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Deleted in malignant brain tumors 1 protein (Hensin)

 DMBT1_RABIT             Reviewed;        1594 AA.
Q95218; Q95219; Q9TV20; Q9TV21; Q9TV22;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 2.
23-MAY-2018, entry version 96.
RecName: Full=Deleted in malignant brain tumors 1 protein;
AltName: Full=Hensin;
Flags: Precursor;
Name=Dmbt1;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 93-129;
732-751 AND 1083-1090, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=8941650; DOI=10.1172/JCI119044;
Takito J., Hikita C., Al-Awqati Q.;
"Hensin, a new collecting duct protein involved in the in vitro
plasticity of intercalated cell polarity.";
J. Clin. Invest. 98:2324-2331(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2),
GLYCOSYLATION, AND TISSUE SPECIFICITY.
PubMed=10444583;
Takito J., Yan L., Ma J., Hikita C., Vijayakumar S., Warburton D.,
Al-Awqati Q.;
"Hensin, the polarity reversal protein, is encoded by DMBT1, a gene
frequently deleted in malignant gliomas.";
Am. J. Physiol. 277:F277-F289(1999).
-!- 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. 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}.
-!- SUBUNIT: Interacts with LGALS3. Binds SFTPD and SPAR in a calcium-
dependent manner (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8941650}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q95218-1; Sequence=Displayed;
Name=2;
IsoId=Q95218-2; Sequence=VSP_034658, VSP_034659;
-!- TISSUE SPECIFICITY: Expressed in small intestine, liver, stomach
and kidney. Present in small intestine and in collecting tubules
of kidney cortex, medulla and papilla (at protein level).
{ECO:0000269|PubMed:10444583, ECO:0000269|PubMed:8941650}.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; AF043112; AAD02242.1; -; mRNA.
EMBL; AF078900; AAD50330.1; -; Genomic_DNA.
EMBL; AF078900; AAD50331.1; -; Genomic_DNA.
EMBL; AF078900; AAD50332.1; -; Genomic_DNA.
PIR; T30549; T30549.
RefSeq; NP_001075502.1; NM_001082033.1. [Q95218-1]
UniGene; Ocu.2321; -.
ProteinModelPortal; Q95218; -.
SMR; Q95218; -.
PRIDE; Q95218; -.
GeneID; 100008679; -.
KEGG; ocu:100008679; -.
CTD; 1755; -.
HOVERGEN; HBG060122; -.
InParanoid; Q95218; -.
KO; K13912; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
CDD; cd00041; CUB; 2.
Gene3D; 2.60.120.290; -; 2.
Gene3D; 3.10.250.10; -; 8.
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; 2.
Pfam; PF00530; SRCR; 8.
Pfam; PF00100; Zona_pellucida; 1.
PRINTS; PR00258; SPERACTRCPTR.
SMART; SM00042; CUB; 2.
SMART; SM00202; SR; 8.
SMART; SM00241; ZP; 1.
SUPFAM; SSF49854; SSF49854; 2.
SUPFAM; SSF56487; SSF56487; 8.
PROSITE; PS01180; CUB; 2.
PROSITE; PS00420; SRCR_1; 6.
PROSITE; PS50287; SRCR_2; 8.
PROSITE; PS00682; ZP_1; 1.
PROSITE; PS51034; ZP_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Developmental protein;
Differentiation; Direct protein sequencing; Disulfide bond;
Glycoprotein; Protein transport; Reference proteome; Repeat; Secreted;
Signal; Transport.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 1594 Deleted in malignant brain tumors 1
protein.
/FTId=PRO_0000343684.
DOMAIN 53 153 SRCR 1. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 192 292 SRCR 2. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 323 423 SRCR 3. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 454 551 SRCR 4. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 582 682 SRCR 5. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 713 813 SRCR 6. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 821 921 SRCR 7. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 951 1061 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1067 1170 SRCR 8. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 1192 1301 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1310 1558 ZP. {ECO:0000255|PROSITE-
ProRule:PRU00375}.
