Reviewed, UniProtKB/Swiss-Prot Q60997 (DMBT1_MOUSE)

Names and origin

Protein names

Recommended name:
    Deleted in malignant brain tumors 1 protein
Alternative name(s):
    CRP-ductin
    Vomeroglandin
    Hensin
    Mucin-like glycoprotein
      Short name=Muclin
    Glycoprotein 300
      Short name=gp300
    Apactin
    p80

Gene names

Name:	Dmbt1
Synonyms:	Crpd

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	2085 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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.
Subunit structure	Interacts with LGALS3. Binds SPAR in a calcium-dependent manner By similarity. Binds SFTPD in a calcium-dependent manner.
Subcellular location	Secreted. Cytoplasmic vesicle › secretory vesicle membrane; Peripheral 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.
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.
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.
Domain	The SRCR domains mediate binding to bacteria By similarity.
Post-translational modification	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.
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 (Ref.16 and Ref.17). In other studies mice die between E4.5 and E5.5 due to defects in the differentiation of the primitive endoderm layer (Ref.14).
Sequence similarities	Belongs to the DMBT1 family. Contains 5 CUB domains. Contains 8 SRCR domains. Contains 1 ZP domain.
Sequence caution	The sequence AAC52505.1 differs from that shown. Reason: Frameshift at positions 227, 233, 236 and 240.

Ontologies

Keywords
Biological process	Differentiation Protein transport Transport
Cellular component	Cytoplasmic vesicle Membrane Secreted
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal Transmembrane
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW inner cell mass cell proliferation Ref.14 Inferred from direct assay. Source: MGI positive regulation of epithelial cell differentiation Ref.14 Inferred from direct assay. Source: MGI
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW proteinaceous extracellular matrix Ref.14 Inferred from direct assay. Source: MGI zymogen granule membrane Inferred from direct assay. Source: UniProtKB
Molecular function	Gram-negative bacterial binding Inferred from direct assay. Source: UniProtKB Gram-positive bacterial binding Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB scavenger receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q60997-1)

Also known as: CPR-ductin alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q60997-2)

Also known as: CPR-ductin beta;

The sequence of this isoform differs from the canonical sequence as follows:
     2032-2085: Missing.

Isoform 3 (identifier: Q60997-3)

The sequence of this isoform differs from the canonical sequence as follows:
     29-29: D → DEVSYTAEQSTE
     397-534: Missing.

Isoform 4 (identifier: Q60997-4)

