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P12021

- MUCAP_PIG

UniProt

P12021 - MUCAP_PIG

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Protein

Apomucin

Gene
N/A
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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? ↔ 1145 By similarity
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...) Reviewed prediction
Glycosylationi547 – 5471N-linked (GlcNAc...) Reviewed prediction
Glycosylationi917 – 9171N-linked (GlcNAc...) Reviewed prediction
Glycosylationi985 – 9851N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1002 – 10021N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1062 ↔ 1109 By similarity
Glycosylationi1068 – 10681N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1076 ↔ 1123 By similarity
Disulfide bondi1085 ↔ 1139 By similarity
Disulfide bondi1089 ↔ 1141 By similarity

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.

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 – 99567VWFCAdd
BLAST
Domaini1062 – 114685CTCKAdd
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 VWFC domain.

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

Non-terminal residue

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: April 16, 2014
This is version 82 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

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