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MUCAP_PIG
ID   MUCAP_PIG               Reviewed;        1150 AA.
AC   P12021;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Apomucin;
DE   AltName: Full=Mucin core protein;
DE   Flags: Fragment;
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 [MRNA].
RC   TISSUE=Submandibular gland;
RX   PubMed=2033060; DOI=10.1016/s0021-9258(18)92874-7;
RA   Eckhardt A.E., Timpte C.S., Abernethy J.L., Zhao Y., Hill R.L.;
RT   "Porcine submaxillary mucin contains a cystine-rich, carboxyl-terminal
RT   domain in addition to a highly repetitive, glycosylated domain.";
RL   J. Biol. Chem. 266:9678-9686(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-503.
RC   TISSUE=Submandibular gland;
RX   PubMed=2826455; DOI=10.1016/s0021-9258(19)35463-8;
RA   Timpte C.S., Eckhardt A.E., Abernethy J.L., Hill R.L.;
RT   "Porcine submaxillary gland apomucin contains tandemly repeated, identical
RT   sequences of 81 residues.";
RL   J. Biol. Chem. 263:1081-1088(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 45-80.
RC   TISSUE=Submandibular gland;
RX   PubMed=3611111; DOI=10.1016/s0021-9258(18)60964-0;
RA   Eckhardt A.E., Timpte C.S., Abernethy J.L., Toumadje A., Johnson W.C. Jr.,
RA   Hill R.L.;
RT   "Structural properties of porcine submaxillary gland apomucin.";
RL   J. Biol. Chem. 262:11339-11344(1987).
RN   [4]
RP   PROTEIN SEQUENCE OF 45-125, AND GLYCOSYLATION AT SER-46; SER-50; SER-51;
RP   SER-57; SER-58; SER-61; THR-66; SER-67; THR-73; THR-74; SER-76; SER-77;
RP   THR-81; THR-83; SER-87; SER-91; THR-93; THR-94; THR-96; SER-98; SER-101;
RP   SER-103; THR-104; SER-106; SER-107; SER-108; SER-110; THR-114; SER-117;
RP   THR-123 AND SER-124.
RC   TISSUE=Submandibular gland;
RX   PubMed=9092502; DOI=10.1074/jbc.272.15.9709;
RA   Gerken T.A., Owens C.L., Pasumarthy M.;
RT   "Determination of the site-specific O-glycosylation pattern of the porcine
RT   submaxillary mucin tandem repeat glycopeptide. Model proposed for the
RT   polypeptide:GalNAc transferase peptide binding site.";
RL   J. Biol. Chem. 272:9709-9719(1997).
CC   -!- FUNCTION: Apomucin is part of mucin, the major glycoprotein synthesized
CC       and secreted by mucous cells of the submaxillary gland. Its highly
CC       viscous aqueous solutions serve to lubricate the oral cavity and to
CC       protect it from the external environment.
CC   -!- SUBUNIT: Intermolecular disulfide bonds could help maintain a
CC       multimeric mucin structure.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Submaxillary mucosae.
CC   -!- DOMAIN: Contains tandemly repeated, identical sequences of 81 residues.
CC   -!- PTM: Extensively O-glycosylated on most but not all Ser and Thr
CC       residues of the repeat units. Highest glycosylation appears to occur on
CC       Ser residues which have Gly at positions at +2 or -2 from the
CC       glycosylation site or, where Gly is the penultimate residue. The
CC       presence of proline (usually at position +3 or -3) appears to also
CC       enhance glycosylation. {ECO:0000269|PubMed:9092502}.
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DR   EMBL; M61883; AAA30998.1; -; mRNA.
DR   EMBL; M21174; AAA30990.1; -; mRNA.
DR   AlphaFoldDB; P12021; -.
DR   SMR; P12021; -.
DR   iPTMnet; P12021; -.
DR   PaxDb; P12021; -.
DR   PRIDE; P12021; -.
DR   eggNOG; KOG1216; Eukaryota.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR006208; Glyco_hormone_CN.
DR   InterPro; IPR001007; VWF_dom.
DR   Pfam; PF00007; Cys_knot; 1.
DR   SMART; SM00041; CT; 1.
DR   SMART; SM00214; VWC; 2.
DR   PROSITE; PS01185; CTCK_1; 1.
DR   PROSITE; PS01225; CTCK_2; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Reference proteome; Repeat; Secreted.
