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Deleted in malignant brain tumors 1 protein (Ebnerin) (Hensin) (Pancrin)

 DMBT1_RAT               Reviewed;        1418 AA.
Q8CIZ5; Q62827; Q6QD54;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
22-NOV-2017, entry version 112.
RecName: Full=Deleted in malignant brain tumors 1 protein;
AltName: Full=Ebnerin;
AltName: Full=Hensin;
AltName: Full=Pancrin;
Flags: Precursor;
Name=Dmbt1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
STRAIN=Wistar; TISSUE=Liver;
PubMed=12368192; DOI=10.1016/S0002-9440(10)64395-7;
Bisgaard H.C., Holmskov U., Santoni-Rugiu E., Nagy P., Nielsen O.,
Ott P., Hage E., Dalhoff K., Rasmussen L.J., Tygstrup N.;
"Heterogeneity of ductular reactions in adult rat and human liver
revealed by novel expression of deleted in malignant brain tumor 1.";
Am. J. Pathol. 161:1187-1198(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=Wistar; TISSUE=Pancreas;
Schmidt K., Kleene R.B., Schrader M.;
"Pancrin a novel member of the scavenger receptor cysteine rich
superfamily in the rat exocrine pancreas.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 98-1418 (ISOFORM 1), PROTEIN SEQUENCE OF
1058-1074, FUNCTION IN LIVER REGENERATION, FUNCTION IN REGULATION OF
TASTE SENSATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Tongue;
PubMed=7629065; DOI=10.1074/jbc.270.30.17674;
Li X.-J., Snyder S.H.;
"Molecular cloning of Ebnerin, a von Ebner's gland protein associated
with taste buds.";
J. Biol. Chem. 270:17674-17679(1995).
[4]
INTERACTION WITH LGALS3, AND FUNCTION.
PubMed=11121438; DOI=10.1083/jcb.151.6.1235;
Hikita C., Vijayakumar S., Takito J., Erdjument-Bromage H., Tempst P.,
Al-Awqati Q.;
"Induction of terminal differentiation in epithelial cells requires
polymerization of hensin by galectin 3.";
J. Cell Biol. 151:1235-1246(2000).
-!- 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). {ECO:0000250,
ECO:0000269|PubMed:11121438, ECO:0000269|PubMed:12368192,
ECO:0000269|PubMed:7629065}.
-!- SUBUNIT: Binds SFTPD and SPAR in a calcium-dependent manner (By
similarity). Interacts with LGALS3. {ECO:0000250,
ECO:0000269|PubMed:11121438}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7629065}.
Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250};
Single-pass membrane protein {ECO:0000250}; Lumenal side
{ECO:0000250}. 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. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Dmbt1 4.7kb;
IsoId=Q8CIZ5-1; Sequence=Displayed;
Name=2;
IsoId=Q8CIZ5-4; Sequence=VSP_016854, VSP_016855, VSP_016856,
VSP_016857, VSP_016858;
-!- 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.
{ECO:0000269|PubMed:12368192, ECO:0000269|PubMed:7629065}.
-!- DOMAIN: The SRCR domains mediate binding to bacteria.
{ECO:0000250}.
-!- PTM: Highly N- and O-glycosylated. The O-glycans are heavily
sulfated (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the DMBT1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC52248.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF540887; AAN16473.1; -; mRNA.
EMBL; AY548057; AAS46613.1; -; mRNA.
EMBL; U32681; AAC52248.1; ALT_INIT; mRNA.
PIR; A57190; A57190.
RefSeq; NP_074040.2; NM_022849.3. [Q8CIZ5-1]
UniGene; Rn.10107; -.
ProteinModelPortal; Q8CIZ5; -.
SMR; Q8CIZ5; -.
PhosphoSitePlus; Q8CIZ5; -.
PRIDE; Q8CIZ5; -.
GeneID; 170568; -.
KEGG; rno:170568; -.
UCSC; RGD:61984; rat. [Q8CIZ5-1]
CTD; 1755; -.
RGD; 61984; Dmbt1.
HOGENOM; HOG000290652; -.
HOVERGEN; HBG060122; -.
InParanoid; Q8CIZ5; -.
KO; K13912; -.
PhylomeDB; Q8CIZ5; -.
PRO; PR:Q8CIZ5; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0031012; C:extracellular matrix; IDA:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; ISO:RGD.
GO; GO:0030670; C:phagocytic vesicle membrane; ISO:RGD.
GO; GO:0005578; C:proteinaceous extracellular matrix; ISO:RGD.
GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0042589; C:zymogen granule membrane; ISS:UniProtKB.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0035375; F:zymogen binding; ISS:UniProtKB.
