PAEP_HUMAN
ID PAEP_HUMAN Reviewed; 180 AA.
AC P09466; Q5T6T1; Q9UG92;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Glycodelin;
DE Short=GD;
DE AltName: Full=Placental protein 14 {ECO:0000303|PubMed:3569148, ECO:0000303|PubMed:9918684};
DE Short=PP14;
DE AltName: Full=Pregnancy-associated endometrial alpha-2 globulin {ECO:0000303|PubMed:3667877};
DE Short=PAEG;
DE Short=PEG;
DE AltName: Full=Progestagen-associated endometrial protein;
DE AltName: Full=Progesterone-associated endometrial protein;
DE AltName: Full=Zona-binding inhibitory factor-1 {ECO:0000303|PubMed:12672671};
DE Short=ZIF-1 {ECO:0000303|PubMed:12672671};
DE Flags: Precursor;
GN Name=PAEP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3194393; DOI=10.1073/pnas.85.23.8845;
RA Julkunen M., Seppala M., Janne O.A.;
RT "Complete amino acid sequence of human placental protein 14: a
RT progesterone-regulated uterine protein homologous to beta-lactoglobulins.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:8845-8849(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2206398; DOI=10.1089/dna.1990.9.401;
RA Vaisse C., Atger M., Potier B., Milgrom E.;
RT "Human placental protein 14 gene: sequence and characterization of a short
RT duplication.";
RL DNA Cell Biol. 9:401-413(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=2006183; DOI=10.1073/pnas.88.6.2456;
RA Garde J., Bell S.C., Eperon I.C.;
RT "Multiple forms of mRNA encoding human pregnancy-associated endometrial
RT alpha 2-globulin, a beta-lactoglobulin homologue.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2456-2460(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 19-56, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=3667877; DOI=10.1210/jcem-65-5-1067;
RA Bell S.C., Keyte J.W., Waites G.T.;
RT "Pregnancy-associated endometrial alpha 2-globulin, the major secretory
RT protein of the luteal phase and first trimester pregnancy endometrium, is
RT not glycosylated prolactin but related to beta-lactoglobulins.";
RL J. Clin. Endocrinol. Metab. 65:1067-1071(1987).
RN [8]
RP PROTEIN SEQUENCE OF 19-30.
RX PubMed=3569148; DOI=10.1210/endo-120-6-2620;
RA Huhtala M.L., Seppala M., Narvanen A., Palomaki P., Julkunen M., Bohn H.;
RT "Amino acid sequence homology between human placental protein 14 and beta-
RT lactoglobulins from various species.";
RL Endocrinology 120:2620-2622(1987).
RN [9]
RP PROTEIN SEQUENCE OF 19-38.
RC TISSUE=Decidua;
RX PubMed=11278680; DOI=10.1074/jbc.m010451200;
RA Vigne J.-L., Hornung D., Mueller M.D., Taylor R.N.;
RT "Purification and characterization of an immunomodulatory endometrial
RT protein, glycodelin.";
RL J. Biol. Chem. 276:17101-17105(2001).
RN [10]
RP PROTEIN SEQUENCE OF 19-43, STRUCTURE OF CARBOHYRATES OF GLYCODELIN-F,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=12672671; DOI=10.1095/biolreprod.102.012658;
RA Chiu P.C., Koistinen R., Koistinen H., Seppala M., Lee K.F., Yeung W.S.;
RT "Zona-binding inhibitory factor-1 from human follicular fluid is an isoform
RT of glycodelin.";
RL Biol. Reprod. 69:365-372(2003).
RN [11]
RP FUNCTION OF GLYCODELIN-A.
RX PubMed=7531163; DOI=10.1016/s0015-0282(16)57372-5;
RA Oehninger S., Coddington C.C., Hodgen G.D., Seppala M.;
RT "Factors affecting fertilization: endometrial placental protein 14 reduces
RT the capacity of human spermatozoa to bind to the human zona pellucida.";
RL Fertil. Steril. 63:377-383(1995).
RN [12]
RP STRUCTURE OF CARBOHYDRATES OF GLYCODELIN-A, GLYCOSYLATION AT ASN-46 AND
RP ASN-81, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Amniotic fluid;
RX PubMed=7592613; DOI=10.1074/jbc.270.41.24116;
RA Dell A., Morris H.R., Easton R.L., Panico M., Patankar M., Oehniger S.,
RA Koistinen R., Koistinen H., Seppala M., Clark G.F.;
RT "Structural analysis of the oligosaccharides derived from glycodelin, a
RT human glycoprotein with potent immunosuppressive and contraceptive
RT activities.";
RL J. Biol. Chem. 270:24116-24126(1995).
RN [13]
RP STRUCTURE OF CARBOHYDRATES OF GLYCODELIN-S.