The sequence of this isoform differs from the canonical sequence as follows:
     397-534: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 2085	2066	Deleted in malignant brain tumors 1 protein		PRO_0000045388
Regions
	Transmembrane	2050 – 2070	21	Potential
	Domain	37 – 137	101	SRCR 1
	Domain	186 – 286	101	SRCR 2
	Domain	324 – 424	101	SRCR 3
	Domain	463 – 563	101	SRCR 4
	Domain	602 – 702	101	SRCR 5
	Domain	741 – 841	101	SRCR 6
	Domain	880 – 980	101	SRCR 7
	Domain	1023 – 1132	110	CUB 1
	Domain	1139 – 1248	110	CUB 2
	Domain	1265 – 1374	110	CUB 3
	Domain	1381 – 1490	110	CUB 4
	Domain	1510 – 1610	101	SRCR 8
	Domain	1633 – 1742	110	CUB 5
	Domain	1751 – 1999	249	ZP
	Compositional bias	987 – 1018	32	Thr-rich
Amino acid modifications
	Modified residue	2073	1	Phosphothreonine
	Modified residue	2082	1	Phosphoserine
	Glycosylation	1088	1	N-linked (GlcNAc...) Potential
	Glycosylation	1100	1	N-linked (GlcNAc...) Potential
	Glycosylation	1136	1	N-linked (GlcNAc...) Potential
	Glycosylation	1204	1	N-linked (GlcNAc...) Potential
	Glycosylation	1216	1	N-linked (GlcNAc...) Potential
	Glycosylation	1330	1	N-linked (GlcNAc...) Potential
	Glycosylation	1342	1	N-linked (GlcNAc...) Potential
	Glycosylation	1378	1	N-linked (GlcNAc...) Potential
	Glycosylation	1446	1	N-linked (GlcNAc...) Potential
	Glycosylation	1458	1	N-linked (GlcNAc...) Potential
	Glycosylation	1500	1	N-linked (GlcNAc...) Potential
	Glycosylation	1504	1	N-linked (GlcNAc...) Potential
	Glycosylation	1514	1	N-linked (GlcNAc...) Potential
	Glycosylation	1630	1	N-linked (GlcNAc...) Potential
	Glycosylation	1745	1	N-linked (GlcNAc...) Potential
	Glycosylation	1746	1	N-linked (GlcNAc...) Potential
	Glycosylation	1782	1	N-linked (GlcNAc...) Potential
	Glycosylation	1813	1	N-linked (GlcNAc...) Potential
	Glycosylation	1817	1	N-linked (GlcNAc...) Potential
	Glycosylation	1858	1	N-linked (GlcNAc...) Potential
	Glycosylation	1874	1	N-linked (GlcNAc...) Potential
	Disulfide bond	62 ↔ 126		By similarity
	Disulfide bond	75 ↔ 136		By similarity
	Disulfide bond	106 ↔ 116		By similarity
	Disulfide bond	211 ↔ 275		By similarity
	Disulfide bond	224 ↔ 285		By similarity
	Disulfide bond	255 ↔ 265		By similarity
	Disulfide bond	349 ↔ 413		By similarity
	Disulfide bond	362 ↔ 423		By similarity
	Disulfide bond	393 ↔ 403		By similarity
	Disulfide bond	488 ↔ 552		By similarity
	Disulfide bond	501 ↔ 562		By similarity
	Disulfide bond	532 ↔ 542		By similarity
	Disulfide bond	627 ↔ 691		By similarity
	Disulfide bond	640 ↔ 701		By similarity
	Disulfide bond	671 ↔ 681		By similarity
	Disulfide bond	766 ↔ 830		By similarity
	Disulfide bond	779 ↔ 840		By similarity
	Disulfide bond	810 ↔ 820		By similarity
	Disulfide bond	905 ↔ 969		By similarity
	Disulfide bond	918 ↔ 979		By similarity
	Disulfide bond	949 ↔ 959		By similarity
	Disulfide bond	1023 ↔ 1049		By similarity
	Disulfide bond	1074 ↔ 1096		By similarity
	Disulfide bond	1139 ↔ 1165		By similarity
	Disulfide bond	1190 ↔ 1212		By similarity
	Disulfide bond	1265 ↔ 1291		By similarity
	Disulfide bond	1316 ↔ 1338		By similarity
	Disulfide bond	1381 ↔ 1407		By similarity
	Disulfide bond	1432 ↔ 1454		By similarity
	Disulfide bond	1535 ↔ 1599		By similarity
	Disulfide bond	1548 ↔ 1609		By similarity
	Disulfide bond	1579 ↔ 1589		By similarity
