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Protein

Glycodelin

Gene

PAEP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This protein is, quantitatively, the main protein synthesized and secreted in the endometrium from mid-luteal phase of the menstrual cycle and during the first semester of pregnancy.

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: CACAO
  • multicellular organism development Source: ProtInc
  • positive regulation of granulocyte macrophage colony-stimulating factor production Source: CACAO
  • positive regulation of interleukin-13 secretion Source: CACAO
  • positive regulation of interleukin-6 secretion Source: CACAO
  • transport Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Glycodelin
Short name:
GD
Alternative name(s):
Placental protein 14
Short name:
PP14
Pregnancy-associated endometrial alpha-2 globulin
Short name:
PAEG
Short name:
PEG
Progestagen-associated endometrial protein
Progesterone-associated endometrial protein
Gene namesi
Name:PAEP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:8573. PAEP.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32904.

Polymorphism and mutation databases

BioMutaiPAEP.
DMDMi130701.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18183 PublicationsAdd
BLAST
Chaini19 – 180162GlycodelinPRO_0000017953Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...)CAR_000123
Glycosylationi81 – 811N-linked (GlcNAc...)CAR_000124
Disulfide bondi84 ↔ 178By similarity
Disulfide bondi124 ↔ 137By similarity

Post-translational modificationi

At least two differentially glycosylated forms are found. Glycodelin-A (GdA) (amniotic fluid) with contraceptive and immunosuppressive activities and glycodelin-S (Gds) (seminal plasma) whose role is not yet known. The gender-specific glycosylation may serve to regulate key process involved in human reproduction.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP09466.
PaxDbiP09466.
PeptideAtlasiP09466.
PRIDEiP09466.

PTM databases

iPTMnetiP09466.
PhosphoSiteiP09466.
UniCarbKBiP09466.

Expressioni

Gene expression databases

BgeeiP09466.
CleanExiHS_PAEP.
ExpressionAtlasiP09466. baseline and differential.
GenevisibleiP09466. HS.

Organism-specific databases

HPAiCAB016762.
HPA020108.
HPA029473.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
GRAMD3Q96HH93EBI-465167,EBI-2832937

Protein-protein interaction databases

BioGridi111084. 19 interactions.
IntActiP09466. 14 interactions.
MINTiMINT-1209116.
STRINGi9606.ENSP00000277508.

Structurei

Secondary structure

1
180
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 334Combined sources
Beta strandi38 – 469Combined sources
Helixi47 – 493Combined sources
Beta strandi60 – 667Combined sources
Beta strandi72 – 798Combined sources
Beta strandi81 – 9313Combined sources
Beta strandi99 – 1046Combined sources
Beta strandi107 – 1159Combined sources
Beta strandi117 – 12711Combined sources
Beta strandi129 – 1324Combined sources
Beta strandi134 – 14411Combined sources
Helixi148 – 15811Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi167 – 1704Combined sources
Turni173 – 1753Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R0BX-ray2.45A20-180[»]
ProteinModelPortaliP09466.
SMRiP09466. Positions 26-178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410JCG3. Eukaryota.
ENOG4111386. LUCA.
GeneTreeiENSGT00620000088158.
HOGENOMiHOG000113272.
HOVERGENiHBG104361.
InParanoidiP09466.
OMAiAMATNNI.
PhylomeDBiP09466.
TreeFamiTF342475.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR002447. Blactoglobulin.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR01172. BLCTOGLOBULN.
PR00179. LIPOCALIN.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P09466-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLCLLLTLGV ALVCGVPAMD IPQTKQDLEL PKLAGTWHSM AMATNNISLM
60 70 80 90 100
ATLKAPLRVH ITSLLPTPED NLEIVLHRWE NNSCVEKKVL GEKTENPKKF
110 120 130 140 150
KINYTVANEA TLLDTDYDNF LFLCLQDTTT PIQSMMCQYL ARVLVEDDEI
160 170 180
MQGFIRAFRP LPRHLWYLLD LKQMEEPCRF
Length:180
Mass (Da):20,624
Last modified:March 1, 1992 - v2
Checksum:i0813A74A4231149E
GO
Isoform 2 (identifier: P09466-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     33-54: Missing.

