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Reviewed (UniProtKB/Swiss-Prot)

Note: Proteins listed in ProtBank™ database are NOT off-the-shelf [catalog] proteins. Customized protein production request can be made for any protein in this database by clicking on the corresponding button under "Quick Quote". Please ensure sequence accuracy and/or make any necessary modifications prior to submitting your quote request

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Reviewed (UniProtKB/Swiss-Prot)


Name Gene Symbol Rec Full Name Protein Information Quick Quote  Price,
Turnaround
DMBT1_RAT, Rattus norvegicus (Norway rat) Dmbt1 Pancrin Functions
wild_type
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Protein Domains
mutant
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Protein Names | ProteinIDs  | Organism | Gene Names  | GeneID | Genome Annotation(Ensembl) |  Protein Sequence | 
General annotation |  References | Order
Protein Names
Recommended name:
 Deleted in malignant brain tumors 1 protein;
Alternative name(s):
 Ebnerin
Hensin
Pancrin
Protein IDs
(Accession numbers)
UniProtKB
 Q8CIZ5
NCBI RefSeq

NP_074040.2, NM_022849.3.
Organism
Latin Name/
(Common Name)
Rattus norvegicus (Rat).
Taxonomic Identifier (NCBI)
 10116
Gene Names
 Dmbt1 [GenPool]
GeneID

170568
Genome
Annotation (Ensembl)
Protein Sequence
 
SEQUENCE   1418 AA;  155720 MW;  1034F44C7465C2E8 CRC64;
MGISIVIFEI CLLWGQILST ASQSRSSTPD WWNHGGTIND VIYDTQETPE VTTTQVPDST
SIGTDSGLAV RLVNGGDRCR GRVEILYQGS WGTMCDDGTD SGLAVRLVNG GDRCRGRVEI
LYQGSWGTMC DDSWDINDAN VVCRQLGCGW ALSAPGSAQF GQGLGPIVLD DVACRGHEAY
LWSCSHRGWL SHNCGHQEDA GVICSDSQTS SPTPGWWNPG GTNNDVIYDT QETTETSQTS
SPTPDWWNHG GTINDVIYDT QETTEGTDSG LAVRLVNGGD RCRGRVEILY QGSWGTVCDD
SWDINDANVV CRQLGCGWAL SAPGSAQFGQ GSGSIVLDDV ACRGHEAYLW SCSHRGWLSH
NCGHQEDAGV ICSYSQTSSP TPDSQTSSPT PGWWNPGGTN NDVSYGPEQT TDATDSGLAV
RLVNGGDRCQ GRVEILYQGS WGTVCDDSWD TKDANVVCRQ LVCGWALSAP GSAHFGQGSG
SIVLDDVACT GHEAYLWSCS HRGWLSHNCG HHEDAGVICS DAQTQSTTWP DMWPTTTPET
TTDWWTTKYS SSVPTTQFPT IADWWTTPSP EYTCGGLLTL PYGQFSSPYY PGSYPNNARC
LWKIFVSSMN RVTVVFTDVQ LEGGCNYDYI LVFDGPENNS SLIARVCDGF NGSFTSTQNF
MSVVFITDGS VTRRGFQADY YSTPISTSTT SPTTFPIVTD WWTTPSPEYT CGGLLTLPYG
QFSSPYYPGS YPNNARCLWK IFVPSMNRVT VVFTDVQLEG GCNYDYILGF DGPEYNSSLI
ARVCDGSNGS FTSTQNFMSV VFITDGSVTR RGFQADYYST PIRTSTTPPT TFPIITGNDS
SLVLRLVNGT NRCEGRVEIL YRGSWVPCAD DSWDINDANV VCRQLGCGSA LSAPGNAWFG
QGSGLIVLDD VSCSGYESHL WNCRHPGWLV HNCRHVEDAG VICSLPDPTP SPGPVWTSPP
FVNYTCGGFL TGLSGQFSSP YYPGSYPNNA RCLWNIEVPN NYRVTVVFRD VQLEGGCNYD
YIEIFDGPHH SSPLIARVCD GAMGSFTSTS NFMSVRFTTD HSVTRRGFRA DYYSDFDNNT
TNLLCLSNHM RASVSRSYLQ SMGYSSRDLV IPGWNVSYQC QPQITQREVI FTIPYTGCGT
TKQADNETIN YSNFLKAAVS NGIIKRRKDL HIHVSCKMLQ NTWVNTMYIT NNTVEIQEVQ
YGNFDVNISF YTSSSFLYPV TSSPYYVDLD QNLYLQAEVL HSDTSLALFV DTCVASPHPN
DFSSLTYDLI RSGCIRDETY QSYSSPSPRI TRFKFSSFHF LNRFPSVYLQ CKLVVCRAND
VSSRCYRGCV VRSKRDVGSY QEKVDVVLGP IQLQSPSKEK RSLDLAVADV EKPASSQEVY
PTAAIFGGVF LALVVAVAAF TLGRKTRTAR GQPPSTKM
General annotation
Function
 May play roles in mucosal defense system, cellular immune defense and epithelial differentiation (By similarity). 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 macrophages 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 similarity).
Cofactor
Subunit structure
 Binds SFTPD and SPAR in a calcium-dependent manner (By similarity). Interacts with LGALS3.
Subcellular location

