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Deleted in malignant brain tumors 1 protein (Glycoprotein 340) (Gp-340) (Hensin) (Salivary agglutinin) (SAG) (Surfactant pulmonary-associated D-binding protein)

 DMBT1_HUMAN             Reviewed;        2413 AA.
Q9UGM3; A6NDG4; A6NDJ5; A8E4R5; B1ARE7; B1ARE8; B1ARE9; B1ARF0;
B7Z8Y2; F8WEF7; Q59EX0; Q5JR26; Q6MZN4; Q96DU4; Q9UGM2; Q9UJ57;
Q9UKJ4; Q9Y211; Q9Y4V9;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
10-JAN-2006, sequence version 2.
22-NOV-2017, entry version 159.
RecName: Full=Deleted in malignant brain tumors 1 protein;
AltName: Full=Glycoprotein 340;
Short=Gp-340;
AltName: Full=Hensin;
AltName: Full=Salivary agglutinin;
Short=SAG;
AltName: Full=Surfactant pulmonary-associated D-binding protein;
Flags: Precursor;
Name=DMBT1; Synonyms=GP340;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION AS A TUMOR
SUPPRESSOR, TISSUE SPECIFICITY, AND VARIANTS THR-42 AND ALA-60.
TISSUE=Lung;
PubMed=9288095; DOI=10.1038/ng0997-32;
Mollenhauer J., Wiemann S., Scheurlen W., Korn B., Hayashi Y.,
Wilgenbus K.K., von Deimling A., Poustka A.;
"DMBT1, a new member of the SRCR superfamily on chromosome 10q25.3-
q26.1 is deleted in malignant brain tumours.";
Nat. Genet. 17:32-39(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN MUCOSAL AND
CELLULAR IMMUNE DEFENSE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
DEVELOPMENTAL STAGE, AND VARIANTS THR-42; LEU-54; ALA-60; MET-649;
MET-780 AND SER-856.
TISSUE=Trachea;
PubMed=10485905; DOI=10.1073/pnas.96.19.10794;
Holmskov U., Mollenhauer J., Madsen J., Vitved L., Gronlund J.,
Tornoe I., Kliem A., Reid K.B.M., Poustka A., Skjodt K.;
"Cloning of gp-340, a putative opsonin receptor for lung surfactant
protein D.";
Proc. Natl. Acad. Sci. U.S.A. 96:10794-10799(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), ALTERNATIVE
SPLICING, AND VARIANTS THR-42; LEU-54; ALA-60; LEU-337 AND SER-856.
TISSUE=Lung;
PubMed=10597221; DOI=10.1038/sj.onc.1203071;
Mollenhauer J., Holmskov U., Wiemann S., Krebs I., Herbertz S.,
Madsen J., Kioschis P., Coy J.F., Poustka A.;
"The genomic structure of the DMBT1 gene: evidence for a region with
susceptibility to genomic instability.";
Oncogene 18:6233-6240(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN LUNG CARCINOGENESIS,
AND VARIANTS THR-42; LEU-54 AND SER-856.
PubMed=10551316; DOI=10.1111/j.1349-7006.1999.tb00833.x;
Takeshita H., Sato M., Shiwaku H.O., Semba S., Sakurada A., Hoshi M.,
Hayashi Y., Tagawa Y., Ayabe H., Horii A.;
"Expression of the DMBT1 gene is frequently suppressed in human lung
cancer.";
Jpn. J. Cancer Res. 90:903-908(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN EPITHELIAL DIFFERENTIATION,
TISSUE SPECIFICITY, ALTERNATIVE SPLICING, INVOLVEMENT IN ESOPHAGEAL
CARCINOMAS, AND VARIANT SER-856.
TISSUE=Small intestine;
PubMed=11751412;
Mollenhauer J., Herbertz S., Helmke B., Kollender G., Krebs I.,
Madsen J., Holmskov U., Sorger K., Schmitt L., Wiemann S., Otto H.F.,
Grone H.-J., Poustka A.;
"Deleted in malignant brain tumors 1 is a versatile mucin-like
molecule likely to play a differential role in digestive tract
cancer.";
Cancer Res. 61:8880-8886(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8), AND VARIANT
LEU-54.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-1480 (ISOFORM 4).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1689-2413 (ISOFORM 5).
TISSUE=Small intestine;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[11]
PROTEIN SEQUENCE OF 2385-2413, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Tear;
PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
Suarez T., Elortza F.;
"Human basal tear peptidome characterization by CID, HCD, and ETD
followed by in silico and in vitro analyses for antimicrobial peptide
identification.";
J. Proteome Res. 14:2649-2658(2015).
[12]
INTERACTION WITH SFTPD.
PubMed=9153228; DOI=10.1074/jbc.272.21.13743;
Holmskov U., Lawson P., Teisner B., Tornoe I., Willis A.C., Morgan C.,
Koch C., Reid K.B.;
"Isolation and characterization of a new member of the scavenger
receptor superfamily, glycoprotein-340 (gp-340), as a lung surfactant
protein-D binding molecule.";
J. Biol. Chem. 272:13743-13749(1997).
[13]
INTERACTION WITH SPAR.
PubMed=10101009; DOI=10.1165/ajrcmb.20.4.3439;
Tino M.J., Wright J.R.;
"Glycoprotein-340 binds surfactant protein-A (SP-A) and stimulates
alveolar macrophage migration in an SP-A-independent manner.";
Am. J. Respir. Cell Mol. Biol. 20:759-768(1999).
[14]
INVOLVEMENT IN ESOPHAGEAL; GASTRIC AND COLON CANCERS.