RC TISSUE=Seminal plasma;
RX PubMed=8943270; DOI=10.1074/jbc.271.50.32159;
RA Morris H.R., Dell A., Easton R.L., Panico M., Koistinen H., Koistinen R.,
RA Oehninger S., Patankar M.S., Seppala M., Clark G.F.;
RT "Gender-specific glycosylation of human glycodelin affects its
RT contraceptive activity.";
RL J. Biol. Chem. 271:32159-32167(1996).
RN [14]
RP STRUCTURE OF CARBOHYDRATES OF GLYCODELIN-S, TISSUE SPECIFICITY, AND
RP SUBUNIT.
RX PubMed=9239694; DOI=10.1093/molehr/2.10.759;
RA Koistinen H., Koistinen R., Dell A., Morris H.R., Easton R.L.,
RA Patankar M.S., Oehninger S., Clark G.F., Seppala M.;
RT "Glycodelin from seminal plasma is a differentially glycosylated form of
RT contraceptive glycodelin-A.";
RL Mol. Hum. Reprod. 2:759-765(1996).
RN [15]
RP FUNCTION.
RX PubMed=9918684; DOI=10.1006/cimm.1998.1408;
RA Rachmilewitz J., Riely G.J., Tykocinski M.L.;
RT "Placental protein 14 functions as a direct T-cell inhibitor.";
RL Cell. Immunol. 191:26-33(1999).
RN [16]
RP FUNCTION OF GLYCODELIN-S.
RX PubMed=15883155; DOI=10.1074/jbc.m504103200;
RA Chiu P.C., Chung M.K., Tsang H.Y., Koistinen R., Koistinen H., Seppala M.,
RA Lee K.F., Yeung W.S.;
RT "Glycodelin-S in human seminal plasma reduces cholesterol efflux and
RT inhibits capacitation of spermatozoa.";
RL J. Biol. Chem. 280:25580-25589(2005).
RN [17]
RP STRUCTURE OF CARBOHYDRATES OF GLYCODELIN-C, FUNCTION, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=17192260; DOI=10.1074/jbc.m607482200;
RA Chiu P.C., Chung M.K., Koistinen R., Koistinen H., Seppala M., Ho P.C.,
RA Ng E.H., Lee K.F., Yeung W.S.;
RT "Cumulus oophorus-associated glycodelin-C displaces sperm-bound glycodelin-
RT A and -F and stimulates spermatozoa-zona pellucida binding.";
RL J. Biol. Chem. 282:5378-5388(2007).
RN [18] {ECO:0007744|PDB:4R0B}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 20-180, DISULFIDE BONDS, AND
RP SUBUNIT.
RX PubMed=25422905; DOI=10.1042/bj20141003;
RA Schiefner A., Rodewald F., Neumaier I., Skerra A.;
RT "The dimeric crystal structure of the human fertility lipocalin glycodelin
RT reveals a protein scaffold for the presentation of complex glycans.";
RL Biochem. J. 466:95-104(2015).
CC -!- FUNCTION: Glycoprotein that regulates critical steps during
CC fertilization and also has immunomonomodulatory effects. Four
CC glycoforms, namely glycodelin-S, -A, -F and -C have been identified in
CC reproductive tissues that differ in glycosylation and biological
CC activity. Glycodelin-A has contraceptive and immunosuppressive
CC activities (PubMed:9918684, PubMed:7531163). Glycodelin-C stimulates
CC binding of spermatozoa to the zona pellucida (PubMed:17192260).
CC Glycodelin-F inhibits spermatozoa-zona pellucida binding and
CC significantly suppresses progesterone-induced acrosome reaction of
CC spermatozoa (PubMed:12672671). Glycodelin-S in seminal plasma maintains
CC the uncapacitated state of human spermatozoa (PubMed:15883155).
CC {ECO:0000269|PubMed:12672671, ECO:0000269|PubMed:15883155,
CC ECO:0000269|PubMed:17192260, ECO:0000269|PubMed:7531163,
CC ECO:0000269|PubMed:9918684}.
CC -!- SUBUNIT: Homodimer (PubMed:25422905, PubMed:9239694).
CC {ECO:0000269|PubMed:25422905, ECO:0000269|PubMed:9239694}.
