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Protein

Deleted in malignant brain tumors 1 protein

Gene

Dmbt1

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

Functioni

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.By similarity8 Publications

GO - Molecular functioni

  • scavenger receptor activity Source: InterPro
  • zymogen binding Source: UniProtKB

GO - Biological processi

  • blastocyst development Source: MGI
  • cell differentiation Source: UniProtKB-KW
  • inner cell mass cell proliferation Source: MGI
  • positive regulation of epithelial cell differentiation Source: MGI
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Deleted in malignant brain tumors 1 protein
Alternative name(s):
Apactin
CRP-ductin
Glycoprotein 300
Short name:
gp300
Hensin
Mucin-like glycoprotein
Short name:
Muclin
Vomeroglandin
p80
Gene namesi
Name:Dmbt1
Synonyms:Crpd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:106210. Dmbt1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei2050 – 2070HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • extrinsic component of membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • intracellular Source: MGI
  • phagocytic vesicle membrane Source: MGI
  • proteinaceous extracellular matrix Source: MGI
  • transport vesicle membrane Source: UniProtKB-SubCell
  • zymogen granule membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

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).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2073T → A: Abolishes phosphorylation. 1 Publication1
Mutagenesisi2082S → A: Abolishes phosphorylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000004538820 – 2085Deleted in malignant brain tumors 1 proteinAdd BLAST2066

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi62 ↔ 126By similarity
Disulfide bondi75 ↔ 136By similarity
Disulfide bondi106 ↔ 116By similarity
Disulfide bondi211 ↔ 275By similarity
Disulfide bondi224 ↔ 285By similarity
Disulfide bondi255 ↔ 265By similarity
Disulfide bondi349 ↔ 413By similarity
Disulfide bondi362 ↔ 423By similarity
Disulfide bondi393 ↔ 403By similarity
Disulfide bondi488 ↔ 552By similarity
Disulfide bondi501 ↔ 562By similarity
Disulfide bondi532 ↔ 542By similarity
Disulfide bondi627 ↔ 691By similarity
Disulfide bondi640 ↔ 701By similarity
Disulfide bondi671 ↔ 681By similarity
Disulfide bondi766 ↔ 830By similarity
Disulfide bondi779 ↔ 840By similarity
Disulfide bondi810 ↔ 820By similarity
Disulfide bondi905 ↔ 969By similarity
Disulfide bondi918 ↔ 979By similarity
Disulfide bondi949 ↔ 959By similarity
Disulfide bondi1023 ↔ 1049By similarity
Disulfide bondi1074 ↔ 1096By similarity
Glycosylationi1088N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1100N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1136N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1139 ↔ 1165By similarity
Disulfide bondi1190 ↔ 1212By similarity
Glycosylationi1204N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1216N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1265 ↔ 1291By similarity
Disulfide bondi1316 ↔ 1338By similarity
Glycosylationi1330N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1342N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1378N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1381 ↔ 1407By similarity
Disulfide bondi1432 ↔ 1454By similarity
Glycosylationi1446N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1458N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1500N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1504N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1514N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1535 ↔ 1599By similarity
Disulfide bondi1548 ↔ 1609By similarity
Disulfide bondi1579 ↔ 1589By similarity
Glycosylationi1630N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1633 ↔ 1659By similarity
Disulfide bondi1684 ↔ 1706By similarity
Glycosylationi1745N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1746N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1782N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1813N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1817N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1858N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1874N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1920 ↔ 1978By similarity
Modified residuei2073Phosphothreonine1 Publication1
Modified residuei2082Phosphoserine1 Publication1

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ60997.
PRIDEiQ60997.

PTM databases

iPTMnetiQ60997.
PhosphoSitePlusiQ60997.

Expressioni

Tissue specificityi

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.6 Publications

Developmental stagei

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.2 Publications

Gene expression databases

CleanExiMM_DMBT1.

Interactioni

Subunit structurei

Interacts with LGALS3. Binds SPAR in a calcium-dependent manner (By similarity). Binds SFTPD in a calcium-dependent manner.By similarity1 Publication

GO - Molecular functioni

  • zymogen binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000081556.