PubMed=9888459; DOI=10.1038/sj.bjc.6690035;
Mori M., Shiraishi T., Tanaka S., Yamagata M., Mafune K., Tanaka Y.,
Ueo H., Barnard G.F., Sugimachi K.;
"Lack of DMBT1 expression in oesophageal, gastric and colon cancers.";
Br. J. Cancer 79:211-213(1999).
[15]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=10749143;
Mollenhauer J., Herbertz S., Holmskov U., Tolnay M., Krebs I.,
Merlo A., Schroder H.D., Maier D., Breitling F., Wiemann S.,
Groene H.-J., Poustka A.;
"DMBT1 encodes a protein involved in the immune defense and in
epithelial differentiation and is highly unstable in cancer.";
Cancer Res. 60:1704-1710(2000).
[16]
IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
TISSUE=Saliva;
PubMed=11007786; DOI=10.1074/jbc.M006928200;
Prakobphol A., Xu F., Hoang V.M., Larsson T., Bergstrom J.,
Johansson I., Fraengsmyr L., Holmskov U., Leffler H., Nilsson C.,
Boren T., Wright J.R., Stroemberg N., Fisher S.J.;
"Salivary agglutinin, which binds Streptococcus mutans and
Helicobacter pylori, is the lung scavenger receptor cysteine-rich
protein gp-340.";
J. Biol. Chem. 275:39860-39866(2000).
[17]
BACTERIAL-BINDING DOMAIN.
PubMed=15355985; DOI=10.1074/jbc.M406095200;
Bikker F.J., Ligtenberg A.J.M., End C., Renner M., Blaich S., Lyer S.,
Wittig R., van't Hof W., Veerman E.C.I., Nazmi K.,
de Blieck-Hogervorst J.M.A., Kioschis P., Nieuw Amerongen A.V.,
Poustka A., Mollenhauer J.;
"Bacteria binding by DMBT1/SAG/gp-340 is confined to the VEVLXXXXW
motif in its scavenger receptor cysteine-rich domains.";
J. Biol. Chem. 279:47699-47703(2004).
[18]
FUNCTION, INTERACTION WITH HIV-1 GP120, AND TISSUE SPECIFICITY.
PubMed=16796526; DOI=10.1089/aid.2006.22.508;
Wu Z., Lee S., Abrams W., Weissman D., Malamud D.;
"The N-terminal SRCR-SID domain of gp-340 interacts with HIV type 1
gp120 sequences and inhibits viral infection.";
AIDS Res. Hum. Retroviruses 22:508-515(2006).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1712; ASN-1889 AND
ASN-2188.
TISSUE=Saliva;
PubMed=16740002; DOI=10.1021/pr050492k;
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
Loo J.A.;
"Identification of N-linked glycoproteins in human saliva by
glycoprotein capture and mass spectrometry.";
J. Proteome Res. 5:1493-1503(2006).
[20]
TISSUE SPECIFICITY.
PubMed=17983803; DOI=10.1053/j.gastro.2007.08.007;
Renner M., Bergmann G., Krebs I., End C., Lyer S., Hilberg F.,
Helmke B., Gassler N., Autschbach F., Bikker F.,
Strobel-Freidekind O., Gronert-Sum S., Benner A., Blaich S.,
Wittig R., Hudler M., Ligtenberg A.J., Madsen J., Holmskov U.,
Annese V., Latiano A., Schirmacher P., Amerongen A.V.N., D'Amato M.,
Kioschis P., Hafner M., Poustka A., Mollenhauer J.;
"DMBT1 confers mucosal protection in vivo and a deletion variant is
associated with Crohn's disease.";
Gastroenterology 133:1499-1509(2007).
[21]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=17548659; DOI=10.4049/jimmunol.178.12.8203;
Rosenstiel P., Sina C., End C., Renner M., Lyer S., Till A.,
Hellmig S., Nikolaus S., Foelsch U.R., Helmke B., Autschbach F.,
Schirmacher P., Kioschis P., Hafner M., Poustka A., Mollenhauer J.,
Schreiber S.;
"Regulation of DMBT1 via NOD2 and TLR4 in intestinal epithelial cells
modulates bacterial recognition and invasion.";
J. Immunol. 178:8203-8211(2007).
[22]
FUNCTION.
PubMed=17709527; DOI=10.4049/jimmunol.179.5.3126;
Stoddard E., Cannon G., Ni H., Kariko K., Capodici J., Malamud D.,
Weissman D.;
"gp340 expressed on human genital epithelia binds HIV-1 envelope
protein and facilitates viral transmission.";
J. Immunol. 179:3126-3132(2007).
[23]
BACTERIAL-BINDING DOMAIN.
PubMed=18713006; DOI=10.1515/BC.2008.135;
Leito J.T.D., Ligtenberg A.J.M., Nazmi K.,
de Blieck-Hogervorst J.M.A., Veerman E.C.I., Nieuw Amerongen A.V.;
"A common binding motif for various bacteria of the bacteria-binding
peptide SRCRP2 of DMBT1/gp-340/salivary agglutinin.";
Biol. Chem. 389:1193-1200(2008).
[24]
FUNCTION.
PubMed=19189310; DOI=10.1002/eji.200838689;
End C., Bikker F., Renner M., Bergmann G., Lyer S., Blaich S.,
Hudler M., Helmke B., Gassler N., Autschbach F., Ligtenberg A.J.M.,
Benner A., Holmskov U., Schirmacher P., Nieuw Amerongen A.V.,
Rosenstiel P., Sina C., Franke A., Hafner M., Kioschis P.,
Schreiber S., Poustka A., Mollenhauer J.;
"DMBT1 functions as pattern-recognition molecule for poly-sulfated and
poly-phosphorylated ligands.";
Eur. J. Immunol. 39:833-842(2009).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
VARIANTS THR-42; TRP-52; LEU-54; GLU-162; ASP-322; SER-357; SER-546;
PRO-1095; THR-1102; TRP-1434; SER-1732 AND MET-2255.