COMPBIAS 41 44 Poly-Thr.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 458 458 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 717 717 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 78 142 {ECO:0000250}.
DISULFID 91 152 {ECO:0000250}.
DISULFID 122 132 {ECO:0000250}.
DISULFID 217 281 {ECO:0000250}.
DISULFID 230 291 {ECO:0000250}.
DISULFID 261 271 {ECO:0000250}.
DISULFID 348 412 {ECO:0000250}.
DISULFID 361 422 {ECO:0000250}.
DISULFID 392 402 {ECO:0000250}.
DISULFID 476 540 {ECO:0000250}.
DISULFID 489 550 {ECO:0000250}.
DISULFID 520 530 {ECO:0000250}.
DISULFID 607 671 {ECO:0000250}.
DISULFID 620 681 {ECO:0000250}.
DISULFID 651 661 {ECO:0000250}.
DISULFID 738 802 {ECO:0000250}.
DISULFID 751 812 {ECO:0000250}.
DISULFID 782 792 {ECO:0000250}.
DISULFID 846 910 {ECO:0000250}.
DISULFID 859 920 {ECO:0000250}.
DISULFID 890 900 {ECO:0000250}.
DISULFID 951 977 {ECO:0000250}.
DISULFID 1004 1025 {ECO:0000250}.
DISULFID 1095 1159 {ECO:0000250}.
DISULFID 1108 1169 {ECO:0000250}.
DISULFID 1139 1149 {ECO:0000250}.
DISULFID 1192 1218 {ECO:0000250}.
DISULFID 1243 1265 {ECO:0000250}.
DISULFID 1479 1537 {ECO:0000250}.
VAR_SEQ 45 302 EVFPSGLELRLANGGDRCQGRVEVLYQGSWGTVCDDGWDIN
DAQVVCRQLGCGMAVSAPGSARFGQGPGQIVLDDVSCSGQE
PYLWSCHHRGWLSHNCGHQEDAGVICSDAMAMTSPPPDTWP
TTVIYESTPHFPSGLELVFPSGLELRLANGSDRCQGRVEVL
YQGSWGTVCDDGWDINDAQVVCRQLGCGMAVSAPGSARFGQ
GPGQIVLDDVSCSGQEPYLWSCHHRGWLSHNCGHQEDAGVI
CSDAVPTTTPPP -> TE (in isoform 2).
{ECO:0000303|PubMed:10444583}.
/FTId=VSP_034658.
VAR_SEQ 361 488 Missing (in isoform 2).
{ECO:0000303|PubMed:10444583}.
/FTId=VSP_034659.
CONFLICT 40 40 E -> EA (in Ref. 2; AAD50330).
{ECO:0000305}.
CONFLICT 41 41 T -> A (in Ref. 2; AAD50332/AAD50331).
{ECO:0000305}.
CONFLICT 160 160 S -> T (in Ref. 2; AAD50330).
{ECO:0000305}.
CONFLICT 177 185 HFPSGLELV -> L (in Ref. 2; AAD50330).
{ECO:0000305}.
CONFLICT 198 198 S -> G (in Ref. 2; AAD50330).
{ECO:0000305}.
CONFLICT 314 314 S -> T (in Ref. 2; AAD50332/AAD50331).
{ECO:0000305}.
CONFLICT 329 329 S -> G (in Ref. 2; AAD50332/AAD50331).
{ECO:0000305}.
CONFLICT 575 575 H -> L (in Ref. 2; AAD50332/AAD50331).
{ECO:0000305}.
CONFLICT 588 588 S -> G (in Ref. 2; AAD50332/AAD50331).
{ECO:0000305}.
CONFLICT 627 627 T -> M (in Ref. 2; AAD50332/AAD50331).
{ECO:0000305}.
CONFLICT 744 744 L -> I (in Ref. 1; AA sequence).
{ECO:0000305}.