	Disulfide bond	1633 ↔ 1659		By similarity
	Disulfide bond	1684 ↔ 1706		By similarity
Natural variations
	Alternative sequence	29	1	D → DEVSYTAEQSTE in isoform 3.		VSP_016851
	Alternative sequence	397 – 534	138	Missing in isoform 3 and isoform 4.		VSP_016852
	Alternative sequence	2032 – 2085	54	Missing in isoform 2.		VSP_016853
Experimental info
	Mutagenesis	2073	1	T → A: Abolishes phosphorylation.
	Mutagenesis	2082	1	S → A: Abolishes phosphorylation.
	Sequence conflict	247 – 248	2	PI → L in AAC52505. Ref.1
	Sequence conflict	1494 – 1497	4	PPSF → SLH in AAC52505. Ref.1
	Sequence conflict	2061	1	V → G in BAA92266. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CPR-ductin alpha) [UniParc]. Last modified January 10, 2006. Version 2. Checksum: 8BE4E77D299B32ED	FASTA	2,085	226,815
	10 20 30 40 50 60 MGISTVIFEI CLLWGQILST ASQTAVPTDG TDSGLAVRLV NGGDRCQGRV EILYQGSWGT 70 80 90 100 110 120 VCDDSWDLND ANVVCRQLGC GLAVSAPGNA RFGQGSGPIV MDDVACGGYE DYLWRCSHRG 130 140 150 160 170 180 WLSHNCGHQE DAGVICSDSQ TSSPTPGWWN PGGTNNDVFY PTEQTTAEQT TIPDYTPIGT 190 200 210 220 230 240 DSGLAVRLVN GGDRCQGRVE ILYQGSWGTV CDDSWDVSDA NVVCRQLGCG WAVSAPGNAY 250 260 270 280 290 300 FGQGQGPIVL DDVACGGYEN YLWSCSHQGW LSHNCGHQED AGVICSASQS SSPTPGWWNP 310 320 330 340 350 360 GGTNNDVFYP TEQTTAGTDS GLAVRLVNGG DRCQGRVEIL YQGSWGTVCD DSWDTNDANV 370 380 390 400 410 420 VCRQLGCGWA VSAPGNAYFG PGSGSIVLDD VACTGHEDYL WRCSHRGWLS HNCGHHEDAG 430 440 450 460 470 480 VICSASQSSS PTPDVFYPTD QTTAEQTTVP DYTPIGTDSG LAVRLVNGGD RCQGRVEILY 490 500 510 520 530 540 QGSWGTVCDD SWDLNDANVV CRQLGCGLAV SAPGSARFGQ GTGPIVMDDV ACGGYEDYLW 550 560 570 580 590 600 RCSHRGWLSH NCGHHEDAGV ICSASQSSSP TPDVFYPTDQ TTAEQTTVPD YTPIGTDSGL 610 620 630 640 650 660 AVRLVNGGDR CQGRVEILYQ GSWGTVCDDS WDLNDANVVC RQLGCGLAVS APGSARFGQG 670 680 690 700 710 720 TGPIVMDDVA CGGYEDYLWR CSHRGWLSHN CGHHEDAGVI CSASQSSSPT PDVFYPTDQT 730 740 750 760 770 780 TAEQTTVPDY TTIGTENSLA VRLENGGDRC QGRVEILYQG SWGTVCDDSW DLNDANVVCR 790 800 810 820 830 840 QLGCGLAVSA PGSARFGQGT GPIVMDDVAC GGYEDYLWRC SHRGWLSHNC GHHEDAGVIC 850 860 870 880 890 900 SASQSSSPTP DVFYPTDQTT VEQTTVPDYT PIGTENSLAV RLENGGDRCQ GRVEILYQGS 910 920 930 940 950 960 WGTVCDDSWD TKDANVVCRQ LGCGWAVSAP GNAYFGPGSG SIVLDDVACT GHEDYLWSCS 970 980 990 1000 1010 1020 HRGWLSHNCG HHEDAGVICS DAQIQSTTRP DLWPTTTTPE TTTELLTTTP YFDWWTTTSD 1030 1040 1050 1060 1070 1080 YSCGGLLTQP SGQFSSPYYP SNYPNNARCS WKIVLPNMNR VTVVFTDVQL EGGCNYDYIL 1090 1100 1110 1120 1130 1140 VYDGPEYNSS LIARVCDGSN GSFTSTGNFM SVVFITDGSV TRRGFQAHYY STVSTNYSCG 1150 1160 1170 1180 1190 1200 GLLTQPSGQF SSPYYPSNYP NNARCSWEIL VPNMNRVTVV FTDVQLEGGC NYDYILVYDG 1210 1220 1230 1240 1250 1260 PQYNSSLIAR VCDGSNGSFT STGNFMSVVF ITDGSVTRRG FQAHYYSTVS TTPPVPIPTT 1270 1280 1290 1300 1310 1320 DDYSCGGLLT LPSGQFSSPH YPSNYPNNAR CSWEILVPNM NRVTVAFTDV QLEGGCNYDY 1330 1340 1350 1360 1370 1380 ILVYDGPEYN SSLIARVCDG SNGSFTSTGN FMSVVFITDG SVTRRGFQAH YYSTVSTNYS 1390 1400 1410 1420 1430 1440 CGGLLTQPSG QFSSPHYPSN YPNNVRCSWE ILVPSMNRVT VAFTDVQLEG GCSFDYILVY 1450 1460 1470 1480 1490 1500 DGPEYNSSLI APVCDGFNGS FTSTGNFMSV VFITDGSVTR RGFQAYYYST VSTPPSFHPN 1510 1520 1530 1540 1550 1560 ITGNDSSLAL RLVNGSNRCE GRVEILYRGS WGTVCDDSWG ISDANVVCRQ LGCGSALSAP 1570 1580 1590 1600 1610 1620 GNAWFGQGSG LIVLDDVSCS