DMBT1_PIG
ID DMBT1_PIG Reviewed; 1204 AA.
AC Q4A3R3; Q0W9P8; Q95316;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Deleted in malignant brain tumors 1 protein;
DE AltName: Full=Hensin;
DE Flags: Precursor;
GN Name=DMBT1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=15922517; DOI=10.1016/j.gene.2005.04.015;
RA Haase B., Schloetterer C., Hundrieser M.E., Kuiper H., Distl O.,
RA Topfer-Petersen E., Leeb T.;
RT "Evolution of the spermadhesin gene family.";
RL Gene 352:20-29(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=16624504; DOI=10.1016/j.gene.2006.03.002;
RA Haase B., Humphray S.J., Lyer S., Renner M., Poustka A., Mollenhauer J.,
RA Leeb T.;
RT "Molecular characterization of the porcine deleted in malignant brain
RT tumors 1 gene (DMBT1).";
RL Gene 376:184-191(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 355-481 (ISOFORM 1).
RC TISSUE=Small intestine;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA
RT library.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play roles in mucosal defense system and cellular immune
CC defense. May play a role in liver regeneration. May be an important
CC factor in fate decision and differentiation of transit-amplifying
CC ductular (oval) cells within the hepatic lineage. May function as a
CC binding protein in saliva for the regulation of taste sensation. May
CC play a role as an opsonin receptor for SFTPD and SPAR in macrophage
CC tissues throughout the body, including epithelial cells lining the
CC gastrointestinal tract. Required for terminal differentiation of
CC columnar epithelial cells during early embryogenesis. Displays a broad
CC calcium-dependent binding spectrum against both Gram-positive and Gram-
CC negative bacteria, suggesting a role in defense against bacterial
CC pathogens. Binds to a range of poly-sulfated and poly-phosphorylated
CC ligands which may explain its broad bacterial-binding specificity.
CC Inhibits cytoinvasion of S.enterica. Associates with the actin
CC cytoskeleton and is involved in its remodeling during regulated
CC exocytosis. Interacts with pancreatic zymogens in a pH-dependent manner
CC and may act as a Golgi cargo receptor in the regulated secretory
CC pathway of the pancreatic acinar cell (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with LGALS3. Binds SFTPD and SPAR in a calcium-
CC dependent manner (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasmic vesicle,
CC secretory vesicle membrane {ECO:0000250}; Single-pass membrane protein
CC {ECO:0000250}; Lumenal side {ECO:0000250}. Note=Localized to the
CC lumenal aspect of crypt cells in the small intestine. In the colon,
CC seen in the lumenal aspect of surface epithelial cells (By similarity).
CC Formed in the ducts of von Ebner gland and released into the fluid
CC bathing the taste buds contained in the taste papillae (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4A3R3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4A3R3-2; Sequence=VSP_034657;
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}.
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DR EMBL; AJ853849; CAJ27171.1; -; Genomic_DNA.
DR EMBL; AM048631; CAJ14977.1; -; mRNA.
DR EMBL; Z81180; CAB03556.1; -; mRNA.
DR RefSeq; NP_001041653.1; NM_001048188.1.
DR AlphaFoldDB; Q4A3R3; -.
DR SMR; Q4A3R3; -.
DR STRING; 9823.ENSSSCP00000020105; -.
DR PaxDb; Q4A3R3; -.
DR PeptideAtlas; Q4A3R3; -.
DR PRIDE; Q4A3R3; -.
DR GeneID; 751862; -.
DR KEGG; ssc:751862; -.
DR CTD; 1755; -.
DR eggNOG; ENOG502RSDM; Eukaryota.
DR InParanoid; Q4A3R3; -.
DR OrthoDB; 1095487at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042589; C:zymogen granule membrane; ISS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0035375; F:zymogen binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR CDD; cd00041; CUB; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 2.60.40.4100; -; 1.
DR Gene3D; 3.10.250.10; -; 4.
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; 2.
DR Pfam; PF00530; SRCR; 4.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00202; SR; 4.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF56487; SSF56487; 4.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00420; SRCR_1; 3.