PubMed=12353266; DOI=10.1002/gcc.10115;
Mollenhauer J., Mueller H., Kollender G., Lyer S., Diedrichs L.,
Helmke B., Holmskov U., Ligtenberg T., Herbertz S., Krebs I.,
Madsen J., Bikker F., Schmitt L., Wiemann S., Scheurlen W., Otto H.F.,
von Deimling A., Poustka A.;
"The SRCR/SID region of DMBT1 defines a complex multi-allele system
representing the major basis for its variability in cancer.";
Genes Chromosomes Cancer 35:242-255(2002).
[27]
VARIANTS THR-42; TRP-52; LEU-54; ALA-60; LEU-65; LEU-337; SER-357;
GLY-364; MET-649; MET-780; TYR-1084; THR-1169; TRP-1176; MET-1545;
SER-1732 AND PRO-1961.
PubMed=12185598; DOI=10.1038/sj.onc.1205733;
Mueller W., Mollenhauer J., Stockhammer F., Poustka A.,
von Deimling A.;
"Rare mutations of the DMBT1 gene in human astrocytic gliomas.";
Oncogene 21:5956-5959(2002).
-!- FUNCTION: May be considered as a candidate tumor suppressor gene
for brain, lung, esophageal, gastric, and colorectal cancers. May
play roles in mucosal defense system, cellular immune defense and
epithelial differentiation. 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. 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. Required for terminal
differentiation of columnar epithelial cells during early
embryogenesis. May function as a binding protein in saliva for the
regulation of taste sensation. Binds to HIV-1 envelope protein and
has been shown to both inhibit and facilitate viral transmission.
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. {ECO:0000269|PubMed:10485905,
ECO:0000269|PubMed:11007786, ECO:0000269|PubMed:11751412,
ECO:0000269|PubMed:16796526, ECO:0000269|PubMed:17548659,
ECO:0000269|PubMed:17709527, ECO:0000269|PubMed:19189310,
ECO:0000269|PubMed:9288095}.
-!- SUBUNIT: Interacts with LGALS3 (By similarity). Binds SFTPD and
SPAR in a calcium-dependent manner. Binds to HIV-1 glycoprotein
120. {ECO:0000250, ECO:0000269|PubMed:10101009,
ECO:0000269|PubMed:16796526, ECO:0000269|PubMed:9153228}.
-!- INTERACTION:
Q8IWL2:SFTPA1; NbExp=2; IntAct=EBI-1044970, EBI-11316418;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Some isoforms
may be membrane-bound. Localized to the lumenal aspect of crypt
cells in the small intestine. In the colon, seen in the lumenal
aspect of surface epithelial cells. Formed in the ducts of von
Ebner gland, and released into the fluid bathing the taste buds
contained in the taste papillae (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Comment=More isoforms may exist.;
Name=1; Synonyms=DMBT1/8kb.2;
IsoId=Q9UGM3-1; Sequence=Displayed;
Name=2; Synonyms=DMBT1/6kb.1;
IsoId=Q9UGM3-2; Sequence=VSP_016846, VSP_016849;
Name=3; Synonyms=DMBT1/8kb.1;
IsoId=Q9UGM3-3; Sequence=VSP_016847;
Name=4;
IsoId=Q9UGM3-4; Sequence=VSP_016848;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q9UGM3-6; Sequence=VSP_034656;
Name=7;
IsoId=Q9UGM3-7; Sequence=VSP_016847, VSP_034656;
Name=8;
IsoId=Q9UGM3-8; Sequence=VSP_034653, VSP_034654, VSP_034655;
Name=5;
IsoId=Q9UGM3-5; Sequence=VSP_016850;
Note=No experimental confirmation available.;
Name=9;
IsoId=Q9UGM3-9; Sequence=VSP_053979, VSP_053980, VSP_053981;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in alveolar and macrophage
tissues. In some macrophages, expression is seen on the membrane,
and in other macrophages, strongly expressed in the
phagosome/phagolysosome compartments. Expressed in lung, trachea,
salivary gland, small intestine and stomach. In pancreas,
expressed in certain cells of the islets of Langerhans. In
digestive tract, confined to tissues with large epithelial
surfaces. In intestinal tissue, moderately expressed in epithelial
cells of the midcrypts and the crypt base. Expression is
significantly elevated in intestinal tissue from patients with
inflammatory bowel disease (IBD), particularly in surface
epithelial and Paneth cells, but not in IBD patients with mutant
NOD2. Present in crypt bases of the duodenum, in crypt tops of the
colon, and in collecting ducts of the cortical kidney. Expressed
in stratified squamous epithelium of vagina and in outer luminar
surface and basilar region of columnar epithelial cells in cervix
(at protein level). Isoform 1 is secreted to the lumen of the
respiratory tract. {ECO:0000269|PubMed:10485905,
ECO:0000269|PubMed:10749143, ECO:0000269|PubMed:11751412,
ECO:0000269|PubMed:16796526, ECO:0000269|PubMed:17548659,
ECO:0000269|PubMed:17983803, ECO:0000269|PubMed:9288095}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal lung, intestine and skin.
Secreted to the extracellular matrix (ECM) in certain fetal
epithelia. {ECO:0000269|PubMed:10485905,
ECO:0000269|PubMed:10749143}.
-!- INDUCTION: Up-regulated in intestinal epithelial cells in response
to proinflammatory stimuli including TNF and bacterial
lipopolysaccharides (LPS). {ECO:0000269|PubMed:17548659}.
-!- DOMAIN: The SRCR domains mediate binding to bacteria. The minimal
bacterial-binding site is an 11-residue repeat of GRVEVLYRGSW
where VEVL and W are critical residues.