GYESHLWNCH HPGWLVHNCR HSEDAGVICA LPEVTSPSPG 1630 1640 1650 1660 1670 1680 WWTTSPSYVN YTCGGFLTQP SGQFSSPFYP GNYPNNARCL WNIEVPNNYR VTVVFRDLQL 1690 1700 1710 1720 1730 1740 ERGCSYDYIE IFDGPHHSSP LIARVCDGSL GSFTSTSNFM SIRFITDHSI TARGFQAHYY 1750 1760 1770 1780 1790 1800 SDFDNNTTNL LCQSNHMQAS VSRSYLQSMG YSARDLVIPG WNSSYHCQPQ ITQREVIFTI 1810 1820 1830 1840 1850 1860 PYTGCGTIKQ ADNETINYSN FLRAVVSNGI IKRRKDLNIH VSCKMLQNTW VNTMYITNNT 1870 1880 1890 1900 1910 1920 VEIQEVQYGN FDVNISFYTS SSFLFPVTSS PYYVDLDQNL YLQAEILHSD ASLALFVDTC 1930 1940 1950 1960 1970 1980 VASPHPNDFS SLTYDLIRSG CVRDDTYQSY SSPSPRVSRF KFSSFHFLNR FPSVYLQCKL 1990 2000 2010 2020 2030 2040 VVCRAYDTSS RCYRGCVVRS KRDVGSYQEK VDVVLGPIQL QSPSKEKRSL DLAVEDVKKP 2050 2060 2070 2080 ASSQAVYPTA AIFGGVFLAM VLAVAAFTLG RRTHIDRGQP PSTKL
	Isoform 2 (CPR-ductin beta). Checksum: 75B4ECA6D1304690	FASTA	2,031	221,165
	10 20 30 40 50 60 MGISTVIFEI CLLWGQILST ASQTAVPTDG TDSGLAVRLV NGGDRCQGRV EILYQGSWGT 70 80 90 100 110 120 VCDDSWDLND ANVVCRQLGC GLAVSAPGNA RFGQGSGPIV MDDVACGGYE DYLWRCSHRG 130 140 150 160 170 180 WLSHNCGHQE DAGVICSDSQ TSSPTPGWWN PGGTNNDVFY PTEQTTAEQT TIPDYTPIGT 190 200 210 220 230 240 DSGLAVRLVN GGDRCQGRVE ILYQGSWGTV CDDSWDVSDA NVVCRQLGCG WAVSAPGNAY 250 260 270 280 290 300 FGQGQGPIVL DDVACGGYEN YLWSCSHQGW LSHNCGHQED AGVICSASQS SSPTPGWWNP 310 320 330 340 350 360 GGTNNDVFYP TEQTTAGTDS GLAVRLVNGG DRCQGRVEIL YQGSWGTVCD DSWDTNDANV 370 380 390 400 410 420 VCRQLGCGWA VSAPGNAYFG PGSGSIVLDD VACTGHEDYL WRCSHRGWLS HNCGHHEDAG 430 440 450 460 470 480 VICSASQSSS PTPDVFYPTD QTTAEQTTVP DYTPIGTDSG LAVRLVNGGD RCQGRVEILY 490 500 510 520 530 540 QGSWGTVCDD SWDLNDANVV CRQLGCGLAV SAPGSARFGQ GTGPIVMDDV ACGGYEDYLW 550 560 570 580 590 600 RCSHRGWLSH NCGHHEDAGV ICSASQSSSP TPDVFYPTDQ TTAEQTTVPD YTPIGTDSGL 610 620 630 640 650 660 AVRLVNGGDR CQGRVEILYQ GSWGTVCDDS WDLNDANVVC RQLGCGLAVS APGSARFGQG 670 680 690 700 710 720 TGPIVMDDVA CGGYEDYLWR CSHRGWLSHN CGHHEDAGVI CSASQSSSPT PDVFYPTDQT 730 740 750 760 770 780 TAEQTTVPDY TTIGTENSLA VRLENGGDRC QGRVEILYQG SWGTVCDDSW DLNDANVVCR 790 800 810 820 830 840 QLGCGLAVSA PGSARFGQGT GPIVMDDVAC GGYEDYLWRC SHRGWLSHNC GHHEDAGVIC 850 860 870 880 890 900 SASQSSSPTP DVFYPTDQTT VEQTTVPDYT PIGTENSLAV RLENGGDRCQ GRVEILYQGS 910 920 930 940 950 960 WGTVCDDSWD TKDANVVCRQ LGCGWAVSAP GNAYFGPGSG SIVLDDVACT GHEDYLWSCS 970 980 990 1000 1010 1020 HRGWLSHNCG HHEDAGVICS DAQIQSTTRP DLWPTTTTPE TTTELLTTTP YFDWWTTTSD 1030 1040 1050 1060 1070 1080 YSCGGLLTQP SGQFSSPYYP SNYPNNARCS WKIVLPNMNR VTVVFTDVQL EGGCNYDYIL 1090 1100 1110 1120 1130 1140 VYDGPEYNSS LIARVCDGSN GSFTSTGNFM SVVFITDGSV TRRGFQAHYY STVSTNYSCG 1150 1160 1170 1180 1190 1200 GLLTQPSGQF SSPYYPSNYP NNARCSWEIL VPNMNRVTVV FTDVQLEGGC NYDYILVYDG 1210 1220 1230 1240 1250 1260 PQYNSSLIAR VCDGSNGSFT STGNFMSVVF ITDGSVTRRG FQAHYYSTVS TTPPVPIPTT 1270 1280 1290 1300 1310 1320 DDYSCGGLLT LPSGQFSSPH YPSNYPNNAR CSWEILVPNM NRVTVAFTDV QLEGGCNYDY 1330 1340 1350 1360 1370 1380 ILVYDGPEYN SSLIARVCDG SNGSFTSTGN FMSVVFITDG SVTRRGFQAH YYSTVSTNYS 1390 1400 1410 1420 1430 1440 CGGLLTQPSG QFSSPHYPSN YPNNVRCSWE ILVPSMNRVT VAFTDVQLEG GCSFDYILVY 1450 1460 1470 1480 1490 1500 DGPEYNSSLI APVCDGFNGS FTSTGNFMSV VFITDGSVTR RGFQAYYYST VSTPPSFHPN 1510 1520 1530 1540 1550 1560 ITGNDSSLAL RLVNGSNRCE GRVEILYRGS WGTVCDDSWG ISDANVVCRQ LGCGSALSAP 