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P12021 (MUCAP_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apomucin
Alternative name(s):
Mucin core protein
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length1150 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Intermolecular disulfide bonds could help maintain a multimeric mucin structure.

Subcellular location

Secreted.

Tissue specificity

Submaxillary mucosae.

Domain

Contains tandemly repeated, identical sequences of 81 residues.

Post-translational modification

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. Ref.4

Sequence similarities

Contains 1 CTCK (C-terminal cystine knot-like) domain.

Contains 1 VWFC domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 1150›1150Apomucin
PRO_0000158958

Regions

Repeat‹1 – 44›441
Repeat45 – 125812
Repeat126 – 206813
Repeat207 – 287814
Repeat288 – 368815
Repeat369 – 391236; truncated
Domain929 – 99567VWFC
Domain1062 – 114685CTCK
Region‹1 – 368›3686 X 81 AA tandem repeats

Amino acid modifications

Glycosylation461O-linked (GalNAc...); partial Ref.4
Glycosylation501O-linked (GalNAc...); partial Ref.4
Glycosylation511O-linked (GalNAc...); partial Ref.4
Glycosylation571O-linked (GalNAc...); partial Ref.4
Glycosylation581O-linked (GalNAc...); partial Ref.4
Glycosylation611O-linked (GalNAc...); partial Ref.4
Glycosylation661O-linked (GalNAc...); partial Ref.4
Glycosylation671O-linked (GalNAc...); partial Ref.4
Glycosylation731O-linked (GalNAc...); partial Ref.4
Glycosylation741O-linked (GalNAc...); partial Ref.4
Glycosylation761O-linked (GalNAc...); partial Ref.4
Glycosylation771O-linked (GalNAc...); partial Ref.4
Glycosylation811O-linked (GalNAc...); partial Ref.4
Glycosylation831O-linked (GalNAc...); partial Ref.4
Glycosylation871O-linked (GalNAc...); partial Ref.4
Glycosylation911O-linked (GalNAc...); partial Ref.4
Glycosylation931O-linked (GalNAc...); partial Ref.4
Glycosylation941O-linked (GalNAc...); partial Ref.4
Glycosylation961O-linked (GalNAc...); partial Ref.4
Glycosylation981O-linked (GalNAc...); partial Ref.4
Glycosylation1011O-linked (GalNAc...); partial Ref.4
Glycosylation1031O-linked (GalNAc...); partial Ref.4
Glycosylation1041O-linked (GalNAc...); partial Ref.4
Glycosylation1061O-linked (GalNAc...); partial Ref.4
Glycosylation1071O-linked (GalNAc...); partial Ref.4
Glycosylation1081O-linked (GalNAc...); partial Ref.4
Glycosylation1101O-linked (GalNAc...); partial Ref.4
Glycosylation1141O-linked (GalNAc...); partial Ref.4
Glycosylation1171O-linked (GalNAc...); partial Ref.4
Glycosylation1231O-linked (GalNAc...); partial Ref.4
Glycosylation1241O-linked (GalNAc...); partial Ref.4
Glycosylation4181N-linked (GlcNAc...) Potential
Glycosylation5471N-linked (GlcNAc...) Potential
Glycosylation9171N-linked (GlcNAc...) Potential
Glycosylation9851N-linked (GlcNAc...) Potential
Glycosylation10021N-linked (GlcNAc...) Potential
Glycosylation10681N-linked (GlcNAc...) Potential
Disulfide bond1062 ↔ 1109 By similarity
Disulfide bond1076 ↔ 1123 By similarity
Disulfide bond1085 ↔ 1139 By similarity
Disulfide bond1089 ↔ 1141 By similarity
Disulfide bond? ↔ 1145 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P12021 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: 3CB68B5D29DD7F5A

FASTA1,150109,616
        10         20         30         40         50         60 
ETARPSVAGS GTTGTVSGAS GSTGSSSGST GATGASIGQP ETSRISVAGS SGAPAVSSGA 