Secreted. Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein; Lumenal side (By similarity). 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 (By similarity). Formed in the ducts of von Ebner gland and released into the fluid bathing the taste buds contained in the taste papillae.
Tissue specificity
 Expressed in von Ebner glands (VEG) (at protein level), olfactory epithelium and the lateral nasal gland. Expressed in transit-amplifying ductular (oval) cells. Up- regulated at day 3 after hepatectomy. Expressed in newly formed bile ducts and in structures resembling intestinal epithelium.
Induction
Domain
 The SRCR domains mediate binding to bacteria (By similarity).
Post-translational modification

Highly N- and O-glycosylated. The O-glycans are heavilysulfated (By similarity).
Involvement in disease

References

  • "Heterogeneity of ductular reactions in adult rat and human liverrevealed by novel expression of deleted in malignant brain tumor 1.";,Bisgaard H.C., Holmskov U., Santoni-Rugiu E., Nagy P., Nielsen O.,Ott P., Hage E., Dalhoff K., Rasmussen L.J., Tygstrup N.;,Am. J. Pathol. 161:1187-1198(2002).,PubMeb:12368192

  • "Pancrin a novel member of the scavenger receptor cysteine richsuperfamily in the rat exocrine pancreas.";,Schmidt K., Kleene R.B., Schrader M.;,Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.

  • "Molecular cloning of Ebnerin, a von Ebner's gland protein associatedwith taste buds.";,Li X.-J., Snyder S.H.;,J. Biol. Chem. 270:17674-17679(1995)., PubMeb:7629065 DOI:10.1074/jbc.270.30.17674

  • "Induction of terminal differentiation in epithelial cells requirespolymerization of hensin by galectin 3.";,Hikita C., Vijayakumar S., Takito J., Erdjument-Bromage H., Tempst P.,Al-Awqati Q.;,J. Cell Biol. 151:1235-1246(2000).,PubMeb:11121438 DOI:10.1083/jcb.151.6.1235

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Protein Domain Databases | 3D Structure Database  | Sequence Annotation | Protein-protein Interaction Databases  | 
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Protein Domain Databases
InterPro

IPR000859, CUB.

IPR017977, Endoglin/CD105_CS.

IPR001190, Srcr_rcpt.

IPR017448, Srcr_rcpt-rel.

IPR001507, Zona_pellucida_Endoglin/CD105.
Gene3D

G3DSA:2.60.120.290, CUB; 3.
PANTHER
Pfam

PF00431, CUB; 3.

PF00530, SRCR; 5.

PF00100, Zona_pellucida; 1.
PRINTS

PR00258, SPERACTRCPTR.
SUPFAM

SSF49854, CUB; 3.

SSF56487, Srcr_receptor; 5.
PROSITE

PS01180, CUB; 3.

PS00420, SRCR_1; 2.

PS50287, SRCR_2; 5.

PS00682, ZP_1; 1.