1570 1580 1590 1600 1610 1620 GNAWFGQGSG LIVLDDVSCS GYESHLWNCH HPGWLVHNCR HSEDAGVICA LPEVTSPSPG 1630 1640 1650 1660 1670 1680 WWTTSPSYVN YTCGGFLTQP SGQFSSPFYP GNYPNNARCL WNIEVPNNYR VTVVFRDLQL 1690 1700 1710 1720 1730 1740 ERGCSYDYIE IFDGPHHSSP LIARVCDGSL GSFTSTSNFM SIRFITDHSI TARGFQAHYY 1750 1760 1770 1780 1790 1800 SDFDNNTTNL LCQSNHMQAS VSRSYLQSMG YSARDLVIPG WNSSYHCQPQ ITQREVIFTI 1810 1820 1830 1840 1850 1860 PYTGCGTIKQ ADNETINYSN FLRAVVSNGI IKRRKDLNIH VSCKMLQNTW VNTMYITNNT 1870 1880 1890 1900 1910 1920 VEIQEVQYGN FDVNISFYTS SSFLFPVTSS PYYVDLDQNL YLQAEILHSD ASLALFVDTC 1930 1940 1950 1960 1970 1980 VASPHPNDFS SLTYDLIRSG CVRDDTYQSY SSPSPRVSRF KFSSFHFLNR FPSVYLQCKL 1990 2000 2010 2020 2030 VVCRAYDTSS RCYRGCVVRS KRDVGSYQEK VDVVLGPIQL QSPSKEKRSL D
	Isoform 3. Checksum: A807608B561959AD	FASTA	1,958	213,435
	10 20 30 40 50 60 MGISTVIFEI CLLWGQILST ASQTAVPTDE VSYTAEQSTE GTDSGLAVRL VNGGDRCQGR 70 80 90 100 110 120 VEILYQGSWG TVCDDSWDLN DANVVCRQLG CGLAVSAPGN ARFGQGSGPI VMDDVACGGY 130 140 150 160 170 180 EDYLWRCSHR GWLSHNCGHQ EDAGVICSDS QTSSPTPGWW NPGGTNNDVF YPTEQTTAEQ 190 200 210 220 230 240 TTIPDYTPIG TDSGLAVRLV NGGDRCQGRV EILYQGSWGT VCDDSWDVSD ANVVCRQLGC 250 260 270 280 290 300 GWAVSAPGNA YFGQGQGPIV LDDVACGGYE NYLWSCSHQG WLSHNCGHQE DAGVICSASQ 310 320 330 340 350 360 SSSPTPGWWN PGGTNNDVFY PTEQTTAGTD SGLAVRLVNG GDRCQGRVEI LYQGSWGTVC 370 380 390 400 410 420 DDSWDTNDAN VVCRQLGCGW AVSAPGNAYF GPGSGSIVLD DVACTGHYED YLWRCSHRGW 430 440 450 460 470 480 LSHNCGHHED AGVICSASQS SSPTPDVFYP TDQTTAEQTT VPDYTPIGTD SGLAVRLVNG 490 500 510 520 530 540 GDRCQGRVEI LYQGSWGTVC DDSWDLNDAN VVCRQLGCGL AVSAPGSARF GQGTGPIVMD 550 560 570 580 590 600 DVACGGYEDY LWRCSHRGWL SHNCGHHEDA GVICSASQSS SPTPDVFYPT DQTTAEQTTV 610 620 630 640 650 660 PDYTTIGTEN SLAVRLENGG DRCQGRVEIL YQGSWGTVCD DSWDLNDANV VCRQLGCGLA 670 680 690 700 710 720 VSAPGSARFG QGTGPIVMDD VACGGYEDYL WRCSHRGWLS HNCGHHEDAG VICSASQSSS 730 740 750 760 770 780 PTPDVFYPTD QTTVEQTTVP DYTPIGTENS LAVRLENGGD RCQGRVEILY QGSWGTVCDD 790 800 810 820 830 840 SWDTKDANVV CRQLGCGWAV SAPGNAYFGP GSGSIVLDDV ACTGHEDYLW SCSHRGWLSH 850 860 870 880 890 900 NCGHHEDAGV ICSDAQIQST TRPDLWPTTT TPETTTELLT TTPYFDWWTT TSDYSCGGLL 910 920 930 940 950 960 TQPSGQFSSP YYPSNYPNNA RCSWKIVLPN MNRVTVVFTD VQLEGGCNYD YILVYDGPEY 970 980 990 1000 1010 1020 NSSLIARVCD GSNGSFTSTG NFMSVVFITD GSVTRRGFQA HYYSTVSTNY SCGGLLTQPS 1030 1040 1050 1060 1070 1080 GQFSSPYYPS NYPNNARCSW EILVPNMNRV TVVFTDVQLE GGCNYDYILV YDGPQYNSSL 1090 1100 1110 1120 1130 1140 IARVCDGSNG SFTSTGNFMS VVFITDGSVT RRGFQAHYYS TVSTTPPVPI PTTDDYSCGG 1150 1160 1170 1180 1190 1200 LLTLPSGQFS SPHYPSNYPN NARCSWEILV PNMNRVTVAF TDVQLEGGCN YDYILVYDGP 1210 1220 1230 1240 1250 1260 EYNSSLIARV CDGSNGSFTS TGNFMSVVFI TDGSVTRRGF QAHYYSTVST NYSCGGLLTQ 1270 1280 1290 1300 1310 1320 PSGQFSSPHY PSNYPNNVRC SWEILVPSMN RVTVAFTDVQ LEGGCSFDYI LVYDGPEYNS 1330 1340 1350 1360 1370 1380 SLIAPVCDGF NGSFTSTGNF MSVVFITDGS VTRRGFQAYY YSTVSTPPSF HPNITGNDSS 1390 1400 1410 1420 1430 1440 LALRLVNGSN RCEGRVEILY RGSWGTVCDD SWGISDANVV CRQLGCGSAL SAPGNAWFGQ 1450 1460 1470 1480 1490 1500 GSGLIVLDDV SCSGYESHLW NCHHPGWLVH NCRHSEDAGV ICALPEVTSP SPGWWTTSPS 1510 1520 1530 1540 1550 1560 YVNYTCGGFL TQPSGQFSSP FYPGNYPNNA RCLWNIEVPN NYRVTVVFRD LQLERGCSYD 1570 1580 1590 1600 1610 1620 YIEIFDGPHH SSPLIARVCD