Structurei

3D structure databases

ProteinModelPortaliQ60997.
SMRiQ60997.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 137SRCR 1PROSITE-ProRule annotationAdd BLAST101
Domaini186 – 286SRCR 2PROSITE-ProRule annotationAdd BLAST101
Domaini324 – 424SRCR 3PROSITE-ProRule annotationAdd BLAST101
Domaini463 – 563SRCR 4PROSITE-ProRule annotationAdd BLAST101
Domaini602 – 702SRCR 5PROSITE-ProRule annotationAdd BLAST101
Domaini741 – 841SRCR 6PROSITE-ProRule annotationAdd BLAST101
Domaini880 – 980SRCR 7PROSITE-ProRule annotationAdd BLAST101
Domaini1023 – 1132CUB 1PROSITE-ProRule annotationAdd BLAST110
Domaini1139 – 1248CUB 2PROSITE-ProRule annotationAdd BLAST110
Domaini1265 – 1374CUB 3PROSITE-ProRule annotationAdd BLAST110
Domaini1381 – 1490CUB 4PROSITE-ProRule annotationAdd BLAST110
Domaini1510 – 1610SRCR 8PROSITE-ProRule annotationAdd BLAST101
Domaini1633 – 1742CUB 5PROSITE-ProRule annotationAdd BLAST110
Domaini1751 – 1999ZPPROSITE-ProRule annotationAdd BLAST249

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi987 – 1018Thr-richAdd BLAST32

Domaini

The SRCR domains mediate binding to bacteria.By similarity

Sequence similaritiesi

Belongs to the DMBT1 family.Curated
Contains 5 CUB domains.PROSITE-ProRule annotation
Contains 8 SRCR domains.PROSITE-ProRule annotation
Contains 1 ZP domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IHBC. Eukaryota.
ENOG410XQVR. LUCA.
HOGENOMiHOG000290652.
HOVERGENiHBG060122.
InParanoidiQ60997.
KOiK13912.
PhylomeDBiQ60997.

