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Protein

Apomucin

Gene
N/A
Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: 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
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000158958‹1 – 1150ApomucinAdd BLAST›1150

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi? ↔ 1145PROSITE-ProRule annotation
Glycosylationi46O-linked (GalNAc...); partial1 Publication1
Glycosylationi50O-linked (GalNAc...); partial1 Publication1
Glycosylationi51O-linked (GalNAc...); partial1 Publication1
Glycosylationi57O-linked (GalNAc...); partial1 Publication1
Glycosylationi58O-linked (GalNAc...); partial1 Publication1
Glycosylationi61O-linked (GalNAc...); partial1 Publication1
Glycosylationi66O-linked (GalNAc...); partial1 Publication1
Glycosylationi67O-linked (GalNAc...); partial1 Publication1
Glycosylationi73O-linked (GalNAc...); partial1 Publication1
Glycosylationi74O-linked (GalNAc...); partial1 Publication1
Glycosylationi76O-linked (GalNAc...); partial1 Publication1
Glycosylationi77O-linked (GalNAc...); partial1 Publication1
Glycosylationi81O-linked (GalNAc...); partial1 Publication1
Glycosylationi83O-linked (GalNAc...); partial1 Publication1
Glycosylationi87O-linked (GalNAc...); partial1 Publication1
Glycosylationi91O-linked (GalNAc...); partial1 Publication1
Glycosylationi93O-linked (GalNAc...); partial1 Publication1
Glycosylationi94O-linked (GalNAc...); partial1 Publication1
Glycosylationi96O-linked (GalNAc...); partial1 Publication1
Glycosylationi98O-linked (GalNAc...); partial1 Publication1
Glycosylationi101O-linked (GalNAc...); partial1 Publication1
Glycosylationi103O-linked (GalNAc...); partial1 Publication1
Glycosylationi104O-linked (GalNAc...); partial1 Publication1
Glycosylationi106O-linked (GalNAc...); partial1 Publication1
Glycosylationi107O-linked (GalNAc...); partial1 Publication1
Glycosylationi108O-linked (GalNAc...); partial1 Publication1
Glycosylationi110O-linked (GalNAc...); partial1 Publication1
Glycosylationi114O-linked (GalNAc...); partial1 Publication1
Glycosylationi117O-linked (GalNAc...); partial1 Publication1
Glycosylationi123O-linked (GalNAc...); partial1 Publication1
Glycosylationi124O-linked (GalNAc...); partial1 Publication1
Glycosylationi418N-linked (GlcNAc...)Sequence analysis1
Glycosylationi547N-linked (GlcNAc...)Sequence analysis1
Glycosylationi917N-linked (GlcNAc...)Sequence analysis1
Glycosylationi985N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1002N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1062 ↔ 1109PROSITE-ProRule annotation
Glycosylationi1068N-linked (GlcNAc...)Sequence analysis1
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

Proteomic databases

PRIDEiP12021.

Expressioni

Tissue specificityi

Submaxillary mucosae.

Interactioni

Subunit structurei

Intermolecular disulfide bonds could help maintain a multimeric mucin structure.

Structurei

3D structure databases

ProteinModelPortaliP12021.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati‹1 – 441Add BLAST›44
Repeati45 – 1252Add BLAST81
Repeati126 – 2063Add BLAST81
Repeati207 – 2874Add BLAST81
Repeati288 – 3685Add BLAST81
Repeati369 – 3916; truncatedAdd BLAST23
Domaini929 – 995VWFCPROSITE-ProRule annotationAdd BLAST67
Domaini1062 – 1146CTCKPROSITE-ProRule annotationAdd BLAST85

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni‹1 – 3686 X 81 AA tandem repeatsAdd BLAST›368

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

HOVERGENiHBG006422.

Family and domain databases

InterProiIPR006207. Cys_knot_C.
IPR006208. Glyco_hormone_CN.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF00007. Cys_knot. 1 hit.
[Graphical view]
SMARTiSM00041. CT. 1 hit.
SM00214. VWC. 2 hits.
[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)DescriptionActionsGraphical viewLength
Non-terminal residuei11

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.
UniGeneiSsc.14474.
Ssc.68696.

3D structure databases

ProteinModelPortaliP12021.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP12021.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006422.

Family and domain databases

InterProiIPR006207. Cys_knot_C.
IPR006208. Glyco_hormone_CN.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF00007. Cys_knot. 1 hit.
[Graphical view]
SMARTiSM00041. CT. 1 hit.
SM00214. VWC. 2 hits.
[Graphical view]
PROSITEiPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 5, 2016
This is version 91 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.