GSLGSFTSTS NFMSIRFITD HSITARGFQA HYYSDFDNNT 1630 1640 1650 1660 1670 1680 TNLLCQSNHM QASVSRSYLQ SMGYSARDLV IPGWNSSYHC QPQITQREVI FTIPYTGCGT 1690 1700 1710 1720 1730 1740 IKQADNETIN YSNFLRAVVS NGIIKRRKDL NIHVSCKMLQ NTWVNTMYIT NNTVEIQEVQ 1750 1760 1770 1780 1790 1800 YGNFDVNISF YTSSSFLFPV TSSPYYVDLD QNLYLQAEIL HSDASLALFV DTCVASPHPN 1810 1820 1830 1840 1850 1860 DFSSLTYDLI RSGCVRDDTY QSYSSPSPRV SRFKFSSFHF LNRFPSVYLQ CKLVVCRAYD 1870 1880 1890 1900 1910 1920 TSSRCYRGCV VRSKRDVGSY QEKVDVVLGP IQLQSPSKEK RSLDLAVEDV KKPASSQAVY 1930 1940 1950 PTAAIFGGVF LAMVLAVAAF TLGRRTHIDR GQPPSTKL
	Isoform 4. Checksum: C4DE1C161903C30A	FASTA	1,947	212,209
	10 20 30 40 50 60 MGISTVIFEI CLLWGQILST ASQTAVPTDG TDSGLAVRLV NGGDRCQGRV EILYQGSWGT 70 80 90 100 110 120 VCDDSWDLND ANVVCRQLGC GLAVSAPGNA RFGQGSGPIV MDDVACGGYE DYLWRCSHRG 130 140 150 160 170 180 WLSHNCGHQE DAGVICSDSQ TSSPTPGWWN PGGTNNDVFY PTEQTTAEQT TIPDYTPIGT 190 200 210 220 230 240 DSGLAVRLVN GGDRCQGRVE ILYQGSWGTV CDDSWDVSDA NVVCRQLGCG WAVSAPGNAY 250 260 270 280 290 300 FGQGQGPIVL DDVACGGYEN YLWSCSHQGW LSHNCGHQED AGVICSASQS SSPTPGWWNP 310 320 330 340 350 360 GGTNNDVFYP TEQTTAGTDS GLAVRLVNGG DRCQGRVEIL YQGSWGTVCD DSWDTNDANV 370 380 390 400 410 420 VCRQLGCGWA VSAPGNAYFG PGSGSIVLDD VACTGHYEDY LWRCSHRGWL SHNCGHHEDA 430 440 450 460 470 480 GVICSASQSS SPTPDVFYPT DQTTAEQTTV PDYTPIGTDS GLAVRLVNGG DRCQGRVEIL 490 500 510 520 530 540 YQGSWGTVCD DSWDLNDANV VCRQLGCGLA VSAPGSARFG QGTGPIVMDD VACGGYEDYL 550 560 570 580 590 600 WRCSHRGWLS HNCGHHEDAG VICSASQSSS PTPDVFYPTD QTTAEQTTVP DYTTIGTENS 610 620 630 640 650 660 LAVRLENGGD RCQGRVEILY QGSWGTVCDD SWDLNDANVV CRQLGCGLAV SAPGSARFGQ 670 680 690 700 710 720 GTGPIVMDDV ACGGYEDYLW RCSHRGWLSH NCGHHEDAGV ICSASQSSSP TPDVFYPTDQ 730 740 750 760 770 780 TTVEQTTVPD YTPIGTENSL AVRLENGGDR CQGRVEILYQ GSWGTVCDDS WDTKDANVVC 790 800 810 820 830 840 RQLGCGWAVS APGNAYFGPG SGSIVLDDVA CTGHEDYLWS CSHRGWLSHN CGHHEDAGVI 850 860 870 880 890 900 CSDAQIQSTT RPDLWPTTTT PETTTELLTT TPYFDWWTTT SDYSCGGLLT QPSGQFSSPY 910 920 930 940 950 960 YPSNYPNNAR CSWKIVLPNM NRVTVVFTDV QLEGGCNYDY ILVYDGPEYN SSLIARVCDG 970 980 990 1000 1010 1020 SNGSFTSTGN FMSVVFITDG SVTRRGFQAH YYSTVSTNYS CGGLLTQPSG QFSSPYYPSN 1030 1040 1050 1060 1070 1080 YPNNARCSWE ILVPNMNRVT VVFTDVQLEG GCNYDYILVY DGPQYNSSLI ARVCDGSNGS 1090 1100 1110 1120 1130 1140 FTSTGNFMSV VFITDGSVTR RGFQAHYYST VSTTPPVPIP TTDDYSCGGL LTLPSGQFSS 1150 1160 1170 1180 1190 1200 PHYPSNYPNN ARCSWEILVP NMNRVTVAFT DVQLEGGCNY DYILVYDGPE YNSSLIARVC 1210 1220 1230 1240 1250 1260 DGSNGSFTST GNFMSVVFIT DGSVTRRGFQ AHYYSTVSTN YSCGGLLTQP SGQFSSPHYP 1270 1280 1290 1300 1310 1320 SNYPNNVRCS WEILVPSMNR VTVAFTDVQL EGGCSFDYIL VYDGPEYNSS LIAPVCDGFN 1330 1340 1350 1360 1370 1380 GSFTSTGNFM SVVFITDGSV TRRGFQAYYY STVSTPPSFH PNITGNDSSL ALRLVNGSNR 1390 1400 1410 1420 1430 1440 CEGRVEILYR GSWGTVCDDS WGISDANVVC RQLGCGSALS APGNAWFGQG SGLIVLDDVS 1450 1460 1470 1480 1490 1500 CSGYESHLWN CHHPGWLVHN CRHSEDAGVI CALPEVTSPS PGWWTTSPSY VNYTCGGFLT 1510 1520 1530 1540 1550 1560 QPSGQFSSPF YPGNYPNNAR CLWNIEVPNN YRVTVVFRDL QLERGCSYDY IEIFDGPHHS 1570 1580 1590 1600 1610 1620 SPLIARVCDG SLGSFTSTSN FMSIRFITDH SITARGFQAH YYSDFDNNTT NLLCQSNHMQ 1630 1640 1650 1660 1670 1680 ASVSRSYLQS MGYSARDLVI PGWNSSYHCQ PQITQREVIF TIPYTGCGTI KQADNETINY 1690 1700 1710 1720 1730 