DMBT1_RAT
ID DMBT1_RAT Reviewed; 1418 AA.
AC Q8CIZ5; Q62827; Q6QD54;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Deleted in malignant brain tumors 1 protein;
DE AltName: Full=Ebnerin;
DE AltName: Full=Hensin;
DE AltName: Full=Pancrin;
DE Flags: Precursor;
GN Name=Dmbt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=12368192; DOI=10.1016/s0002-9440(10)64395-7;
RA Bisgaard H.C., Holmskov U., Santoni-Rugiu E., Nagy P., Nielsen O., Ott P.,
RA Hage E., Dalhoff K., Rasmussen L.J., Tygstrup N.;
RT "Heterogeneity of ductular reactions in adult rat and human liver revealed
RT by novel expression of deleted in malignant brain tumor 1.";
RL Am. J. Pathol. 161:1187-1198(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Wistar; TISSUE=Pancreas;
RA Schmidt K., Kleene R.B., Schrader M.;
RT "Pancrin a novel member of the scavenger receptor cysteine rich superfamily
RT in the rat exocrine pancreas.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 98-1418 (ISOFORM 1), PROTEIN SEQUENCE OF
RP 1058-1074, FUNCTION IN LIVER REGENERATION, FUNCTION IN REGULATION OF TASTE
RP SENSATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Tongue;
RX PubMed=7629065; DOI=10.1074/jbc.270.30.17674;
RA Li X.-J., Snyder S.H.;
RT "Molecular cloning of Ebnerin, a von Ebner's gland protein associated with
RT taste buds.";
RL J. Biol. Chem. 270:17674-17679(1995).
RN [4]
RP INTERACTION WITH LGALS3, AND FUNCTION.
RX PubMed=11121438; DOI=10.1083/jcb.151.6.1235;
RA Hikita C., Vijayakumar S., Takito J., Erdjument-Bromage H., Tempst P.,
RA Al-Awqati Q.;
RT "Induction of terminal differentiation in epithelial cells requires
RT polymerization of hensin by galectin 3.";
RL J. Cell Biol. 151:1235-1246(2000).
CC -!- FUNCTION: May play roles in mucosal defense system, cellular immune
CC defense and epithelial differentiation (By similarity). May play a role
CC in liver regeneration. May be an important factor in fate decision and
CC differentiation of transit-amplifying ductular (oval) cells within the
CC hepatic lineage. May function as a binding protein in saliva for the
CC regulation of taste sensation. May play a role as an opsonin receptor
CC for SFTPD and SPAR in macrophages tissues throughout the body,
CC including epithelial cells lining the gastrointestinal tract (By
CC similarity). Required for terminal differentiation of columnar
CC epithelial cells during early embryogenesis. Displays a broad calcium-
CC dependent binding spectrum against both Gram-positive and Gram-negative
CC bacteria, suggesting a role in defense against bacterial pathogens.
CC Binds to a range of poly-sulfated and poly-phosphorylated ligands which
CC may explain its broad bacterial-binding specificity. Inhibits
CC cytoinvasion of S.enterica. Associates with the actin cytoskeleton and
CC is involved in its remodeling during regulated exocytosis. Interacts
CC with pancreatic zymogens in a pH-dependent manner and may act as a
CC Golgi cargo receptor in the regulated secretory pathway of the
CC pancreatic acinar cell (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11121438, ECO:0000269|PubMed:12368192,
CC ECO:0000269|PubMed:7629065}.
CC -!- SUBUNIT: Binds SFTPD and SPAR in a calcium-dependent manner (By
CC similarity). Interacts with LGALS3. {ECO:0000250,
CC ECO:0000269|PubMed:11121438}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7629065}.
CC Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Single-
CC pass membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}.
CC Note=Localized to the lumenal aspect of crypt cells in the small
CC intestine. In the colon, seen in the lumenal aspect of surface
CC epithelial cells (By similarity). Formed in the ducts of von Ebner
CC gland and released into the fluid bathing the taste buds contained in
CC the taste papillae. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Dmbt1 4.7kb;
CC IsoId=Q8CIZ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CIZ5-4; Sequence=VSP_016854, VSP_016855, VSP_016856,
CC VSP_016857, VSP_016858;
CC -!- TISSUE SPECIFICITY: Expressed in von Ebner glands (VEG) (at protein
CC level), olfactory epithelium and the lateral nasal gland. Expressed in
CC transit-amplifying ductular (oval) cells. Up-regulated at day 3 after
CC hepatectomy. Expressed in newly formed bile ducts and in structures
CC resembling intestinal epithelium. {ECO:0000269|PubMed:12368192,
CC ECO:0000269|PubMed:7629065}.
CC -!- DOMAIN: The SRCR domains mediate binding to bacteria. {ECO:0000250}.
CC -!- PTM: Highly N- and O-glycosylated. The O-glycans are heavily sulfated
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DMBT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52248.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF540887; AAN16473.1; -; mRNA.
DR EMBL; AY548057; AAS46613.1; -; mRNA.
DR EMBL; U32681; AAC52248.1; ALT_INIT; mRNA.
DR PIR; A57190; A57190.