Show »
Length:158
Mass (Da):18,279
Checksum:iFEB77A0B313F33C8
GO
Isoform 3 (identifier: P09466-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     33-126: Missing.

Show »
Length:86
Mass (Da):9,953
Checksum:i01C203BBE8D26652
GO

Sequence cautioni

The sequence AAA60147.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAB43305.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 373GTW → VTA AA sequence (PubMed:11278680).Curated
Sequence conflicti36 – 361T → K AA sequence (PubMed:3667877).Curated
Sequence conflicti95 – 951E → G (PubMed:3194393).Curated
Sequence conflicti152 – 1521Q → E (PubMed:3194393).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281L → V.
Corresponds to variant rs34284195 [ dbSNP | Ensembl ].
VAR_050178
Natural varianti126 – 1261Q → K.
Corresponds to variant rs3748210 [ dbSNP | Ensembl ].
VAR_034355

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei33 – 12694Missing in isoform 3. CuratedVSP_003141Add
BLAST
Alternative sequencei33 – 5422Missing in isoform 2. CuratedVSP_003140Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04129 mRNA. Translation: AAA60147.1. Different initiation.
M34046 Genomic DNA. Translation: AAA60148.1.
M61886 mRNA. Translation: AAA35801.1.
M61886 mRNA. Translation: AAA35802.1.
AL050169 mRNA. Translation: CAB43305.1. Different initiation.
AL354761 Genomic DNA. Translation: CAI17197.1.
BC069451 mRNA. Translation: AAH69451.1.
BC069562 mRNA. Translation: AAH69562.1.
BC112304 mRNA. Translation: AAI12305.1.
BC113728 mRNA. Translation: AAI13729.1.
CCDSiCCDS35173.1. [P09466-1]
PIRiA35570. A39167.
RefSeqiNP_001018058.1. NM_001018048.1. [P09466-2]
NP_001018059.1. NM_001018049.2. [P09466-1]
NP_002562.2. NM_002571.3. [P09466-1]
XP_011517051.1. XM_011518749.1. [P09466-1]
XP_011517053.1. XM_011518751.1. [P09466-2]
UniGeneiHs.532325.

Genome annotation databases

EnsembliENST00000277508; ENSP00000277508; ENSG00000122133. [P09466-1]
ENST00000371766; ENSP00000360831; ENSG00000122133. [P09466-1]
ENST00000479141; ENSP00000417898; ENSG00000122133. [P09466-1]
GeneIDi5047.
KEGGihsa:5047.
UCSCiuc004cgd.2. human. [P09466-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04129 mRNA. Translation: AAA60147.1. Different initiation.
M34046 Genomic DNA. Translation: AAA60148.1.
M61886 mRNA. Translation: AAA35801.1.
M61886 mRNA. Translation: AAA35802.1.
AL050169 mRNA. Translation: CAB43305.1. Different initiation.
AL354761 Genomic DNA. Translation: CAI17197.1.
BC069451 mRNA. Translation: AAH69451.1.
BC069562 mRNA. Translation: AAH69562.1.
BC112304 mRNA. Translation: AAI12305.1.
BC113728 mRNA. Translation: AAI13729.1.
CCDSiCCDS35173.1. [P09466-1]
PIRiA35570. A39167.
RefSeqiNP_001018058.1. NM_001018048.1. [P09466-2]
NP_001018059.1. NM_001018049.2. [P09466-1]
NP_002562.2. NM_002571.3. [P09466-1]
XP_011517051.1. XM_011518749.1. [P09466-1]
XP_011517053.1. XM_011518751.1. [P09466-2]
UniGeneiHs.532325.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R0BX-ray2.45A20-180[»]
ProteinModelPortaliP09466.
SMRiP09466. Positions 26-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111084. 19 interactions.
IntActiP09466. 14 interactions.
MINTiMINT-1209116.
STRINGi9606.ENSP00000277508.

PTM databases

iPTMnetiP09466.
PhosphoSiteiP09466.
UniCarbKBiP09466.

Polymorphism and mutation databases

BioMutaiPAEP.
DMDMi130701.

Proteomic databases

EPDiP09466.
PaxDbiP09466.
PeptideAtlasiP09466.
PRIDEiP09466.