-!- PTM: Highly N- and O-glycosylated. The O-glycans are heavily
sulfated (By similarity). {ECO:0000250}.
-!- POLYMORPHISM: The number of SRCR and SRCR-interspersed domains is
polymorphic in a variety of tumors and may represent the major
site of alterations in cancer.
-!- DISEASE: Glioma (GLM) [MIM:137800]: Gliomas are benign or
malignant central nervous system neoplasms derived from glial
cells. They comprise astrocytomas and glioblastoma multiforme that
are derived from astrocytes, oligodendrogliomas derived from
oligodendrocytes and ependymomas derived from ependymocytes.
Note=The gene represented in this entry is involved in disease
pathogenesis. Homozygous deletions may be the predominant
mechanism of DMBT1 inactivation playing a role in carcinogenesis.
DMBT1 is deleted in medulloblastoma and glioblastoma cell lines;
point mutations have also been reported in patients with glioma. A
loss or reduction of DMBT1 expression has been seen in esophageal,
gastric, lung and colorectal carcinomas as well.
-!- SIMILARITY: Belongs to the DMBT1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DMBT1ID309ch10q26.html";
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EMBL; AJ000342; CAA04019.1; -; mRNA.
EMBL; AF159456; AAD49696.1; -; mRNA.
EMBL; AJ243212; CAB56155.1; -; mRNA.
EMBL; AJ243211; CAB63941.1; -; Genomic_DNA.
EMBL; AJ243224; CAB63942.1; -; mRNA.
EMBL; AB020851; BAA78577.1; -; Genomic_DNA.
EMBL; AJ297935; CAC44122.1; -; mRNA.
EMBL; AK304149; BAH14118.1; -; mRNA.
EMBL; AL603764; CAI14487.1; -; Genomic_DNA.
EMBL; AL603764; CAI14488.1; -; Genomic_DNA.
EMBL; AL603764; CAI14489.1; -; Genomic_DNA.
EMBL; AL603764; CAI14490.1; -; Genomic_DNA.
EMBL; AL603764; CAI14491.1; -; Genomic_DNA.
EMBL; AL603764; CAI14492.1; -; Genomic_DNA.
EMBL; AL603764; CAI14493.1; -; Genomic_DNA.
EMBL; AL603764; CAI14494.1; -; Genomic_DNA.
EMBL; AL603764; CAI14495.1; -; Genomic_DNA.
EMBL; AL603764; CAI14496.1; -; Genomic_DNA.
EMBL; BC153299; AAI53300.1; -; mRNA.
EMBL; AB209691; BAD92928.1; -; mRNA.
EMBL; BX640988; CAE45995.1; -; mRNA.
CCDS; CCDS44490.1; -. [Q9UGM3-1]
CCDS; CCDS44491.1; -. [Q9UGM3-2]
CCDS; CCDS44492.1; -. [Q9UGM3-3]
PIR; A59386; A59386.
RefSeq; NP_001307573.1; NM_001320644.1.
RefSeq; NP_004397.2; NM_004406.2. [Q9UGM3-2]
RefSeq; NP_015568.2; NM_007329.2. [Q9UGM3-1]
RefSeq; NP_060049.2; NM_017579.2. [Q9UGM3-3]
RefSeq; XP_011537690.1; XM_011539388.2. [Q9UGM3-6]
RefSeq; XP_011537693.1; XM_011539391.2. [Q9UGM3-7]
RefSeq; XP_011537707.1; XM_011539405.2. [Q9UGM3-1]
UniGene; Hs.279611; -.
ProteinModelPortal; Q9UGM3; -.
SMR; Q9UGM3; -.
BioGrid; 108095; 17.
DIP; DIP-50763N; -.
IntAct; Q9UGM3; 7.
STRING; 9606.ENSP00000357905; -.
iPTMnet; Q9UGM3; -.
PhosphoSitePlus; Q9UGM3; -.
BioMuta; DMBT1; -.
DMDM; 85687556; -.
PaxDb; Q9UGM3; -.
PeptideAtlas; Q9UGM3; -.
PRIDE; Q9UGM3; -.
DNASU; 1755; -.
Ensembl; ENST00000330163; ENSP00000327747; ENSG00000187908. [Q9UGM3-2]
Ensembl; ENST00000338354; ENSP00000342210; ENSG00000187908. [Q9UGM3-1]
Ensembl; ENST00000344338; ENSP00000343175; ENSG00000187908. [Q9UGM3-3]
Ensembl; ENST00000368909; ENSP00000357905; ENSG00000187908. [Q9UGM3-1]
Ensembl; ENST00000368955; ENSP00000357951; ENSG00000187908. [Q9UGM3-3]
Ensembl; ENST00000368956; ENSP00000357952; ENSG00000187908. [Q9UGM3-2]
Ensembl; ENST00000619379; ENSP00000484603; ENSG00000187908. [Q9UGM3-1]
GeneID; 1755; -.
KEGG; hsa:1755; -.
UCSC; uc001lgk.1; human. [Q9UGM3-1]
CTD; 1755; -.
DisGeNET; 1755; -.
EuPathDB; HostDB:ENSG00000187908.15; -.
GeneCards; DMBT1; -.
H-InvDB; HIX0026114; -.
HGNC; HGNC:2926; DMBT1.
HPA; HPA040778; -.
MIM; 137800; phenotype.
MIM; 601969; gene.
neXtProt; NX_Q9UGM3; -.
OpenTargets; ENSG00000187908; -.
PharmGKB; PA27376; -.
eggNOG; ENOG410IHBC; Eukaryota.
eggNOG; ENOG410XQVR; LUCA.
GeneTree; ENSGT00900000140803; -.
HOVERGEN; HBG060122; -.