        70         80         90        100        110        120 
SQAAGTSGAG PGTTASSVGV TETARPSVAG SGTTGTVSGA SGSTGSSSGS PGATGASIGQ 

       130        140        150        160        170        180 
PETSRISVAG SSGAPAVSSG ASQAAGTSGA GPGTTASSVG VTETARPSVA GSGTTGTVSG 

       190        200        210        220        230        240 
ASGSTGSSSG SPGATGASIG QPETSRISVA GSSGAPAVSS GASQAAGTSG AGPGTTASSV 

       250        260        270        280        290        300 
GVTETARPSV AGSGTTGTVS GASGSTGSSS GSPGATGASI GQPETSRISV AGSSGAPAVS 

       310        320        330        340        350        360 
SGASQAAGTS GAGPGTTASS VGVTETARPS VAGSGTTGTV SGASGSTGSS SGSPGATGAS 

       370        380        390        400        410        420 
IGQPETSRIS VAGSSGAPAV SSGASQAAGT SEATTSIEGA GTSGVGFKTE ATTFPGENET 

       430        440        450        460        470        480 
TRVGIATGTT GIVSRKTLEP GSYNTEATTS IGRSGTTHTD LPGGTTIVLP GFSHSSQSSK 

       490        500        510        520        530        540 
PGSSVTTPGS PESGSETGTS GEFSTTVISG SSHTEATTFI GGSGSPGTGS RPGTTGELSG 

       550        560        570        580        590        600 
TTIASGNATT EATTSTETRI GPQTGAQTTV PGSQVSGSET GTSEAVSNPA IASGSSSTGT 

       610        620        630        640        650        660 
TSGASDSQVT GSRTGTTGVV LGTTVAPGSS STGATTGVLI NEGTRSTSLG TTRVASGTTY 

       670        680        690        700        710        720 
ESGTSNSVPS GGSGTPGSGI NTGGSSTQVT GIQTGTTAVG FGSTLLPGSS NTGATTSPSE 

       730        740        750        760        770        780 
RTSPGSKTGI TRVVSGTTVA SGSSNTGATT SLGRGETTQG GIKIVITGVT VGTTVAPGSF 

       790        800        810        820        830        840 
NTKATTPTEV RAATGAGTAV GATSRSTGIS TGPENSTPGT TETGSGTTSS PGGVKTEATT 

       850        860        870        880        890        900 
FKGVGTTEAG ISSGNSPGSG GVTSSQEGTS REASETTTAP RISATGSTSV SKEITASPKV 

       910        920        930        940        950        960 
SSPETTAGAT EDQENENKTG CPAPLPPPPV CHGPLGEEKS PGDVWTANCH KCTCTEAKTV 

       970        980        990       1000       1010       1020 
DCKPKECPSP PTCKTGERLI KFKANDTCCE IGHCEKRTCL FNNTDYEVGS SFDDPNNPCV 

      1030       1040       1050       1060       1070       1080 
TYSCQNTGFT AVVQNCPKQT WCAEEDRVYD SKQCCYTCKS SCKPSPVNVT VRYNGCTIKV 

      1090       1100       1110       1120       1130       1140 
EMARCVGECK KTVTYDYDIF QLKNSCLCCQ EEDYEFRDIV LDCPDGSTLP YRYRHITACS 

      1150 
CLDPCQQSMT 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M61883 mRNA. Translation: AAA30998.1.
M21174 mRNA. Translation: AAA30990.1.
UniGeneSsc.14474.
Ssc.68696.

3D structure databases

ProteinModelPortalP12021.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000000836.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG006422.

Family and domain databases

InterProIPR006207. Cys_knot_C.
IPR006208. Glyco_hormone_CN.
IPR001007. VWF_C.
[Graphical view]
PfamPF00007. Cys_knot. 1 hit.
[Graphical view]
SMARTSM00041. CT. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMUCAP_PIG
AccessionPrimary (citable) accession number: P12021
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families