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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-KW
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? ↔ 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

        10         20         30         40         50
ETARPSVAGS GTTGTVSGAS GSTGSSSGST GATGASIGQP ETSRISVAGS
60 70 80 90 100
SGAPAVSSGA SQAAGTSGAG PGTTASSVGV TETARPSVAG SGTTGTVSGA
110 120 130 140 150
SGSTGSSSGS PGATGASIGQ PETSRISVAG SSGAPAVSSG ASQAAGTSGA
160 170 180 190 200
GPGTTASSVG VTETARPSVA GSGTTGTVSG ASGSTGSSSG SPGATGASIG
210 220 230 240 250
QPETSRISVA GSSGAPAVSS GASQAAGTSG AGPGTTASSV GVTETARPSV
260 270 280 290 300
AGSGTTGTVS GASGSTGSSS GSPGATGASI GQPETSRISV AGSSGAPAVS
310 320 330 340 350
SGASQAAGTS GAGPGTTASS VGVTETARPS VAGSGTTGTV SGASGSTGSS
360 370 380 390 400
SGSPGATGAS IGQPETSRIS VAGSSGAPAV SSGASQAAGT SEATTSIEGA
410 420 430 440 450
GTSGVGFKTE ATTFPGENET TRVGIATGTT GIVSRKTLEP GSYNTEATTS
460 470 480 490 500
IGRSGTTHTD LPGGTTIVLP GFSHSSQSSK PGSSVTTPGS PESGSETGTS
510 520 530 540 550
GEFSTTVISG SSHTEATTFI GGSGSPGTGS RPGTTGELSG TTIASGNATT
560 570 580 590 600
EATTSTETRI GPQTGAQTTV PGSQVSGSET GTSEAVSNPA IASGSSSTGT
610 620 630 640 650
TSGASDSQVT GSRTGTTGVV LGTTVAPGSS STGATTGVLI NEGTRSTSLG
660 670 680 690 700
TTRVASGTTY ESGTSNSVPS GGSGTPGSGI NTGGSSTQVT GIQTGTTAVG
710 720 730 740 750
FGSTLLPGSS NTGATTSPSE RTSPGSKTGI TRVVSGTTVA SGSSNTGATT
760 770 780 790 800
SLGRGETTQG GIKIVITGVT VGTTVAPGSF NTKATTPTEV RAATGAGTAV
810 820 830 840 850
GATSRSTGIS TGPENSTPGT TETGSGTTSS PGGVKTEATT FKGVGTTEAG
860 870 880 890 900
ISSGNSPGSG GVTSSQEGTS REASETTTAP RISATGSTSV SKEITASPKV
910 920 930 940 950
SSPETTAGAT EDQENENKTG CPAPLPPPPV CHGPLGEEKS PGDVWTANCH
960 970 980 990 1000
KCTCTEAKTV DCKPKECPSP PTCKTGERLI KFKANDTCCE IGHCEKRTCL
1010 1020 1030 1040 1050
FNNTDYEVGS SFDDPNNPCV TYSCQNTGFT AVVQNCPKQT WCAEEDRVYD
1060 1070 1080 1090 1100
SKQCCYTCKS SCKPSPVNVT VRYNGCTIKV EMARCVGECK KTVTYDYDIF
1110 1120 1130 1140 1150
QLKNSCLCCQ EEDYEFRDIV LDCPDGSTLP YRYRHITACS CLDPCQQSMT
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:
EMBLi
GenBanki
DDBJi
Links Updated
M61883 mRNA. Translation: AAA30998.1.
M21174 mRNA. Translation: AAA30990.1.
UniGeneiSsc.14474.
Ssc.68696.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 29, 2014
This is version 84 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