CC -!- INTERACTION:
CC P09466; Q13520: AQP6; NbExp=3; IntAct=EBI-465167, EBI-13059134;
CC P09466; O43315: AQP9; NbExp=3; IntAct=EBI-465167, EBI-17444777;
CC P09466; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-465167, EBI-11343438;
CC P09466; P60508: ERVFRD-1; NbExp=3; IntAct=EBI-465167, EBI-17973325;
CC P09466; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-465167, EBI-3917143;
CC P09466; O15529: GPR42; NbExp=3; IntAct=EBI-465167, EBI-18076404;
CC P09466; Q8TED1: GPX8; NbExp=3; IntAct=EBI-465167, EBI-11721746;
CC P09466; Q96HH9: GRAMD2B; NbExp=8; IntAct=EBI-465167, EBI-2832937;
CC P09466; P31937: HIBADH; NbExp=3; IntAct=EBI-465167, EBI-11427100;
CC P09466; Q8IU57: IFNLR1; NbExp=3; IntAct=EBI-465167, EBI-373215;
CC P09466; Q9Y5G9: PCDHGA4; NbExp=3; IntAct=EBI-465167, EBI-12956949;
CC P09466; Q9Y320: TMX2; NbExp=3; IntAct=EBI-465167, EBI-6447886;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12672671,
CC ECO:0000269|PubMed:17192260, ECO:0000269|PubMed:3667877}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P09466-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09466-2; Sequence=VSP_003140;
CC Name=3;
CC IsoId=P09466-3; Sequence=VSP_003141;
CC -!- TISSUE SPECIFICITY: This protein is, the main protein synthesized and
CC secreted in the endometrium from mid-luteal phase of the menstrual
CC cycle and during the first semester of pregnancy (PubMed:3667877).
CC Glycodelin-A is expressed in amniotic fluid, endometrium/decidua and
CC maternal serum (at protein level) (PubMed:3194393). Glycodelin-F is
CC expressed in follicular fluid, luteinized granulosa cells and the
CC oviduct (at protein level) (PubMed:12672671). Glycodelin-S is expressed
CC in seminal plasma and seminal vesicles (at protein level)
CC (PubMed:9239694). Glycodelin-C is detected in cumulus cells (at protein
CC level), but cumulus cells do not synthesize Glycodelin-C but take up
CC and convert glycodelin-A and -F vis glycan remodeling
CC (PubMed:17192260). {ECO:0000269|PubMed:12672671,
CC ECO:0000269|PubMed:17192260, ECO:0000269|PubMed:3194393,
CC ECO:0000269|PubMed:3667877, ECO:0000269|PubMed:9239694}.
CC -!- PTM: Four distinct glycoforms A, C, F and S arise from different N-
CC linked oligosaccharide chains at amino acid residues Asn-46 and Asn-81.
CC Glycodelin-A and -F are taken up by the cumulus cells in which partial
CC deglycosylation takes place to produce glycodelin-C.
CC {ECO:0000269|PubMed:12672671, ECO:0000269|PubMed:17192260,
CC ECO:0000269|PubMed:7592613, ECO:0000269|PubMed:8943270}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60147.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB43305.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PAEPID46067ch9q34.html";
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DR EMBL; J04129; AAA60147.1; ALT_INIT; mRNA.
DR EMBL; M34046; AAA60148.1; -; Genomic_DNA.
DR EMBL; M61886; AAA35801.1; -; mRNA.
DR EMBL; M61886; AAA35802.1; -; mRNA.
DR EMBL; AL050169; CAB43305.1; ALT_INIT; mRNA.
DR EMBL; AL354761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069451; AAH69451.1; -; mRNA.
DR EMBL; BC069562; AAH69562.1; -; mRNA.
DR EMBL; BC112304; AAI12305.1; -; mRNA.
DR EMBL; BC113728; AAI13729.1; -; mRNA.
DR CCDS; CCDS35173.1; -. [P09466-1]
DR PIR; A35570; A39167.
DR RefSeq; NP_001018058.1; NM_001018048.1. [P09466-2]
DR RefSeq; NP_001018059.1; NM_001018049.2. [P09466-1]
DR RefSeq; NP_002562.2; NM_002571.3. [P09466-1]
DR RefSeq; XP_011517051.1; XM_011518749.2. [P09466-1]
DR RefSeq; XP_011517053.1; XM_011518751.1. [P09466-2]
DR PDB; 4R0B; X-ray; 2.45 A; A=20-180.
DR PDBsum; 4R0B; -.
DR AlphaFoldDB; P09466; -.
DR SMR; P09466; -.
DR BioGRID; 111084; 69.
DR IntAct; P09466; 25.
DR MINT; P09466; -.
DR STRING; 9606.ENSP00000417898; -.
DR DrugBank; DB02405; 12-Bromododecanoic Acid.
DR DrugBank; DB09462; Glycerin.
DR DrugBank; DB03796; Palmitic Acid.
DR GlyConnect; 177; 20 N-Linked glycans (2 sites).
DR GlyGen; P09466; 3 sites, 41 N-linked glycans (3 sites).
DR iPTMnet; P09466; -.
DR PhosphoSitePlus; P09466; -.
DR BioMuta; PAEP; -.
DR DMDM; 130701; -.
DR jPOST; P09466; -.
DR MassIVE; P09466; -.
DR PaxDb; P09466; -.
DR PeptideAtlas; P09466; -.