Family and domain databases

CDDicd00041. CUB. 5 hits.
Gene3Di2.60.120.290. 5 hits.
3.10.250.10. 8 hits.
InterProiIPR000859. CUB_dom.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamiPF00431. CUB. 5 hits.
PF00530. SRCR. 8 hits.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSiPR00258. SPERACTRCPTR.
SMARTiSM00042. CUB. 5 hits.
SM00202. SR. 8 hits.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 5 hits.
SSF56487. SSF56487. 8 hits.
PROSITEiPS01180. 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]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q60997-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MGISTVIFEI CLLWGQILST ASQTAVPTDG TDSGLAVRLV NGGDRCQGRV
60 70 80 90 100
EILYQGSWGT VCDDSWDLND ANVVCRQLGC GLAVSAPGNA RFGQGSGPIV
110 120 130 140 150
MDDVACGGYE DYLWRCSHRG WLSHNCGHQE DAGVICSDSQ TSSPTPGWWN
160 170 180 190 200
PGGTNNDVFY PTEQTTAEQT TIPDYTPIGT DSGLAVRLVN GGDRCQGRVE
210 220 230 240 250
ILYQGSWGTV CDDSWDVSDA NVVCRQLGCG WAVSAPGNAY FGQGQGPIVL
260 270 280 290 300
DDVACGGYEN YLWSCSHQGW LSHNCGHQED AGVICSASQS SSPTPGWWNP
310 320 330 340 350
GGTNNDVFYP TEQTTAGTDS GLAVRLVNGG DRCQGRVEIL YQGSWGTVCD
360 370 380 390 400
DSWDTNDANV VCRQLGCGWA VSAPGNAYFG PGSGSIVLDD VACTGHEDYL
410 420 430 440 450
WRCSHRGWLS HNCGHHEDAG VICSASQSSS PTPDVFYPTD QTTAEQTTVP
460 470 480 490 500
DYTPIGTDSG LAVRLVNGGD RCQGRVEILY QGSWGTVCDD SWDLNDANVV
510 520 530 540 550
CRQLGCGLAV SAPGSARFGQ GTGPIVMDDV ACGGYEDYLW RCSHRGWLSH
560 570 580 590 600
NCGHHEDAGV ICSASQSSSP TPDVFYPTDQ TTAEQTTVPD YTPIGTDSGL
610 620 630 640 650
AVRLVNGGDR CQGRVEILYQ GSWGTVCDDS WDLNDANVVC RQLGCGLAVS
660 670 680 690 700
APGSARFGQG TGPIVMDDVA CGGYEDYLWR CSHRGWLSHN CGHHEDAGVI
710 720 730 740 750
CSASQSSSPT PDVFYPTDQT TAEQTTVPDY TTIGTENSLA VRLENGGDRC
760 770 780 790 800
QGRVEILYQG SWGTVCDDSW DLNDANVVCR QLGCGLAVSA PGSARFGQGT
810 820 830 840 850
GPIVMDDVAC GGYEDYLWRC SHRGWLSHNC GHHEDAGVIC SASQSSSPTP
860 870 880 890 900
DVFYPTDQTT VEQTTVPDYT PIGTENSLAV RLENGGDRCQ GRVEILYQGS
910 920 930 940 950
WGTVCDDSWD TKDANVVCRQ LGCGWAVSAP GNAYFGPGSG SIVLDDVACT
960 970 980 990 1000
GHEDYLWSCS HRGWLSHNCG HHEDAGVICS DAQIQSTTRP DLWPTTTTPE
1010 1020 1030 1040 1050
TTTELLTTTP YFDWWTTTSD YSCGGLLTQP SGQFSSPYYP SNYPNNARCS
1060 1070 1080 1090 1100
WKIVLPNMNR VTVVFTDVQL EGGCNYDYIL VYDGPEYNSS LIARVCDGSN
1110 1120 1130 1140 1150
GSFTSTGNFM SVVFITDGSV TRRGFQAHYY STVSTNYSCG GLLTQPSGQF
1160 1170 1180 1190 1200
SSPYYPSNYP NNARCSWEIL VPNMNRVTVV FTDVQLEGGC NYDYILVYDG
1210 1220 1230 1240 1250
PQYNSSLIAR VCDGSNGSFT STGNFMSVVF ITDGSVTRRG FQAHYYSTVS
1260 1270 1280 1290 1300
TTPPVPIPTT DDYSCGGLLT LPSGQFSSPH YPSNYPNNAR CSWEILVPNM
1310 1320 1330 1340 1350
NRVTVAFTDV QLEGGCNYDY ILVYDGPEYN SSLIARVCDG SNGSFTSTGN
1360 1370 1380 1390 1400
FMSVVFITDG SVTRRGFQAH YYSTVSTNYS CGGLLTQPSG QFSSPHYPSN
1410 1420 1430 1440 1450
YPNNVRCSWE ILVPSMNRVT VAFTDVQLEG GCSFDYILVY DGPEYNSSLI
1460 1470 1480 1490 1500
APVCDGFNGS FTSTGNFMSV VFITDGSVTR RGFQAYYYST VSTPPSFHPN
1510 1520 1530 1540 1550
ITGNDSSLAL RLVNGSNRCE GRVEILYRGS WGTVCDDSWG ISDANVVCRQ
1560 1570 1580 1590 1600
LGCGSALSAP GNAWFGQGSG LIVLDDVSCS GYESHLWNCH HPGWLVHNCR
1610 1620 1630 1640 1650
HSEDAGVICA LPEVTSPSPG WWTTSPSYVN YTCGGFLTQP SGQFSSPFYP
1660 1670 1680 1690 1700
GNYPNNARCL WNIEVPNNYR VTVVFRDLQL ERGCSYDYIE IFDGPHHSSP
1710 1720 1730 1740 1750
LIARVCDGSL GSFTSTSNFM SIRFITDHSI TARGFQAHYY SDFDNNTTNL
1760 1770 1780 1790 1800
LCQSNHMQAS VSRSYLQSMG YSARDLVIPG WNSSYHCQPQ ITQREVIFTI
1810 1820 1830 1840 1850
PYTGCGTIKQ ADNETINYSN FLRAVVSNGI IKRRKDLNIH VSCKMLQNTW
1860 1870 1880 1890 1900
VNTMYITNNT VEIQEVQYGN FDVNISFYTS SSFLFPVTSS PYYVDLDQNL
1910 1920 1930 1940 1950
YLQAEILHSD ASLALFVDTC VASPHPNDFS SLTYDLIRSG CVRDDTYQSY
1960 1970 1980 1990 2000
SSPSPRVSRF KFSSFHFLNR FPSVYLQCKL VVCRAYDTSS RCYRGCVVRS
2010 2020 2030 2040 2050
KRDVGSYQEK VDVVLGPIQL QSPSKEKRSL DLAVEDVKKP ASSQAVYPTA
2060 2070 2080
AIFGGVFLAM VLAVAAFTLG RRTHIDRGQP PSTKL
Length:2,085
Mass (Da):226,815
Last modified:January 10, 2006 - v2
Checksum:i8BE4E77D299B32ED
GO
Isoform 2 (identifier: Q60997-2) [UniParc]FASTAAdd to basket
Also known as: CPR-ductin beta