InParanoid; Q9UGM3; -.
KO; K13912; -.
OMA; NTHNCGH; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; Q9UGM3; -.
TreeFam; TF329295; -.
Reactome; R-HSA-5683826; Surfactant metabolism.
ChiTaRS; DMBT1; human.
GeneWiki; DMBT1; -.
GenomeRNAi; 1755; -.
PRO; PR:Q9UGM3; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000187908; -.
Genevisible; Q9UGM3; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; IDA:UniProtKB.
GO; GO:0042589; C:zymogen granule membrane; ISS:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; TAS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:1904399; F:heparan sulfate binding; IDA:UniProtKB.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
GO; GO:0070891; F:lipoteichoic acid binding; IDA:UniProtKB.
GO; GO:0038187; F:pattern recognition receptor activity; IDA:UniProtKB.
GO; GO:0005044; F:scavenger receptor activity; IDA:UniProtKB.
GO; GO:0008329; F:signaling pattern recognition receptor activity; TAS:UniProtKB.
GO; GO:0035375; F:zymogen binding; ISS:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0030855; P:epithelial cell differentiation; TAS:UniProtKB.
GO; GO:0043152; P:induction of bacterial agglutination; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00041; CUB; 2.
Gene3D; 2.60.120.290; -; 2.
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; 14.
Pfam; PF00100; Zona_pellucida; 1.
PRINTS; PR00258; SPERACTRCPTR.
SMART; SM00042; CUB; 2.
SMART; SM00202; SR; 14.
SMART; SM00241; ZP; 1.
SUPFAM; SSF49854; SSF49854; 2.
SUPFAM; SSF56487; SSF56487; 14.
PROSITE; PS01180; CUB; 2.
PROSITE; PS00420; SRCR_1; 13.
PROSITE; PS50287; SRCR_2; 14.
PROSITE; PS00682; ZP_1; 1.
PROSITE; PS51034; ZP_2; 1.
1: Evidence at protein level;
Alternative splicing; Antiviral defense; Complete proteome;
Developmental protein; Differentiation; Direct protein sequencing;
Disulfide bond; Glycoprotein; Host-virus interaction; Polymorphism;
Protein transport; Reference proteome; Repeat; Secreted; Signal;
Transport; Tumor suppressor.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 2413 Deleted in malignant brain tumors 1
protein.
/FTId=PRO_0000045387.
DOMAIN 102 202 SRCR 1. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 234 334 SRCR 2. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 363 463 SRCR 3. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 494 594 SRCR 4. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 602 702 SRCR 5. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 733 833 SRCR 6. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 862 962 SRCR 7. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 993 1093 SRCR 8. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 1122 1222 SRCR 9. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 1251 1351 SRCR 10. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 1380 1480 SRCR 11. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 1509 1609 SRCR 12. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 1640 1740 SRCR 13. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 1766 1877 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1883 1986 SRCR 14. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 2008 2117 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 2126 2381 ZP. {ECO:0000255|PROSITE-
ProRule:PRU00375}.
COMPBIAS 1755 1759 Poly-Thr.
CARBOHYD 566 566 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 737 737 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1712 1712 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16740002}.
CARBOHYD 1745 1745 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1818 1818 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1832 1832 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1842 1842 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1889 1889 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16740002}.
CARBOHYD 1998 1998 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2120 2120 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2188 2188 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16740002}.
CARBOHYD 2233 2233 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2240 2240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2256 2256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 127 191 {ECO:0000250}.
DISULFID 140 201 {ECO:0000250}.
DISULFID 171 181 {ECO:0000250}.
DISULFID 259 323 {ECO:0000250}.
DISULFID 272 333 {ECO:0000250}.
DISULFID 303 313 {ECO:0000250}.
DISULFID 388 452 {ECO:0000250}.
DISULFID 401 462 {ECO:0000250}.
DISULFID 432 442 {ECO:0000250}.
DISULFID 519 583 {ECO:0000250}.
DISULFID 532 593 {ECO:0000250}.
DISULFID 563 573 {ECO:0000250}.
DISULFID 627 691 {ECO:0000250}.
DISULFID 640 701 {ECO:0000250}.
DISULFID 671 681 {ECO:0000250}.
DISULFID 758 822 {ECO:0000250}.
DISULFID 771 832 {ECO:0000250}.
DISULFID 802 812 {ECO:0000250}.
DISULFID 887 951 {ECO:0000250}.
DISULFID 900 961 {ECO:0000250}.
DISULFID 931 941 {ECO:0000250}.
DISULFID 1018 1082 {ECO:0000250}.
DISULFID 1031 1092 {ECO:0000250}.
DISULFID 1062 1072 {ECO:0000250}.
DISULFID 1147 1211 {ECO:0000250}.
DISULFID 1160 1221 {ECO:0000250}.
DISULFID 1191 1201 {ECO:0000250}.
DISULFID 1276 1340 {ECO:0000250}.
DISULFID 1289 1350 {ECO:0000250}.
DISULFID 1320 1330 {ECO:0000250}.
DISULFID 1405 1469 {ECO:0000250}.
DISULFID 1418 1479 {ECO:0000250}.
DISULFID 1449 1459 {ECO:0000250}.
DISULFID 1534 1598 {ECO:0000250}.
DISULFID 1547 1608 {ECO:0000250}.
DISULFID 1578 1588 {ECO:0000250}.
DISULFID 1665 1729 {ECO:0000250}.
DISULFID 1678 1739 {ECO:0000250}.
DISULFID 1709 1719 {ECO:0000250}.
DISULFID 1766 1792 {ECO:0000250}.
DISULFID 1819 1841 {ECO:0000250}.
DISULFID 1911 1975 {ECO:0000250}.
DISULFID 1924 1985 {ECO:0000250}.
