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SMGC_MOUSE
ID   SMGC_MOUSE              Reviewed;         733 AA.
AC   Q6JHY2; A7UN65; Q3V1B0; Q58E46; Q6IS33; Q7TNU8; Q80ZH6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Submandibular gland protein C;
DE   Flags: Precursor;
GN   Name=Muc19; Synonyms=Smgc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP   GLYCOSYLATION.
RC   STRAIN=C57BL/6J; TISSUE=Submandibular gland;
RX   PubMed=15256252; DOI=10.1016/j.gene.2004.03.014;
RA   Zinzen K.M., Hand A.R., Yankova M., Ball W.D., Mirels L.;
RT   "Molecular cloning and characterization of the neonatal rat and mouse
RT   submandibular gland protein SMGC.";
RL   Gene 334:23-33(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), ALTERNATIVE SPLICING (ISOFORMS 1
RP   AND 2), AND TISSUE SPECIFICITY.
RC   STRAIN=NFS; TISSUE=Sublingual gland;
RX   PubMed=15340121; DOI=10.1152/physiolgenomics.00161.2004;
RA   Culp D.J., Latchney L.R., Fallon M.A., Denny P.A., Denny P.C.,
RA   Couwenhoven R.I., Chuang S.;
RT   "The gene encoding mouse Muc19: cDNA, genomic organization and relationship
RT   to Smgc.";
RL   Physiol. Genomics 19:303-318(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 47-733 (ISOFORM 6), AND NUCLEOTIDE SEQUENCE [LARGE
RP   SCALE MRNA] OF 319-733 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC         Comment=Isoform 1 and isoform 2-6 share the first 17 amino acid
CC         residues that correspond to the signal sequence.;
CC       Name=2; Synonyms=Smgc;
CC         IsoId=Q6JHY2-1; Sequence=Displayed;
CC       Name=1; Synonyms=Mucin-19;
CC         IsoId=Q6PZE0-1; Sequence=External;
CC       Name=3;
CC         IsoId=Q6JHY2-2; Sequence=VSP_034526;
CC       Name=4;
CC         IsoId=Q6JHY2-3; Sequence=VSP_034524;
CC       Name=5; Synonyms=t-Smgc;
CC         IsoId=Q6JHY2-4; Sequence=VSP_034523;
CC       Name=6;
CC         IsoId=Q6JHY2-5; Sequence=VSP_034525;
CC   -!- TISSUE SPECIFICITY: Detected in terminal tubule cells of the
CC       submandibular gland (at protein level). Expressed in submandibular
CC       salivary glands of 3-day-old males but not adults. Expression in adult
CC       submandibular glands is restricted to females. Isoform 5 is expressed
CC       in both 3-day-old and adult sublingual glands.
CC       {ECO:0000269|PubMed:15256252, ECO:0000269|PubMed:15340121}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15256252}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH55490.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Mucin database;
CC       URL="http://www.medkem.gu.se/mucinbiology/databases/";
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DR   EMBL; AY459348; AAR23240.1; -; mRNA.
DR   EMBL; EU089958; ABU50845.1; -; mRNA.
DR   EMBL; AK132579; BAE21241.1; -; mRNA.
DR   EMBL; BC049243; AAH49243.1; -; mRNA.
DR   EMBL; BC092073; AAH92073.1; -; mRNA.
DR   EMBL; BC055490; AAH55490.1; ALT_INIT; mRNA.
DR   EMBL; BC069958; AAH69958.1; -; mRNA.
DR   CCDS; CCDS27762.1; -. [Q6JHY2-1]
DR   RefSeq; NP_945121.1; NM_198927.3. [Q6JHY2-1]
DR   AlphaFoldDB; Q6JHY2; -.
DR   STRING; 10090.ENSMUSP00000085915; -.
DR   GlyGen; Q6JHY2; 10 sites.
DR   iPTMnet; Q6JHY2; -.
DR   PhosphoSitePlus; Q6JHY2; -.
DR   MaxQB; Q6JHY2; -.
DR   PaxDb; Q6JHY2; -.
DR   PRIDE; Q6JHY2; -.
DR   ProteomicsDB; 261265; -. [Q6JHY2-1]
DR   ProteomicsDB; 261266; -. [Q6JHY2-2]
DR   ProteomicsDB; 261267; -. [Q6JHY2-3]
DR   ProteomicsDB; 261268; -. [Q6JHY2-4]
DR   ProteomicsDB; 261269; -. [Q6JHY2-5]
DR   DNASU; 223809; -.