FT   CHAIN           <1..1150
FT                   /note="Apomucin"
FT                   /id="PRO_0000158958"
FT   REPEAT          <1..44
FT                   /note="1"
FT   REPEAT          45..125
FT                   /note="2"
FT   REPEAT          126..206
FT                   /note="3"
FT   REPEAT          207..287
FT                   /note="4"
FT   REPEAT          288..368
FT                   /note="5"
FT   REPEAT          369..391
FT                   /note="6; truncated"
FT   DOMAIN          929..995
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          1062..1146
FT                   /note="CTCK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   REGION          <1..368
FT                   /note="6 X 81 AA tandem repeats"
FT   REGION          1..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..792
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..917
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        46
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        50
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        51
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        57
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        58
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        61
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        66
FT                   /note="O-linked (GalNAc...) threonine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        67
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        73
FT                   /note="O-linked (GalNAc...) threonine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        74
FT                   /note="O-linked (GalNAc...) threonine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        76
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        77
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        81
FT                   /note="O-linked (GalNAc...) threonine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        83
FT                   /note="O-linked (GalNAc...) threonine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        87
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        91
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        93
FT                   /note="O-linked (GalNAc...) threonine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        94
FT                   /note="O-linked (GalNAc...) threonine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        96
FT                   /note="O-linked (GalNAc...) threonine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        98
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        101
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        103
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        104
FT                   /note="O-linked (GalNAc...) threonine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        106
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        107
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        108
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        110
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        114
FT                   /note="O-linked (GalNAc...) threonine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        117
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        123
FT                   /note="O-linked (GalNAc...) threonine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        124
FT                   /note="O-linked (GalNAc...) serine; partial"
FT                   /evidence="ECO:0000269|PubMed:9092502"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        547
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        917
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        985
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1002
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1068
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1062..1109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        1076..1123
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        1085..1139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        1089..1141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        ?..1145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   NON_TER         1
SQ   SEQUENCE   1150 AA;  109616 MW;  3CB68B5D29DD7F5A CRC64;
     ETARPSVAGS GTTGTVSGAS GSTGSSSGST GATGASIGQP ETSRISVAGS SGAPAVSSGA
     SQAAGTSGAG PGTTASSVGV TETARPSVAG SGTTGTVSGA SGSTGSSSGS PGATGASIGQ
     PETSRISVAG SSGAPAVSSG ASQAAGTSGA GPGTTASSVG VTETARPSVA GSGTTGTVSG
     ASGSTGSSSG SPGATGASIG QPETSRISVA GSSGAPAVSS GASQAAGTSG AGPGTTASSV
     GVTETARPSV AGSGTTGTVS GASGSTGSSS GSPGATGASI GQPETSRISV AGSSGAPAVS
     SGASQAAGTS GAGPGTTASS VGVTETARPS VAGSGTTGTV SGASGSTGSS SGSPGATGAS
     IGQPETSRIS VAGSSGAPAV SSGASQAAGT SEATTSIEGA GTSGVGFKTE ATTFPGENET
     TRVGIATGTT GIVSRKTLEP GSYNTEATTS IGRSGTTHTD LPGGTTIVLP GFSHSSQSSK
     PGSSVTTPGS PESGSETGTS GEFSTTVISG SSHTEATTFI GGSGSPGTGS RPGTTGELSG
     TTIASGNATT EATTSTETRI GPQTGAQTTV PGSQVSGSET GTSEAVSNPA IASGSSSTGT
     TSGASDSQVT GSRTGTTGVV LGTTVAPGSS STGATTGVLI NEGTRSTSLG TTRVASGTTY
     ESGTSNSVPS GGSGTPGSGI NTGGSSTQVT GIQTGTTAVG FGSTLLPGSS NTGATTSPSE
     RTSPGSKTGI TRVVSGTTVA SGSSNTGATT SLGRGETTQG GIKIVITGVT VGTTVAPGSF
     NTKATTPTEV RAATGAGTAV GATSRSTGIS TGPENSTPGT TETGSGTTSS PGGVKTEATT
     FKGVGTTEAG ISSGNSPGSG GVTSSQEGTS REASETTTAP RISATGSTSV SKEITASPKV
     SSPETTAGAT EDQENENKTG CPAPLPPPPV CHGPLGEEKS PGDVWTANCH KCTCTEAKTV
     DCKPKECPSP PTCKTGERLI KFKANDTCCE IGHCEKRTCL FNNTDYEVGS SFDDPNNPCV
     TYSCQNTGFT AVVQNCPKQT WCAEEDRVYD SKQCCYTCKS SCKPSPVNVT VRYNGCTIKV
     EMARCVGECK KTVTYDYDIF QLKNSCLCCQ EEDYEFRDIV LDCPDGSTLP YRYRHITACS
     CLDPCQQSMT
 
 
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