DISULFID 1955 1965 {ECO:0000250}.
DISULFID 2008 2034 {ECO:0000250}.
DISULFID 2059 2081 {ECO:0000250}.
DISULFID 2302 2360 {ECO:0000250}.
VAR_SEQ 201 332 Missing (in isoform 9).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053979.
VAR_SEQ 337 835 Missing (in isoform 2).
{ECO:0000303|PubMed:9288095}.
/FTId=VSP_016846.
VAR_SEQ 344 1360 Missing (in isoform 9).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053980.
VAR_SEQ 464 473 Missing (in isoform 3 and isoform 7).
{ECO:0000303|PubMed:10597221}.
/FTId=VSP_016847.
VAR_SEQ 472 478 SPDTLPT -> RPGERPR (in isoform 8).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034653.
VAR_SEQ 479 971 Missing (in isoform 8).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034654.
VAR_SEQ 523 1408 Missing (in isoform 4).
{ECO:0000303|Ref.9}.
/FTId=VSP_016848.
VAR_SEQ 1099 1356 Missing (in isoform 8).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034655.
VAR_SEQ 1169 1169 M -> MSAPGNARFGQGSGPIVLDDVRCSGHESYLWSCPHN
GWLSHNCGHHEDAGVICSASQSQPTPSPDTWPTSHASTAGS
ESSLALRLVNGGDRCQGRVEVLYRGSWGTVCDDYWDTNDAN
VVCRQLGCGWAT (in isoform 6 and isoform
7). {ECO:0000305}.
/FTId=VSP_034656.
VAR_SEQ 1170 1298 Missing (in isoform 2).
{ECO:0000303|PubMed:9288095}.
/FTId=VSP_016849.
VAR_SEQ 1608 1738 Missing (in isoform 9).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053981.
VAR_SEQ 1741 1761 ATQINSTTTDWWHPTTTTTAR -> G (in isoform
5). {ECO:0000303|PubMed:17974005}.
/FTId=VSP_016850.
VARIANT 42 42 P -> T (in dbSNP:rs11523871).
{ECO:0000269|PubMed:10485905,
ECO:0000269|PubMed:10551316,
ECO:0000269|PubMed:10597221,
ECO:0000269|PubMed:12185598,
ECO:0000269|PubMed:12353266,
ECO:0000269|PubMed:9288095}.
/FTId=VAR_024788.
VARIANT 52 52 S -> W (in dbSNP:rs75209396).
{ECO:0000269|PubMed:12185598,
ECO:0000269|PubMed:12353266}.
/FTId=VAR_024789.
VARIANT 54 54 S -> L (in dbSNP:rs3013236).
{ECO:0000269|PubMed:10485905,
ECO:0000269|PubMed:10551316,
ECO:0000269|PubMed:10597221,
ECO:0000269|PubMed:12185598,
ECO:0000269|PubMed:12353266,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_024790.
VARIANT 60 60 V -> A (in dbSNP:rs3204770).
{ECO:0000269|PubMed:10485905,
ECO:0000269|PubMed:10597221,
ECO:0000269|PubMed:12185598,
ECO:0000269|PubMed:9288095}.
/FTId=VAR_024791.
VARIANT 65 65 P -> L (in dbSNP:rs185045706).
{ECO:0000269|PubMed:12185598}.
/FTId=VAR_024792.
VARIANT 162 162 G -> E (in a glioma cell line;
dbSNP:rs200664624).
{ECO:0000269|PubMed:12353266}.
/FTId=VAR_057981.
VARIANT 322 322 N -> D (in dbSNP:rs1969620).
{ECO:0000269|PubMed:12353266}.
/FTId=VAR_044417.
VARIANT 337 337 Q -> L. {ECO:0000269|PubMed:10597221,
ECO:0000269|PubMed:12185598}.
/FTId=VAR_024793.
VARIANT 357 357 P -> S (in dbSNP:rs141757453).
{ECO:0000269|PubMed:12185598,
ECO:0000269|PubMed:12353266}.
/FTId=VAR_024794.
VARIANT 364 364 R -> G. {ECO:0000269|PubMed:12185598}.
/FTId=VAR_024795.
VARIANT 420 420 Q -> H (in a glioma sample; glioblastoma
multiforme; somatic mutation;
dbSNP:rs104894156).
/FTId=VAR_024796.
VARIANT 546 546 N -> S (in a glioma cell line;
dbSNP:rs200713568).
{ECO:0000269|PubMed:12353266}.
/FTId=VAR_057982.
VARIANT 607 607 G -> V (in a glioma sample; pilocytic
astrocytoma).
/FTId=VAR_024797.
VARIANT 649 649 T -> M (in dbSNP:rs189478437).
{ECO:0000269|PubMed:10485905,
ECO:0000269|PubMed:12185598}.
/FTId=VAR_024798.
VARIANT 656 656 R -> W.
/FTId=VAR_024799.
VARIANT 670 670 R -> C (in dbSNP:rs2277237).
/FTId=VAR_052994.
VARIANT 719 719 T -> M (in dbSNP:rs2277238).
/FTId=VAR_052995.
VARIANT 780 780 T -> M (in dbSNP:rs199704744).
{ECO:0000269|PubMed:10485905,
ECO:0000269|PubMed:12185598}.
/FTId=VAR_024800.
VARIANT 856 856 P -> S (in dbSNP:rs144450471).
{ECO:0000269|PubMed:10485905,
ECO:0000269|PubMed:10551316,
ECO:0000269|PubMed:10597221,
ECO:0000269|PubMed:11751412}.
/FTId=VAR_024801.
VARIANT 1084 1084 H -> Y (in dbSNP:rs2277244).
{ECO:0000269|PubMed:12185598}.