PS51034, ZP_2; 1.
3D Structure
Database (PDB)
Entry
Method
Resolution (A)
Chain
Positions
PDBsum
Sequence
Annotation
Feature key
Position(s)
Length
Description
Signal sequence 1 - 19 19 Potential.
Polypeptide chain 20 - 1418 1399 Deleted in malignant brain tumors 1 /FTId=PRO_0000045389.
Transmembrane region 1383 - 1403 21 Helical; (Potential).
Domain 70 - 170 101 SRCR 1.
Domain 105 - 205 101 SRCR 2.
Domain 273 - 373 101 SRCR 3.
Domain 420 - 520 101 SRCR 4.
Domain 574 - 683 110 CUB 1.
Domain 711 - 820 110 CUB 2.
Domain 844 - 944 101 SRCR 5.
Domain 966 - 1075 110 CUB 3.
Domain 1084 - 1332 249 ZP.
Compositionally biased region 524 - 567 44 Thr-rich.
Posttranslational modification of a residue 1406 1 Phosphothreonine (By similarity).
Posttranslational modification of a residue 1415 1 Phosphoserine (By similarity).
Glycosylation site 638 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 639 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 651 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 776 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 788 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 838 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 848 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 963 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 1078 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 1079 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 1115 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 1146 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 1150 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 1191 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 1207 1 N-linked (GlcNAc...) (Potential).
Disulfide bond 130 - 194 65 By similarity.
Disulfide bond 143 - 204 62 By similarity.
Disulfide bond 174 - 184 11 By similarity.
Disulfide bond 298 - 362 65 By similarity.
Disulfide bond 311 - 372 62 By similarity.
Disulfide bond 342 - 352 11 By similarity.
Disulfide bond 445 - 509 65 By similarity.
Disulfide bond 458 - 519 62 By similarity.
Disulfide bond 489 - 499 11 By similarity.
Disulfide bond 574 - 600 27 By similarity.
Disulfide bond 625 - 647 23 By similarity.
Disulfide bond 711 - 737 27 By similarity.
Disulfide bond 762 - 784 23 By similarity.
Disulfide bond 882 - 943 62 By similarity.
Disulfide bond 913 - 923 11 By similarity.
Disulfide bond 966 - 992 27 By similarity.
Disulfide bond 1017 - 1039 23 By similarity.
Natural variance 63 - 97 35 Missing (in isoform 2). /FTId=VSP_016854.
Natural variance 375 1 S -> SPTSSPTPGWWNPGFTNSDVSYRTELPTDDS (in /FTId=VSP_016855.
Natural variance 827 - 837 11 TPPTTFPIITG -> R (in isoform 2). /FTId=VSP_016856.
Natural variance 866 - 871 6 VPCADD -> GTVCDN (in isoform 2). /FTId=VSP_016857.
Natural variance 955 - 961 7 Missing (in isoform 2). /FTId=VSP_016858.
Different sources report differing sequences 129 1 M -> V (in Ref. 2; AAS46613).
Different sources report differing sequences 164 - 166 3 LGP -> SGS (in Ref. 2; AAS46613).
Different sources report differing sequences 343 1 R -> T (in Ref. 2; AAS46613).
Different sources report differing sequences 462 1 V -> G (in Ref. 2; AAS46613).
Different sources report differing sequences 638 1 N -> Y (in Ref. 2; AAS46613).
Different sources report differing sequences 769 1 G -> V (in Ref. 2; AAS46613).
Different sources report differing sequences 1058 1 T -> I (in Ref. 2; AAS46613).
Different sources report differing sequences 1106 1 S -> A (in Ref. 2; AAS46613).
Different sources report differing sequences 1319 1 N -> Y (in Ref. 2; AAS46613).
Protein-protein
Interaction
Databases
DIP
IntAct
MINT
STRING

Q8CIZ5
Binary Interactions
With
Entry
#Exp.
IntAct
Enzyme and Pathway Databases
Pathway
Interaction DB
Reactome
Phylogenomic Database
HOVERGEN

HBG060122
InParanoid

Q8CIZ5
OMA
OrthoDB

EOG4RR6GF
Proteomics
Database (PRIDE)

Q8CIZ5
Comparative
Toxicogenomics
Database (CTD)

1755
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Email: [email protected]
Phone: 1-877-436-7274 (Toll-Free) 1-732-885-9188
Fax: 1-732-210-0262