GO; GO:0001824; P:blastocyst development; ISO:RGD.
GO; GO:0030154; P:cell differentiation; IEP:RGD.
GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
GO; GO:0001833; P:inner cell mass cell proliferation; ISO:RGD.
GO; GO:0030858; P:positive regulation of epithelial cell differentiation; ISO:RGD.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0009611; P:response to wounding; IEP:RGD.
GO; GO:0042246; P:tissue regeneration; IEP:RGD.
CDD; cd00041; CUB; 3.
Gene3D; 2.60.120.290; -; 3.
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; 3.
Pfam; PF00530; SRCR; 4.
Pfam; PF00100; Zona_pellucida; 1.
PRINTS; PR00258; SPERACTRCPTR.
SMART; SM00042; CUB; 3.
SMART; SM00202; SR; 4.
SMART; SM00241; ZP; 1.
SUPFAM; SSF49854; SSF49854; 3.
SUPFAM; SSF56487; SSF56487; 5.
PROSITE; PS01180; CUB; 3.
PROSITE; PS00420; SRCR_1; 2.
PROSITE; PS50287; SRCR_2; 5.
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 1418 Deleted in malignant brain tumors 1
protein.
/FTId=PRO_0000045389.
TRANSMEM 1383 1403 Helical. {ECO:0000255}.
DOMAIN 70 170 SRCR 1. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 105 205 SRCR 2. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 273 373 SRCR 3. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 420 520 SRCR 4. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 574 683 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 711 820 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 844 944 SRCR 5. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 966 1075 CUB 3. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1084 1332 ZP. {ECO:0000255|PROSITE-
ProRule:PRU00375}.
COMPBIAS 524 567 Thr-rich.
MOD_RES 1406 1406 Phosphothreonine.
{ECO:0000250|UniProtKB:Q60997}.
MOD_RES 1415 1415 Phosphoserine.
{ECO:0000250|UniProtKB:Q60997}.
CARBOHYD 638 638 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 639 639 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 651 651 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 776 776 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 788 788 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 838 838 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 848 848 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 963 963 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1078 1078 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1079 1079 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1115 1115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1146 1146 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1150 1150 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1191 1191 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1207 1207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 130 194 {ECO:0000250}.
DISULFID 143 204 {ECO:0000250}.
DISULFID 174 184 {ECO:0000250}.
DISULFID 298 362 {ECO:0000250}.
DISULFID 311 372 {ECO:0000250}.
DISULFID 342 352 {ECO:0000250}.
DISULFID 445 509 {ECO:0000250}.
DISULFID 458 519 {ECO:0000250}.
DISULFID 489 499 {ECO:0000250}.
DISULFID 574 600 {ECO:0000250}.
DISULFID 625 647 {ECO:0000250}.
DISULFID 711 737 {ECO:0000250}.
DISULFID 762 784 {ECO:0000250}.
DISULFID 882 943 {ECO:0000250}.
DISULFID 913 923 {ECO:0000250}.
DISULFID 966 992 {ECO:0000250}.
DISULFID 1017 1039 {ECO:0000250}.
DISULFID 1253 1311 {ECO:0000250}.
VAR_SEQ 63 97 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_016854.
VAR_SEQ 375 375 S -> SPTSSPTPGWWNPGFTNSDVSYRTELPTDDS (in
isoform 2). {ECO:0000303|Ref.2}.
/FTId=VSP_016855.
VAR_SEQ 827 837 TPPTTFPIITG -> R (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_016856.
VAR_SEQ 866 871 VPCADD -> GTVCDN (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_016857.
VAR_SEQ 955 961 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_016858.
CONFLICT 129 129 M -> V (in Ref. 2; AAS46613).
{ECO:0000305}.
CONFLICT 164 166 LGP -> SGS (in Ref. 2; AAS46613).
{ECO:0000305}.
CONFLICT 343 343 R -> T (in Ref. 2; AAS46613).
{ECO:0000305}.
CONFLICT 462 462 V -> G (in Ref. 2; AAS46613).
{ECO:0000305}.
CONFLICT 638 638 N -> Y (in Ref. 2; AAS46613).
{ECO:0000305}.
CONFLICT 769 769 G -> V (in Ref. 2; AAS46613).
{ECO:0000305}.
CONFLICT 1058 1058 T -> I (in Ref. 2; AAS46613).
{ECO:0000305}.
CONFLICT 1106 1106 S -> A (in Ref. 2; AAS46613).
{ECO:0000305}.
CONFLICT 1319 1319 N -> Y (in Ref. 2; AAS46613).
{ECO:0000305}.
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


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