DR PROSITE; PS50287; SRCR_2; 4.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasmic vesicle; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Membrane; Protein transport;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1204
FT /note="Deleted in malignant brain tumors 1 protein"
FT /id="PRO_0000045390"
FT TRANSMEM 1168..1188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 84..184
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 232..332
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 380..480
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 517..628
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 634..737
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 752..861
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 870..1118
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 932
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 977
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1029
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..173
FT /evidence="ECO:0000250"
FT DISULFID 122..183
FT /evidence="ECO:0000250"
FT DISULFID 153..163
FT /evidence="ECO:0000250"
FT DISULFID 257..321
FT /evidence="ECO:0000250"
FT DISULFID 270..331
FT /evidence="ECO:0000250"
FT DISULFID 301..311
FT /evidence="ECO:0000250"
FT DISULFID 405..469
FT /evidence="ECO:0000250"
FT DISULFID 418..479
FT /evidence="ECO:0000250"
FT DISULFID 449..459
FT /evidence="ECO:0000250"
FT DISULFID 517..543
FT /evidence="ECO:0000250"
FT DISULFID 570..592
FT /evidence="ECO:0000250"
FT DISULFID 662..726
FT /evidence="ECO:0000250"
FT DISULFID 675..736
FT /evidence="ECO:0000250"
FT DISULFID 706..716
FT /evidence="ECO:0000250"
FT DISULFID 752..778
FT /evidence="ECO:0000250"
FT DISULFID 803..825
FT /evidence="ECO:0000250"
FT DISULFID 1039..1097
FT /evidence="ECO:0000250"
FT VAR_SEQ 78
FT /note="T -> TEWDLALRLVNGGDRCQGRVEILYQGSWGTVCDDSWDTNDANVVCRQ
FT LGCGWAISAPGSARFGQGSGPILLDDLRCSGHETYLWSCPHSGWKTHNCGHQEDAGVIC
FT SGAQRSSTVIPAWWHPTTTTTATSSFHTEEPLTTIAAEGT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16624504"
FT /id="VSP_034657"
FT CONFLICT 445
FT /note="D -> G (in Ref. 3; CAB03556)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1204 AA; 132225 MW; 939E8B7F4825B976 CRC64;
MGTSAVILEI CLLLSQVLTT VSSTTQTEST TEDRTQITET AFWETQTINS VSESDLPGTH
ASSFHTEEPL TTIAAEGTEW DLALRLVNGG DRCQGRVEIL YQGSWGTVCD DSWDTNDANV
VCRQLGCGWA VSAPGSARFG QGLGPILLDD LRCSGHETYL WSCPHSGWKT HNCGHQEDAG
VICSGAQRSS TVIPDWWYTT TRSQTAHIRS TIPAWWHPTT TTAARTEWDL ALRLVNGGDR
CQGRVEVLYQ GSWGTVCDDS WDTNDANVVC RQLGCGWAVS APGSARFGQG SGPILLDDLR
CSGHETYLWS CPHSGWNTHN CGHHEDAGVI CSDAQRSSTV IPDWWYTTTP SQTAHIRSTI
PAWWHPTTTT AARTEWDLAL RLVNGGDRCQ GRVEVLYQGS WGTVCDDSWD TNDANVVCRQ
LGCGWAVSAP GSARFGQGSG PILLDDLRCS GHETYLWSCP HSGWNTHNCG HHEDAGVICS
DAQRSSTVIP DWWYTTTPSQ TWWHPTTTTA ASPSSPCGGF LTSASGTFSS PSYPGLYPNN
ANCVWEIEVN SGYRINLGFN NLQLEVHINC IYDYIEIFDE SPGSNTSLGK ICNHTSQIFT
SSYNRMTVRF RSDGSVQKPG FSAWYNSFPR DASLRLVNSN SSYPSCAGRV EIYQGGRWGT
VCDDGWDIQD AQVVCRQLGC GNAVSAPGNA YFGPGSGPIT LDDVACSGTE STLWQCRNRG
WFSHNCGHSE DAGVICSVPA FTTTPPATNY SCGGFLSQAA GGFNSPFYPG NYPNNANCVW
DIEVQNNYRV TVVFRDVQLE SGCNFDYIEV FDGPYRSSPL LARVCNGASG SFTSSSNFMS
IRFISDVSVT RAGFRANYYS SPSSGSTRLH CLQNHMQASV STSYLQSLGY SARDLVIPGW
EWSYQCQPQI TSTQVTFTIP YSSCGTIQRV DNDTITYSNS LRAAVSSGII KRKKDLNMYV
SCRMLQNTWV NTVYIANDTL EVQNVQYGNF DVNISFFTSS SFLYPVRSSP YYVDLNQNLY
LQAELLHANA SLALFVDTCV ASPYPNDFTT LTYDLIRSGC VKDETYQSYS QPSPRIVRFK
FSSFHFLSRF PSVYLQCKMV VCRAFDSSSR CRRGCVVRSK RDVGSYQEKV DVVLGPIQLQ
TLHAEKRSLD QPAVDLEEKA SAQGSYDGAA ISAGIFLVVV LAVAAFTLGR RGRAADGQPL
ISKT