Protocols and materials databases

DNASUi5047.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000277508; ENSP00000277508; ENSG00000122133. [P09466-1]
ENST00000371766; ENSP00000360831; ENSG00000122133. [P09466-1]
ENST00000479141; ENSP00000417898; ENSG00000122133. [P09466-1]
GeneIDi5047.
KEGGihsa:5047.
UCSCiuc004cgd.2. human. [P09466-1]

Organism-specific databases

CTDi5047.
GeneCardsiPAEP.
HGNCiHGNC:8573. PAEP.
HPAiCAB016762.
HPA020108.
HPA029473.
MIMi173310. gene.
neXtProtiNX_P09466.
PharmGKBiPA32904.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410JCG3. Eukaryota.
ENOG4111386. LUCA.
GeneTreeiENSGT00620000088158.
HOGENOMiHOG000113272.
HOVERGENiHBG104361.
InParanoidiP09466.
OMAiAMATNNI.
PhylomeDBiP09466.
TreeFamiTF342475.

Miscellaneous databases

GeneWikiiPAEP.
GenomeRNAii5047.
PROiP09466.
SOURCEiSearch...

Gene expression databases

BgeeiP09466.
CleanExiHS_PAEP.
ExpressionAtlasiP09466. baseline and differential.
GenevisibleiP09466. HS.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR002447. Blactoglobulin.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR01172. BLCTOGLOBULN.
PR00179. LIPOCALIN.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete amino acid sequence of human placental protein 14: a progesterone-regulated uterine protein homologous to beta-lactoglobulins."
    Julkunen M., Seppala M., Janne O.A.
    Proc. Natl. Acad. Sci. U.S.A. 85:8845-8849(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human placental protein 14 gene: sequence and characterization of a short duplication."
    Vaisse C., Atger M., Potier B., Milgrom E.
    DNA Cell Biol. 9:401-413(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Multiple forms of mRNA encoding human pregnancy-associated endometrial alpha 2-globulin, a beta-lactoglobulin homologue."
    Garde J., Bell S.C., Eperon I.C.
    Proc. Natl. Acad. Sci. U.S.A. 88:2456-2460(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  7. "Pregnancy-associated endometrial alpha 2-globulin, the major secretory protein of the luteal phase and first trimester pregnancy endometrium, is not glycosylated prolactin but related to beta-lactoglobulins."
    Bell S.C., Keyte J.W., Waites G.T.
    J. Clin. Endocrinol. Metab. 65:1067-1071(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-56.
  8. "Amino acid sequence homology between human placental protein 14 and beta-lactoglobulins from various species."
    Huhtala M.L., Seppala M., Narvanen A., Palomaki P., Julkunen M., Bohn H.
    Endocrinology 120:2620-2622(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-30.
  9. "Purification and characterization of an immunomodulatory endometrial protein, glycodelin."
    Vigne J.-L., Hornung D., Mueller M.D., Taylor R.N.
    J. Biol. Chem. 276:17101-17105(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-38.
    Tissue: Decidua.
  10. "Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities."
    Dell A., Morris H.R., Easton R.L., Panico M., Patankar M., Oehniger S., Koistinen R., Koistinen H., Seppala M., Clark G.F.
    J. Biol. Chem. 270:24116-24126(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATES OF GLYCODELIN-A.
    Tissue: Amniotic fluid.
  11. "Gender-specific glycosylation of human glycodelin affects its contraceptive activity."
    Morris H.R., Dell A., Easton R.L., Panico M., Koistinen H., Koistinen R., Oehninger S., Patankar M.S., Seppala M., Clark G.F.
    J. Biol. Chem. 271:32159-32167(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATES OF GLYCODELIN-S.
    Tissue: Seminal plasma.
  12. "Glycodelin from seminal plasma is a differentially glycosylated form of contraceptive glycodelin-A."
    Koistinen H., Koistinen R., Dell A., Morris H.R., Easton R.L., Patankar M.S., Oehninger S., Clark G.F., Seppala M.
    Mol. Hum. Reprod. 2:759-765(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATES.

Entry informationi

Entry nameiPAEP_HUMAN
AccessioniPrimary (citable) accession number: P09466
Secondary accession number(s): Q5T6T1, Q9UG92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 1, 1992
Last modified: July 6, 2016
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.