYVN YTCGGFLTQP SGQFSSPFYP GNYPNNARCL WNIEVPNNYR VTVVFRDLQL
ERGCSYDYIE IFDGPHHSSP LIARVCDGSL GSFTSTSNFM SIRFITDHSI TARGFQAHYY
SDFDNNTTNL LCQSNHMQAS VSRSYLQSMG YSARDLVIPG WNSSYHCQPQ ITQREVIFTI
PYTGCGTIKQ ADNETINYSN FLRAVVSNGI IKRRKDLNIH VSCKMLQNTW VNTMYITNNT
VEIQEVQYGN FDVNISFYTS SSFLFPVTSS PYYVDLDQNL YLQAEILHSD ASLALFVDTC
VASPHPNDFS SLTYDLIRSG CVRDDTYQSY SSPSPRVSRF KFSSFHFLNR FPSVYLQCKL
VVCRAYDTSS RCYRGCVVRS KRDVGSYQEK VDVVLGPIQL QSPSKEKRSL DLAVEDVKKP
ASSQAVYPTA AIFGGVFLAM VLAVAAFTLG RRTHIDRGQP PSTKL


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