DR   Ensembl; ENSMUST00000088555; ENSMUSP00000085915; ENSMUSG00000047295. [Q6JHY2-1]
DR   Ensembl; ENSMUST00000100293; ENSMUSP00000097866; ENSMUSG00000047295. [Q6JHY2-2]
DR   Ensembl; ENSMUST00000109277; ENSMUSP00000104900; ENSMUSG00000047295. [Q6JHY2-4]
DR   GeneID; 223809; -.
DR   KEGG; mmu:223809; -.
DR   UCSC; uc007xic.1; mouse. [Q6JHY2-1]
DR   UCSC; uc007xid.1; mouse. [Q6JHY2-4]
DR   UCSC; uc011zxz.1; mouse. [Q6JHY2-2]
DR   UCSC; uc011zya.1; mouse. [Q6JHY2-3]
DR   UCSC; uc011zyb.1; mouse. [Q6JHY2-5]
DR   CTD; 223809; -.
DR   MGI; MGI:1859618; Smgc.
DR   VEuPathDB; HostDB:ENSMUSG00000047295; -.
DR   GeneTree; ENSGT00680000100886; -.
DR   HOGENOM; CLU_407649_0_0_1; -.
DR   OMA; DPLMEES; -.
DR   PhylomeDB; Q6JHY2; -.
DR   BioGRID-ORCS; 223809; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Muc19; mouse.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q6JHY2; protein.
DR   Bgee; ENSMUSG00000047295; Expressed in submandibular gland and 17 other tissues.
DR   ExpressionAtlas; Q6JHY2; baseline and differential.
DR   Genevisible; Q6JHY2; MM.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..733
FT                   /note="Submandibular gland protein C"
FT                   /id="PRO_5000092417"
FT   REGION          48..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..733
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        514
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        611
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        686
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        696
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         18..622
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15340121"
FT                   /id="VSP_034523"
FT   VAR_SEQ         231..622
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_034524"
FT   VAR_SEQ         320..621
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_034525"
FT   VAR_SEQ         470..502
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_034526"
FT   CONFLICT        274..276
FT                   /note="GHS -> DHP (in Ref. 4; AAH92073)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        629
FT                   /note="R -> S (in Ref. 4; AAH92073/AAH55490/AAH69958/
FT                   AAH49243)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   733 AA;  74383 MW;  243B1628F29ADF6B CRC64;
     MKLILLYLAV VLCFVGKARS FRNGAGFYTS LGGQMRVFDF NKKTLDAKSS GGSKDYNLSD
     GGKSNSRKNL SPATGGSATQ QSNLDDSHAP NLGKSETMLS LLGYLGAFRP VLSGLTSLPR
     VGGGAHGNIG LRAEISRNGV NLSGDSSARG SLNVNPLSGL STKSGNDATV QGQQAAASGG
     SKHNVENSSL STGSATSNKG ADKPSEHLSN LFLKGLKGIV EPITSAAGGS VSSAVENLKA
     QIKKFIEPLT EDHGPTSTSA SVSGDSSTSS RLDGHSSDGL SKVSGDDPTV QGHDVAASDG
     SKQNVEDSTL STGSATSNEG DDKSSDNSSN TFREDLEKIL EQITSAPGGS VSSAVENLKA
     QIKKFIEPLT EDHGPTSTSA SVSGDSSTSS RLDGHSSDGL SKVSGDDPTV QGHDVAASDG
     SKQNVEDSTL STGSATSNEG DDKSSDNSSN TFREDLEKIL EQITSAPGGS VSTVNNPDED
     RLISIIENLA GHIQQSVTEA SQSAERPNAQ SSNNLSGKLE PKYENPTNGS SSASSADKPY
     EEGMRKLLKF LEEQYGQTGT DASVSGMSSE SSRSNVHLSD GFSMESGDDA TVQGQQAAAS
     GGPKQNVESS NSSTGSATSN GGGDSNEVRG PSSSAVDSTD SGDRGNLADK QGPGFNGPEG
     VGENNGGSFR AGSLDTGSKS DSGSHNLSSG SGSRSNVSTG GEPSDKNEPA DPGVSGRVTC
     PTGKTQSGSP SVA
 
 
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