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

Show »
Length:2,031
Mass (Da):221,165
Checksum:i75B4ECA6D1304690
GO
Isoform 3 (identifier: Q60997-3) [UniParc]FASTAAdd to basket

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

Show »
Length:1,958
Mass (Da):213,435
Checksum:iA807608B561959AD
GO
Isoform 4 (identifier: Q60997-4) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:1,947
Mass (Da):212,209
Checksum:iC4DE1C161903C30A
GO

Sequence cautioni

The sequence AAC52505 differs from that shown. Reason: Frameshift at positions 227, 233, 236 and 240.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti247 – 248PI → L in AAC52505 (PubMed:8742698).Curated2
Sequence conflicti1494 – 1497PPSF → SLH in AAC52505 (PubMed:8742698).Curated4
Sequence conflicti2061V → G in BAA92266 (PubMed:10679193).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01685129D → DEVSYTAEQSTE in isoform 3. 1 Publication1
Alternative sequenceiVSP_016852397 – 534Missing in isoform 3 and isoform 4. 2 PublicationsAdd BLAST138
Alternative sequenceiVSP_0168532032 – 2085Missing in isoform 2. 1 PublicationAdd BLAST54

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37438 mRNA. Translation: AAC52505.1. Frameshift.
AB005909 mRNA. Translation: BAA92266.1.
BC049835 mRNA. Translation: AAH49835.1.
PIRiT42721.
RefSeqiNP_031795.2. NM_007769.2.
UniGeneiMm.4138.

Genome annotation databases

GeneIDi12945.
KEGGimmu:12945.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37438 mRNA. Translation: AAC52505.1. Frameshift.
AB005909 mRNA. Translation: BAA92266.1.
BC049835 mRNA. Translation: AAH49835.1.
PIRiT42721.
RefSeqiNP_031795.2. NM_007769.2.
UniGeneiMm.4138.

3D structure databases

ProteinModelPortaliQ60997.
SMRiQ60997.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000081556.

PTM databases

iPTMnetiQ60997.
PhosphoSitePlusiQ60997.

Proteomic databases

PaxDbiQ60997.
PRIDEiQ60997.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi12945.
KEGGimmu:12945.

Organism-specific databases

CTDi1755.
MGIiMGI:106210. Dmbt1.

Phylogenomic databases

eggNOGiENOG410IHBC. Eukaryota.
ENOG410XQVR. LUCA.
HOGENOMiHOG000290652.
HOVERGENiHBG060122.
InParanoidiQ60997.
KOiK13912.
PhylomeDBiQ60997.

Miscellaneous databases

PROiQ60997.
SOURCEiSearch...

Gene expression databases

CleanExiMM_DMBT1.

Family and domain databases

CDDicd00041. CUB. 5 hits.
Gene3Di2.60.120.290. 5 hits.
3.10.250.10. 8 hits.
InterProiIPR000859. CUB_dom.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamiPF00431. CUB. 5 hits.
PF00530. SRCR. 8 hits.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSiPR00258. SPERACTRCPTR.
SMARTiSM00042. CUB. 5 hits.
SM00202. SR. 8 hits.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 5 hits.
SSF56487. SSF56487. 8 hits.
PROSITEiPS01180. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiDMBT1_MOUSE
AccessioniPrimary (citable) accession number: Q60997
Secondary accession number(s): Q80YC6, Q9JMJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: November 30, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.