/FTId=VAR_024802.
VARIANT 1095 1095 S -> P (in dbSNP:rs200551848).
{ECO:0000269|PubMed:12353266}.
/FTId=VAR_057983.
VARIANT 1102 1102 S -> T (in dbSNP:rs566926424).
{ECO:0000269|PubMed:12353266}.
/FTId=VAR_057984.
VARIANT 1169 1169 M -> T (in dbSNP:rs149099696).
{ECO:0000269|PubMed:12185598}.
/FTId=VAR_024803.
VARIANT 1176 1176 R -> W (in dbSNP:rs761527369).
{ECO:0000269|PubMed:12185598}.
/FTId=VAR_024804.
VARIANT 1434 1434 R -> W. {ECO:0000269|PubMed:12353266}.
/FTId=VAR_057985.
VARIANT 1545 1545 V -> M (in dbSNP:rs189221852).
{ECO:0000269|PubMed:12185598}.
/FTId=VAR_024805.
VARIANT 1732 1732 H -> S (requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:12185598,
ECO:0000269|PubMed:12353266}.
/FTId=VAR_024806.
VARIANT 1860 1860 R -> L (in dbSNP:rs7099177).
/FTId=VAR_044418.
VARIANT 1961 1961 T -> P. {ECO:0000269|PubMed:12185598}.
/FTId=VAR_024807.
VARIANT 2255 2255 V -> M (in dbSNP:rs183135544).
{ECO:0000269|PubMed:12353266}.
/FTId=VAR_057986.
CONFLICT 10 10 M -> V (in Ref. 5; CAC44122).
{ECO:0000305}.
CONFLICT 13 13 L -> S (in Ref. 6; BAH14118).
{ECO:0000305}.
CONFLICT 31 31 A -> T (in Ref. 8; AAI53300).
{ECO:0000305}.
CONFLICT 42 42 P -> Q (in Ref. 2; AAD49696 and 8;
AAI53300). {ECO:0000305}.
CONFLICT 74 74 S -> T (in Ref. 2; CAB56155).
{ECO:0000305}.
CONFLICT 125 125 T -> A (in Ref. 2; CAB56155).
{ECO:0000305}.
CONFLICT 188 188 S -> T (in Ref. 6; BAH14118).
{ECO:0000305}.
CONFLICT 194 194 G -> S (in Ref. 6; BAH14118).
{ECO:0000305}.
CONFLICT 468 468 W -> R (in Ref. 5; CAC44122).
{ECO:0000305}.
CONFLICT 594 594 S -> SDTLPTTTLPASTV (in Ref. 3;
CAB63941). {ECO:0000305}.
CONFLICT 603 603 R -> G (in Ref. 3; CAB63942).
{ECO:0000305}.
CONFLICT 711 711 R -> G (in Ref. 5; CAC44122).
{ECO:0000305}.
CONFLICT 902 902 Q -> R (in Ref. 3; CAB63942).
{ECO:0000305}.
CONFLICT 1034 1034 L -> P (in Ref. 1; CAA04019 and 2;
AAD49696). {ECO:0000305}.
CONFLICT 1060 1060 V -> A (in Ref. 2; CAB56155).
{ECO:0000305}.
CONFLICT 1069 1069 L -> P (in Ref. 1; CAA04019 and 2;
AAD49696). {ECO:0000305}.
CONFLICT 1159 1159 V -> A (in Ref. 2; CAB56155).
{ECO:0000305}.
CONFLICT 1204 1204 N -> D (in Ref. 3; CAB63942).
{ECO:0000305}.
CONFLICT 1271 1271 S -> P (in Ref. 3; CAB63942).
{ECO:0000305}.
CONFLICT 1295 1295 G -> S (in Ref. 5; CAC44122).
{ECO:0000305}.
CONFLICT 1336 1336 L -> F (in Ref. 5; CAC44122).
{ECO:0000305}.
CONFLICT 1411 1411 T -> I (in Ref. 8; AAI53300).
{ECO:0000305}.
CONFLICT 1432 1432 N -> S (in Ref. 3; CAB63942).
{ECO:0000305}.
CONFLICT 1443 1443 V -> A (in Ref. 3; CAB63942).
{ECO:0000305}.
CONFLICT 1448 1448 R -> H (in Ref. 8; AAI53300).
{ECO:0000305}.
CONFLICT 1482 1482 S -> F (in Ref. 2; CAB56155).
{ECO:0000305}.
CONFLICT 1583 1583 S -> P (in Ref. 2; CAB56155).
{ECO:0000305}.
CONFLICT 1591 1591 N -> K (in Ref. 6; BAH14118).
{ECO:0000305}.
CONFLICT 1595 1595 S -> T (in Ref. 6; BAH14118).
{ECO:0000305}.
CONFLICT 1705 1705 D -> G (in Ref. 2; CAB56155).
{ECO:0000305}.
CONFLICT 1845 1845 R -> G (in Ref. 10). {ECO:0000305}.
CONFLICT 1909 1909 T -> A (in Ref. 2; CAB56155).
{ECO:0000305}.
CONFLICT 2004 2005 TD -> N (in Ref. 2; CAB56155 and 7;
CAI14494). {ECO:0000305}.
CONFLICT 2196 2196 F -> L (in Ref. 2; CAB56155).
{ECO:0000305}.
CONFLICT 2380 2380 L -> S (in Ref. 8; AAI53300).
{ECO:0000305}.
CONFLICT 2405 2405 P -> A (in Ref. 5; CAC44122).
{ECO:0000305}.