DR RefSeq; NP_074040.2; NM_022849.3. [Q8CIZ5-1]
DR AlphaFoldDB; Q8CIZ5; -.
DR SMR; Q8CIZ5; -.
DR GlyGen; Q8CIZ5; 15 sites.
DR PhosphoSitePlus; Q8CIZ5; -.
DR PRIDE; Q8CIZ5; -.
DR GeneID; 170568; -.
DR KEGG; rno:170568; -.
DR UCSC; RGD:61984; rat. [Q8CIZ5-1]
DR CTD; 1755; -.
DR RGD; 61984; Dmbt1.
DR eggNOG; ENOG502QQ5W; Eukaryota.
DR InParanoid; Q8CIZ5; -.
DR OrthoDB; 1095487at2759; -.
DR PhylomeDB; Q8CIZ5; -.
DR Reactome; R-RNO-5683826; Surfactant metabolism.
DR PRO; PR:Q8CIZ5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030670; C:phagocytic vesicle membrane; ISO:RGD.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042589; C:zymogen granule membrane; ISS:UniProtKB.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0035375; F:zymogen binding; ISS:UniProtKB.
DR GO; GO:0001824; P:blastocyst development; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEP:RGD.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0042494; P:detection of bacterial lipoprotein; IBA:GO_Central.
DR GO; GO:0001833; P:inner cell mass cell proliferation; ISO:RGD.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR GO; GO:0042246; P:tissue regeneration; IEP:RGD.
DR CDD; cd00041; CUB; 3.
DR Gene3D; 2.60.120.290; -; 3.
DR Gene3D; 2.60.40.4100; -; 1.
DR Gene3D; 3.10.250.10; -; 5.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR Pfam; PF00431; CUB; 3.
DR Pfam; PF00530; SRCR; 4.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00042; CUB; 3.
DR SMART; SM00202; SR; 4.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF49854; SSF49854; 3.
DR SUPFAM; SSF56487; SSF56487; 5.
DR PROSITE; PS01180; CUB; 3.
DR PROSITE; PS00420; SRCR_1; 2.
DR PROSITE; PS50287; SRCR_2; 5.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Developmental protein;
KW Differentiation; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1418
FT /note="Deleted in malignant brain tumors 1 protein"
FT /id="PRO_0000045389"
FT TRANSMEM 1383..1403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 70..170
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 105..205
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 273..373
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 420..520
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 574..683
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 711..820
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 844..944
FT /note="SRCR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 966..1075
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1084..1332
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 375..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q60997"
FT MOD_RES 1415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60997"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 838
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 848
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 963
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1078
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1079
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 130..194
FT /evidence="ECO:0000250"
FT DISULFID 143..204
FT /evidence="ECO:0000250"
FT DISULFID 174..184
FT /evidence="ECO:0000250"
FT DISULFID 298..362
FT /evidence="ECO:0000250"
FT DISULFID 311..372
FT /evidence="ECO:0000250"
FT DISULFID 342..352
FT /evidence="ECO:0000250"
FT DISULFID 445..509
FT /evidence="ECO:0000250"
FT DISULFID 458..519
FT /evidence="ECO:0000250"
FT DISULFID 489..499
FT /evidence="ECO:0000250"
FT DISULFID 574..600
FT /evidence="ECO:0000250"
FT DISULFID 625..647
FT /evidence="ECO:0000250"
FT DISULFID 711..737
FT /evidence="ECO:0000250"
FT DISULFID 762..784
FT /evidence="ECO:0000250"
FT DISULFID 882..943
FT /evidence="ECO:0000250"
FT DISULFID 913..923
FT /evidence="ECO:0000250"
FT DISULFID 966..992
FT /evidence="ECO:0000250"
FT DISULFID 1017..1039
FT /evidence="ECO:0000250"
FT DISULFID 1253..1311
FT /evidence="ECO:0000250"
FT VAR_SEQ 63..97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016854"
FT VAR_SEQ 375
FT /note="S -> SPTSSPTPGWWNPGFTNSDVSYRTELPTDDS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016855"
FT VAR_SEQ 827..837
FT /note="TPPTTFPIITG -> R (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016856"
FT VAR_SEQ 866..871
FT /note="VPCADD -> GTVCDN (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016857"
FT VAR_SEQ 955..961
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016858"
FT CONFLICT 129
FT /note="M -> V (in Ref. 2; AAS46613)"
FT /evidence="ECO:0000305"
FT CONFLICT 164..166
FT /note="LGP -> SGS (in Ref. 2; AAS46613)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="R -> T (in Ref. 2; AAS46613)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="V -> G (in Ref. 2; AAS46613)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="N -> Y (in Ref. 2; AAS46613)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="G -> V (in Ref. 2; AAS46613)"
FT /evidence="ECO:0000305"
FT CONFLICT 1058
FT /note="T -> I (in Ref. 2; AAS46613)"
FT /evidence="ECO:0000305"
FT CONFLICT 1106
FT /note="S -> A (in Ref. 2; AAS46613)"
FT /evidence="ECO:0000305"
FT CONFLICT 1319
FT /note="N -> Y (in Ref. 2; AAS46613)"
FT /evidence="ECO:0000305"
SQ 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
