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P12021

- MUCAP_PIG

UniProt

P12021 - MUCAP_PIG

Protein

Apomucin

Gene
N/A
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 2 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    Apomucin is part of mucin, the major glycoprotein synthesized and secreted by mucous cells of the submaxillary gland. Its highly viscous aqueous solutions serve to lubricate the oral cavity and to protect it from the external environment.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Apomucin
    Alternative name(s):
    Mucin core protein
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 1150›1150ApomucinPRO_0000158958Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi? ↔ 1145PROSITE-ProRule annotation
    Glycosylationi46 – 461O-linked (GalNAc...); partial1 Publication
    Glycosylationi50 – 501O-linked (GalNAc...); partial1 Publication
    Glycosylationi51 – 511O-linked (GalNAc...); partial1 Publication
    Glycosylationi57 – 571O-linked (GalNAc...); partial1 Publication
    Glycosylationi58 – 581O-linked (GalNAc...); partial1 Publication
    Glycosylationi61 – 611O-linked (GalNAc...); partial1 Publication
    Glycosylationi66 – 661O-linked (GalNAc...); partial1 Publication
    Glycosylationi67 – 671O-linked (GalNAc...); partial1 Publication
    Glycosylationi73 – 731O-linked (GalNAc...); partial1 Publication
    Glycosylationi74 – 741O-linked (GalNAc...); partial1 Publication
    Glycosylationi76 – 761O-linked (GalNAc...); partial1 Publication
    Glycosylationi77 – 771O-linked (GalNAc...); partial1 Publication
    Glycosylationi81 – 811O-linked (GalNAc...); partial1 Publication
    Glycosylationi83 – 831O-linked (GalNAc...); partial1 Publication
    Glycosylationi87 – 871O-linked (GalNAc...); partial1 Publication
    Glycosylationi91 – 911O-linked (GalNAc...); partial1 Publication
    Glycosylationi93 – 931O-linked (GalNAc...); partial1 Publication
    Glycosylationi94 – 941O-linked (GalNAc...); partial1 Publication
    Glycosylationi96 – 961O-linked (GalNAc...); partial1 Publication
    Glycosylationi98 – 981O-linked (GalNAc...); partial1 Publication
    Glycosylationi101 – 1011O-linked (GalNAc...); partial1 Publication
    Glycosylationi103 – 1031O-linked (GalNAc...); partial1 Publication
    Glycosylationi104 – 1041O-linked (GalNAc...); partial1 Publication
    Glycosylationi106 – 1061O-linked (GalNAc...); partial1 Publication
    Glycosylationi107 – 1071O-linked (GalNAc...); partial1 Publication
    Glycosylationi108 – 1081O-linked (GalNAc...); partial1 Publication
    Glycosylationi110 – 1101O-linked (GalNAc...); partial1 Publication
    Glycosylationi114 – 1141O-linked (GalNAc...); partial1 Publication
    Glycosylationi117 – 1171O-linked (GalNAc...); partial1 Publication
    Glycosylationi123 – 1231O-linked (GalNAc...); partial1 Publication
    Glycosylationi124 – 1241O-linked (GalNAc...); partial1 Publication
    Glycosylationi418 – 4181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi547 – 5471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi917 – 9171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi985 – 9851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1002 – 10021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1062 ↔ 1109PROSITE-ProRule annotation
    Glycosylationi1068 – 10681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1076 ↔ 1123PROSITE-ProRule annotation
    Disulfide bondi1085 ↔ 1139PROSITE-ProRule annotation
    Disulfide bondi1089 ↔ 1141PROSITE-ProRule annotation

    Post-translational modificationi

    Extensively O-glycosylated on most but not all Ser and Thr residues of the repeat units. Highest glycosylation appears to occur on Ser residues which have Gly at positions at +2 or -2 from the glycosylation site or, where Gly is the penultimate residue. The presence of proline (usually at position +3 or -3) appears to also enhance glycosylation.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Submaxillary mucosae.

    Interactioni

    Subunit structurei

    Intermolecular disulfide bonds could help maintain a multimeric mucin structure.

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000000836.

    Structurei

    3D structure databases

    ProteinModelPortaliP12021.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati‹1 – 44›441Add
    BLAST
    Repeati45 – 125812Add
    BLAST
    Repeati126 – 206813Add
    BLAST
    Repeati207 – 287814Add
    BLAST
    Repeati288 – 368815Add
    BLAST
    Repeati369 – 391236; truncatedAdd
    BLAST
    Domaini929 – 99567VWFCPROSITE-ProRule annotationAdd
    BLAST
    Domaini1062 – 114685CTCKPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni‹1 – 368›3686 X 81 AA tandem repeatsAdd
    BLAST

    Domaini

    Contains tandemly repeated, identical sequences of 81 residues.

    Sequence similaritiesi

    Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation
    Contains 1 VWFC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG006422.