SEQUENCE 2413 AA; 260735 MW; 25363E6263234F15 CRC64;
MGISTVILEM CLLWGQVLST GGWIPRTTDY ASLIPSEVPL DPTVAEGSPF PSESTLESTV
AEGSPISLES TLESTVAEGS LIPSESTLES TVAEGSDSGL ALRLVNGDGR CQGRVEILYR
GSWGTVCDDS WDTNDANVVC RQLGCGWAMS APGNAWFGQG SGPIALDDVR CSGHESYLWS
CPHNGWLSHN CGHGEDAGVI CSAAQPQSTL RPESWPVRIS PPVPTEGSES SLALRLVNGG
DRCRGRVEVL YRGSWGTVCD DYWDTNDANV VCRQLGCGWA MSAPGNAQFG QGSGPIVLDD
VRCSGHESYL WSCPHNGWLT HNCGHSEDAG VICSAPQSRP TPSPDTWPTS HASTAGPESS
LALRLVNGGD RCQGRVEVLY RGSWGTVCDD SWDTSDANVV CRQLGCGWAT SAPGNARFGQ
GSGPIVLDDV RCSGYESYLW SCPHNGWLSH NCQHSEDAGV ICSAAHSWST PSPDTLPTIT
LPASTVGSES SLALRLVNGG DRCQGRVEVL YRGSWGTVCD DSWDTNDANV VCRQLGCGWA
MLAPGNARFG QGSGPIVLDD VRCSGNESYL WSCPHNGWLS HNCGHSEDAG VICSGPESSL
ALRLVNGGDR CQGRVEVLYR GSWGTVCDDS WDTNDANVVC RQLGCGWATS APGNARFGQG
SGPIVLDDVR CSGHESYLWS CPNNGWLSHN CGHHEDAGVI CSAAQSRSTP RPDTLSTITL
PPSTVGSESS LTLRLVNGSD RCQGRVEVLY RGSWGTVCDD SWDTNDANVV CRQLGCGWAT
SAPGNARFGQ GSGPIVLDDV RCSGHESYLW SCPHNGWLSH NCGHHEDAGV ICSVSQSRPT
PSPDTWPTSH ASTAGPESSL ALRLVNGGDR CQGRVEVLYR GSWGTVCDDS WDTSDANVVC
RQLGCGWATS APGNARFGQG SGPIVLDDVR CSGYESYLWS CPHNGWLSHN CQHSEDAGVI
CSAAHSWSTP SPDTLPTITL PASTVGSESS LALRLVNGGD RCQGRVEVLY QGSWGTVCDD
SWDTNDANVV CRQLGCGWAM SAPGNARFGQ GSGPIVLDDV RCSGHESYLW SCPHNGWLSH
NCGHSEDAGV ICSASQSRPT PSPDTWPTSH ASTAGSESSL ALRLVNGGDR CQGRVEVLYR
GSWGTVCDDY WDTNDANVVC RQLGCGWAMS APGNARFGQG SGPIVLDDVR CSGHESYLWS
CPHNGWLSHN CGHHEDAGVI CSASQSQPTP SPDTWPTSHA STAGSESSLA LRLVNGGDRC
QGRVEVLYRG SWGTVCDDYW DTNDANVVCR QLGCGWATSA PGNARFGQGS GPIVLDDVRC
SGHESYLWSC PHNGWLSHNC GHHEDAGVIC SASQSQPTPS PDTWPTSHAS TAGSESSLAL
RLVNGGDRCQ GRVEVLYRGS WGTVCDDYWD TNDANVVCRQ LGCGWATSAP GNARFGQGSG
PIVLDDVRCS GHESYLWSCP HNGWLSHNCG HHEDAGVICS ASQSQPTPSP DTWPTSRAST
AGSESTLALR LVNGGDRCRG RVEVLYQGSW GTVCDDYWDT NDANVVCRQL GCGWAMSAPG
NAQFGQGSGP IVLDDVRCSG HESYLWSCPH NGWLSHNCGH HEDAGVICSA AQSQSTPRPD
TWLTTNLPAL TVGSESSLAL RLVNGGDRCR GRVEVLYRGS WGTVCDDSWD TNDANVVCRQ
LGCGWAMSAP GNARFGQGSG PIVLDDVRCS GNESYLWSCP HKGWLTHNCG HHEDAGVICS
ATQINSTTTD WWHPTTTTTA RPSSNCGGFL FYASGTFSSP SYPAYYPNNA KCVWEIEVNS
GYRINLGFSN LKLEAHHNCS FDYVEIFDGS LNSSLLLGKI CNDTRQIFTS SYNRMTIHFR
SDISFQNTGF LAWYNSFPSD ATLRLVNLNS SYGLCAGRVE IYHGGTWGTV CDDSWTIQEA
EVVCRQLGCG RAVSALGNAY FGSGSGPITL DDVECSGTES TLWQCRNRGW FSHNCNHRED
AGVICSGNHL STPAPFLNIT RPNTDYSCGG FLSQPSGDFS SPFYPGNYPN NAKCVWDIEV
QNNYRVTVIF RDVQLEGGCN YDYIEVFDGP YRSSPLIARV CDGARGSFTS SSNFMSIRFI
SDHSITRRGF RAEYYSSPSN DSTNLLCLPN HMQASVSRSY LQSLGFSASD LVISTWNGYY
ECRPQITPNL VIFTIPYSGC GTFKQADNDT IDYSNFLTAA VSGGIIKRRT DLRIHVSCRM
LQNTWVDTMY IANDTIHVAN NTIQVEEVQY GNFDVNISFY TSSSFLYPVT SRPYYVDLNQ
DLYVQAEILH SDAVLTLFVD TCVASPYSND FTSLTYDLIR SGCVRDDTYG PYSSPSLRIA
RFRFRAFHFL NRFPSVYLRC KMVVCRAYDP SSRCYRGCVL RSKRDVGSYQ EKVDVVLGPI
QLQTPPRREE EPR


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