1740 SNFLRAVVSN GIIKRRKDLN IHVSCKMLQN TWVNTMYITN NTVEIQEVQY GNFDVNISFY 1750 1760 1770 1780 1790 1800 TSSSFLFPVT SSPYYVDLDQ NLYLQAEILH SDASLALFVD TCVASPHPND FSSLTYDLIR 1810 1820 1830 1840 1850 1860 SGCVRDDTYQ SYSSPSPRVS RFKFSSFHFL NRFPSVYLQC KLVVCRAYDT SSRCYRGCVV 1870 1880 1890 1900 1910 1920 RSKRDVGSYQ EKVDVVLGPI QLQSPSKEKR SLDLAVEDVK KPASSQAVYP TAAIFGGVFL 1930 1940 AMVLAVAAFT LGRRTHIDRG QPPSTKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CRP-ductin: a gene expressed in intestinal crypts and in pancreatic and hepatic ducts." Cheng H., Bjerknes M., Chen H. Anat. Rec. 244:327-343(1996) [PubMed: 8742698] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION IN EPITHELIAL DIFFERENTIATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Strain: BALB/c. Tissue: Jejunal epithelium.
[2]	"Vomeroglandin/CRP-ductin is strongly expressed in the glands associated with the mouse vomeronasal organ: identification and characterization of mouse vomeroglandin." Matsushita F., Miyawaki A., Mikoshiba K. Biochem. Biophys. Res. Commun. 268:275-281(2000) [PubMed: 10679193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PROTEIN SEQUENCE OF 22-40 AND 1942-1957, TISSUE SPECIFICITY. Strain: ddY.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Strain: FVB/N. Tissue: Colon.
[4]	"Characterization of the major sulfated protein of mouse pancreatic acinar cells: a high molecular weight peripheral membrane glycoprotein of zymogen granules." De Lisle R.C. J. Cell. Biochem. 56:385-396(1994) [PubMed: 7876332] [Abstract] Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
[5]	"Increased expression of sulfated gp300 and acinar tissue pathology in pancreas of CFTR(-/-) mice." De Lisle R.C. Am. J. Physiol. 268:G717-G723(1995) [PubMed: 7537458] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"Expression of sulfated gp300 and changes in glycosylation during pancreatic development." De Lisle R.C., Isom K.S. J. Histochem. Cytochem. 44:57-66(1996) [PubMed: 8543783] [Abstract] Cited for: DEVELOPMENTAL STAGE, GLYCOSYLATION.
[7]	"Muclin expression in the cystic fibrosis transmembrane conductance regulator knockout mouse." De Lisle R.C., Petitt M., Huff J., Isom K.S., Agbas A. Gastroenterology 113:521-532(1997) [PubMed: 9247472] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]	"Developmental expression of a mucinlike glycoprotein (MUCLIN) in pancreas and small intestine of CF mice." De Lisle R.C., Petitt M., Isom K.S., Ziemer D. Am. J. Physiol. 275:G219-G227(1998) [PubMed: 9688648] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"Processing of pro-muclin and divergent trafficking of its products to zymogen granules and the apical plasma membrane of pancreatic acinar cells." De Lisle R.C., Ziemer D. Eur. J. Cell Biol. 79:892-904(2000) [PubMed: 11152281] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]	"Role of sulfated O-linked glycoproteins in zymogen granule formation." De Lisle R.C. J. Cell Sci. 115:2941-2952(2002) [PubMed: 12082154] [Abstract] Cited for: FUNCTION.
[11]	"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." Madsen J., Tornoee I., Nielsen O., Lausen M., Krebs I., Mollenhauer J., Kollender G., Poustka A., Skjodt K., Holmskov U. Eur. J. Immunol. 33:2327-2336(2003) [PubMed: 12884308] [Abstract] Cited for: FUNCTION, INTERACTION WITH SFTPD, TISSUE SPECIFICITY.