    Family and domain databases

    InterProiIPR006207. Cys_knot_C.
    IPR006208. Glyco_hormone_CN.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF00007. Cys_knot. 1 hit.
    [Graphical view]
    SMARTiSM00041. CT. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view]
    PROSITEiPS01185. CTCK_1. 1 hit.
    PS01225. CTCK_2. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    P12021-1 [UniParc]FASTAAdd to Basket

    « Hide

    ETARPSVAGS GTTGTVSGAS GSTGSSSGST GATGASIGQP ETSRISVAGS     50
    SGAPAVSSGA SQAAGTSGAG PGTTASSVGV TETARPSVAG SGTTGTVSGA 100
    SGSTGSSSGS PGATGASIGQ PETSRISVAG SSGAPAVSSG ASQAAGTSGA 150
    GPGTTASSVG VTETARPSVA GSGTTGTVSG ASGSTGSSSG SPGATGASIG 200
    QPETSRISVA GSSGAPAVSS GASQAAGTSG AGPGTTASSV GVTETARPSV 250
    AGSGTTGTVS GASGSTGSSS GSPGATGASI GQPETSRISV AGSSGAPAVS 300
    SGASQAAGTS GAGPGTTASS VGVTETARPS VAGSGTTGTV SGASGSTGSS 350
    SGSPGATGAS IGQPETSRIS VAGSSGAPAV SSGASQAAGT SEATTSIEGA 400
    GTSGVGFKTE ATTFPGENET TRVGIATGTT GIVSRKTLEP GSYNTEATTS 450
    IGRSGTTHTD LPGGTTIVLP GFSHSSQSSK PGSSVTTPGS PESGSETGTS 500
    GEFSTTVISG SSHTEATTFI GGSGSPGTGS RPGTTGELSG TTIASGNATT 550
    EATTSTETRI GPQTGAQTTV PGSQVSGSET GTSEAVSNPA IASGSSSTGT 600
    TSGASDSQVT GSRTGTTGVV LGTTVAPGSS STGATTGVLI NEGTRSTSLG 650
    TTRVASGTTY ESGTSNSVPS GGSGTPGSGI NTGGSSTQVT GIQTGTTAVG 700
    FGSTLLPGSS NTGATTSPSE RTSPGSKTGI TRVVSGTTVA SGSSNTGATT 750
    SLGRGETTQG GIKIVITGVT VGTTVAPGSF NTKATTPTEV RAATGAGTAV 800
    GATSRSTGIS TGPENSTPGT TETGSGTTSS PGGVKTEATT FKGVGTTEAG 850
    ISSGNSPGSG GVTSSQEGTS REASETTTAP RISATGSTSV SKEITASPKV 900
    SSPETTAGAT EDQENENKTG CPAPLPPPPV CHGPLGEEKS PGDVWTANCH 950
    KCTCTEAKTV DCKPKECPSP PTCKTGERLI KFKANDTCCE IGHCEKRTCL 1000
    FNNTDYEVGS SFDDPNNPCV TYSCQNTGFT AVVQNCPKQT WCAEEDRVYD 1050
    SKQCCYTCKS SCKPSPVNVT VRYNGCTIKV EMARCVGECK KTVTYDYDIF 1100
    QLKNSCLCCQ EEDYEFRDIV LDCPDGSTLP YRYRHITACS CLDPCQQSMT 1150
    Length:1,150
    Mass (Da):109,616
    Last modified:December 1, 1992 - v2
    Checksum:i3CB68B5D29DD7F5A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61883 mRNA. Translation: AAA30998.1.
    M21174 mRNA. Translation: AAA30990.1.
    UniGeneiSsc.14474.
    Ssc.68696.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61883 mRNA. Translation: AAA30998.1 .
    M21174 mRNA. Translation: AAA30990.1 .
    UniGenei Ssc.14474.
    Ssc.68696.

    3D structure databases

    ProteinModelPortali P12021.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000000836.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG006422.

    Family and domain databases

    InterProi IPR006207. Cys_knot_C.
    IPR006208. Glyco_hormone_CN.
    IPR001007. VWF_C.
    [Graphical view ]
    Pfami PF00007. Cys_knot. 1 hit.
    [Graphical view ]
    SMARTi SM00041. CT. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view ]
    PROSITEi PS01185. CTCK_1. 1 hit.
    PS01225. CTCK_2. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Porcine submaxillary mucin contains a cystine-rich, carboxyl-terminal domain in addition to a highly repetitive, glycosylated domain."
      Eckhardt A.E., Timpte C.S., Abernethy J.L., Zhao Y., Hill R.L.
      J. Biol. Chem. 266:9678-9686(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Submandibular gland.
    2. "Porcine submaxillary gland apomucin contains tandemly repeated, identical sequences of 81 residues."
      Timpte C.S., Eckhardt A.E., Abernethy J.L., Hill R.L.
      J. Biol. Chem. 263:1081-1088(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-503.
      Tissue: Submandibular gland.
    3. "Structural properties of porcine submaxillary gland apomucin."
      Eckhardt A.E., Timpte C.S., Abernethy J.L., Toumadje A., Johnson W.C. Jr., Hill R.L.
      J. Biol. Chem. 262:11339-11344(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 45-80.
      Tissue: Submandibular gland.
    4. "Determination of the site-specific O-glycosylation pattern of the porcine submaxillary mucin tandem repeat glycopeptide. Model proposed for the polypeptide:GalNAc transferase peptide binding site."
      Gerken T.A., Owens C.L., Pasumarthy M.
      J. Biol. Chem. 272:9709-9719(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 45-125, GLYCOSYLATION AT SER-46; SER-50; SER-51; SER-57; SER-58; SER-61; THR-66; SER-67; THR-73; THR-74; SER-76; SER-77; THR-81; THR-83; SER-87; SER-91; THR-93; THR-94; THR-96; SER-98; SER-101; SER-103; THR-104; SER-106; SER-107; SER-108; SER-110; THR-114; SER-117; THR-123 AND SER-124.
      Tissue: Submandibular gland.

    Entry informationi

    Entry nameiMUCAP_PIG
    AccessioniPrimary (citable) accession number: P12021
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 83 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3