DR PRIDE; P09466; -.
DR ProteomicsDB; 52220; -. [P09466-1]
DR ProteomicsDB; 52221; -. [P09466-2]
DR ProteomicsDB; 52222; -. [P09466-3]
DR Antibodypedia; 3391; 384 antibodies from 30 providers.
DR DNASU; 5047; -.
DR Ensembl; ENST00000277508.9; ENSP00000277508.5; ENSG00000122133.17. [P09466-1]
DR Ensembl; ENST00000371766.6; ENSP00000360831.1; ENSG00000122133.17. [P09466-1]
DR Ensembl; ENST00000479141.6; ENSP00000417898.1; ENSG00000122133.17. [P09466-1]
DR GeneID; 5047; -.
DR KEGG; hsa:5047; -.
DR MANE-Select; ENST00000479141.6; ENSP00000417898.1; NM_002571.4; NP_002562.2.
DR UCSC; uc004cgd.2; human. [P09466-1]
DR CTD; 5047; -.
DR DisGeNET; 5047; -.
DR GeneCards; PAEP; -.
DR HGNC; HGNC:8573; PAEP.
DR HPA; ENSG00000122133; Tissue enriched (endometrium).
DR MalaCards; PAEP; -.
DR MIM; 173310; gene.
DR neXtProt; NX_P09466; -.
DR OpenTargets; ENSG00000122133; -.
DR PharmGKB; PA32904; -.
DR VEuPathDB; HostDB:ENSG00000122133; -.
DR eggNOG; ENOG502T0EI; Eukaryota.
DR GeneTree; ENSGT01050000244868; -.
DR InParanoid; P09466; -.
DR OMA; WEDNRCV; -.
DR OrthoDB; 1551422at2759; -.
DR PhylomeDB; P09466; -.
DR TreeFam; TF342475; -.
DR PathwayCommons; P09466; -.
DR SignaLink; P09466; -.
DR BioGRID-ORCS; 5047; 14 hits in 1069 CRISPR screens.
DR ChiTaRS; PAEP; human.
DR GeneWiki; PAEP; -.
DR GenomeRNAi; 5047; -.
DR Pharos; P09466; Tbio.
DR PRO; PR:P09466; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P09466; protein.
DR Bgee; ENSG00000122133; Expressed in decidua and 92 other tissues.
DR ExpressionAtlas; P09466; baseline and differential.
DR Genevisible; P09466; HS.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IDA:CACAO.
DR GO; GO:1902491; P:negative regulation of sperm capacitation; IMP:UniProtKB.
DR GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IDA:CACAO.
DR GO; GO:2000359; P:regulation of binding of sperm to zona pellucida; IDA:UniProtKB.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR002447; Blactoglobulin.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002345; Lipocalin.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11430; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01172; BLCTOGLOBULN.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:11278680,
FT ECO:0000269|PubMed:3569148, ECO:0000269|PubMed:3667877"
FT CHAIN 19..180
FT /note="Glycodelin"
FT /id="PRO_0000017953"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:7592613"
FT /id="CAR_000123"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:7592613"
FT /id="CAR_000124"
FT DISULFID 84..178
FT /evidence="ECO:0000269|PubMed:25422905,
FT ECO:0007744|PDB:4R0B"
FT DISULFID 124..137
FT /evidence="ECO:0000269|PubMed:25422905,
FT ECO:0007744|PDB:4R0B"
FT VAR_SEQ 33..126
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003141"
FT VAR_SEQ 33..54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003140"
FT VARIANT 28
FT /note="L -> V (in dbSNP:rs34284195)"
FT /id="VAR_050178"
FT VARIANT 126
FT /note="Q -> K (in dbSNP:rs3748210)"
FT /id="VAR_034355"
FT CONFLICT 35..37
FT /note="GTW -> VTA (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="T -> K (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="E -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="Q -> E (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:4R0B"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:4R0B"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4R0B"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4R0B"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:4R0B"
FT STRAND 81..93
FT /evidence="ECO:0007829|PDB:4R0B"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:4R0B"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:4R0B"
FT STRAND 117..127
FT /evidence="ECO:0007829|PDB:4R0B"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:4R0B"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:4R0B"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:4R0B"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4R0B"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:4R0B"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:4R0B"
SQ SEQUENCE 180 AA; 20624 MW; 0813A74A4231149E CRC64;
MLCLLLTLGV ALVCGVPAMD IPQTKQDLEL PKLAGTWHSM AMATNNISLM ATLKAPLRVH
ITSLLPTPED NLEIVLHRWE NNSCVEKKVL GEKTENPKKF KINYTVANEA TLLDTDYDNF
LFLCLQDTTT PIQSMMCQYL ARVLVEDDEI MQGFIRAFRP LPRHLWYLLD LKQMEEPCRF