[12]	"Apactin is involved in remodeling of the actin cytoskeleton during regulated exocytosis." Tandon C., De Lisle R.C. Eur. J. Cell Biol. 83:79-89(2004) [PubMed: 15146979] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT THR-2073 AND SER-2082, MUTAGENESIS OF THR-2073 AND SER-2082.
[13]	"Binding of the Golgi sorting receptor muclin to pancreatic zymogens through sulfated O-linked oligosaccharides." Boulatnikov I., De Lisle R.C. J. Biol. Chem. 279:40918-40926(2004) [PubMed: 15292166] [Abstract] Cited for: FUNCTION.
[14]	"Conversion of ES cells to columnar epithelia by hensin and to squamous epithelia by laminin." Takito J., Al-Awqati Q. J. Cell Biol. 166:1093-1102(2004) [PubMed: 15452149] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION, DEVELOPMENTAL STAGE.
[15]	"Expression of pro-muclin in pancreatic AR42J cells induces functional regulated secretory granules." De Lisle R.C., Norkina O., Roach E., Ziemer D. Am. J. Physiol. 289:C1169-C1178(2005) [PubMed: 15987769] [Abstract] Cited for: FUNCTION.
[16]	"DMBT1 confers mucosal protection in vivo and a deletion variant is associated with Crohn's disease." 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. Gastroenterology 133:1499-1509(2007) [PubMed: 17983803] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[17]	"Effects of muclin (Dmbt1) deficiency on the gastrointestinal system." De Lisle R.C., Xu W., Roe B.A., Ziemer D. Am. J. Physiol. 294:G717-G727(2008) [PubMed: 18202109] [Abstract] Cited for: DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U37438 mRNA. Translation: AAC52505.1. Frameshift. AB005909 mRNA. Translation: BAA92266.1. BC049835 mRNA. Translation: AAH49835.1.
IPI	IPI00311384. IPI00662070. IPI00675302. IPI00678471.
PIR	T42721.
RefSeq	NP_031795.2.
UniGene	Mm.4138
3D structure databases
HSSP	HSSP built from PDB template 1BY2 based on UniProtKB Q08380.
ModBase	Search...
PTM databases
PhosphoSite	Q60997.
Proteomic databases
PRIDE	Q60997.
Genome annotation databases
Ensembl	ENSMUSG00000047517. Mus musculus. [Contig view]
GeneID	12945.
KEGG	mmu:12945.
Organism-specific databases
MGI	MGI:106210. Dmbt1.
Phylogenomic databases
HOGENOM	Q60997.
HOVERGEN	Q60997.
Gene expression databases
ArrayExpress	Q60997.
Bgee	Q60997.
CleanEx	MM_DMBT1.
GermOnline	ENSMUSG00000047517. Mus musculus.
Family and domain databases
InterPro	IPR000859. CUB. IPR001507. Endoglin/CD105. IPR017977. Endoglin/CD105_CS. IPR001190. Srcr_rcpt. IPR017448. Srcr_rcpt-rel. [Graphical view]
Gene3D	G3DSA:2.60.120.290. CUB. 5 hits.
Pfam	PF00431. CUB. 5 hits. PF00530. SRCR. 8 hits. PF00100. Zona_pellucida. 1 hit. [Graphical view]
SMART	SM00042. CUB. 5 hits. SM00202. SR. 8 hits. SM00241. ZP. 1 hit. [Graphical view]
PROSITE	PS01180. CUB. 5 hits. PS00420. SRCR_1. 8 hits. PS50287. SRCR_2. 8 hits. PS00682. ZP_1. 1 hit. PS51034. ZP_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	282642.
SOURCE	Search...

Entry information

Entry name

DMBT1_MOUSE

Accession

Primary (citable) accession number: Q60997
Secondary accession number(s): Q80YC6, Q9JMJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	January 10, 2006
Last modified:	July 7, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)