SEQUENCE 1594 AA; 172764 MW; 29D6BEFEAA987CC4 CRC64;
MGISTVLALS LLWGPALSQG QWIPYTTYHD SVSSPGAPVE TTTTEVFPSG LELRLANGGD
RCQGRVEVLY QGSWGTVCDD GWDINDAQVV CRQLGCGMAV SAPGSARFGQ GPGQIVLDDV
SCSGQEPYLW SCHHRGWLSH NCGHQEDAGV ICSDAMAMTS PPPDTWPTTV IYESTPHFPS
GLELVFPSGL ELRLANGSDR CQGRVEVLYQ GSWGTVCDDG WDINDAQVVC RQLGCGMAVS
APGSARFGQG PGQIVLDDVS CSGQEPYLWS CHHRGWLSHN CGHQEDAGVI CSDAVPTTTP
PPDTWPTTVI YESSPVFPSG LELRLANGSD RCQGRVEVLY QGSWGTVCDD GWDINDAQVV
CRQLGCGTAV SAPGSARFGQ GPGQIVLDDV SCSGQEPYLW SCHHRGWLSH NCGHQEDAGV
ICSDAMAMTT PLPDTWPTTV IHESTPVFPS GLELQLANGS DRCQGRVEVL YQGTVCDDGW
DINDAQVVCR QLGCGMAVSA PGSARFGQGP GQIVLDDVSC SGQEPYLWSC HHRGWLSHNC
GHQEDAGVIC SDAMAMTTPP PDTWPTTVIY ESTPHFPSGL ELRLANGSDR CQGRVEVLYQ
GSWGTVCDDG WDINDAQVVC RQLGCGTAVS APGSARFGQG PGQIVLDDVS CSGQEPYLWS
CHHRGWLSHN CGHQEDAGVI CSGAMDTTTP LPDTWPTTVI YESTPVHISG LQLRLVNGSD
RCEGRVEVLY QGSWGTVCDD SWDLNDASVV CRQLGCGTAL SAPASAQFGQ SSGSIVLDDV
SCSGSEPNLW SCSHRGWLSH NCGHHEDAGV VCSGPDSRLA VRLVNGSTRC QGRVEVLYRG
SWGTVCDDSW DINDASVVCR QLGCGWAVSA PGSARFGQGS GSIFLDEVSC SGQEPYLWNC
SHRGWLSHNC GHYEDAGVIC SDGWTTVTPP APTTDWWEPT VTTTVGPSSN CGGFLYNATG
SFSSPSYPGY YPNNALCVWE IAVPSGYLIN LGFSQLRLEQ HSYCNFDYVE IFDGSTDSSL
LGKICNDSGQ IFTTSSNRMT VLFRSDISVQ NTGFLAWYNS FPRDASLRLV SGNSSYGACA
GRVEIYHGGR WGTVCDDSWD TQDAQVVCRQ LQCGDAVSAP GGAYFGSGSG PITLDDVNCS
GTEATLWQCR SQSWFSHNCG HHEDASVICT GNYGTTTASV PNISTSNASY SCGGFLSQHS
GRFSSPFYPG NYPNNARCVW DIEVQNNYQV TVTFTDVQLE GGCQYDYIEV FDGPYHSSPL
IARVCDGARG SFTSSSNFLS VRFVSDGSIT RRGFQAEFYS LPSNDSTNLL CLMNHMQASV
SRAYLQSLGF SAWELVVSGW NGNYQCQRQI TPSQVIFTIP YSGCGTIKQV DNETITYSNF
LKAAVSSGVI KRKKDLHIHV SCRMLQDSWV HTMYIANDTI EVSEVQYSNF NVNVSFYTSS
SFSYPVTSSP YYVDLDQNLY LQAEILHSDA SLALFVDTCV ASPNPNDFTS VTYDLIRSGC
VRDETYRSYA QPSPRVVRFR FNSFHFLNRF PAVYLRCKMV VCRAYDYSSR CYRGCVVRSK
RDVGSYQERV DVVLGPIQLL DPPAGKKSPG KGSP


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