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UniProtKB/Swiss-Prot entry P12273


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PIP_HUMAN
Primary accession number P12273
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on October 1, 1989 (Sequence version 1)
Annotations were last modified on    May 26, 2009 (Entry version 89)
Name and origin of the protein
Protein name Prolactin-inducible protein [Precursor]
Synonyms Prolactin-induced protein
Secretory actin-binding protein
SABP
Gross cystic disease fluid protein 15
GCDFP-15
gp17
Gene name
Name: PIP
Synonyms: GCDFP15, GPIP4
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3667631 [NCBI, ExPASy, EBI, Israel, Japan]
Murphy L.C., Tsuyuki D., Myal Y., Shiu R.P.C.;
"Isolation and sequencing of a cDNA clone for a prolactin-inducible protein (PIP). Regulation of PIP gene expression in the human breast cancer cell line, T-47D.";
J. Biol. Chem. 262:15236-15241(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0303-7207(91)90153-J; PubMed=1955075 [NCBI, ExPASy, EBI, Israel, Japan]
Myal Y., Iwasiow B., Tsuyuki D., Wong P., Shiu R.P.C.;
"The prolactin-inducible protein (PIP/GCDFP-15) gene: cloning, structure and regulation.";
Mol. Cell. Endocrinol. 80:165-175(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Seminal vesicle;
DOI=10.1007/s002510050215; PubMed=9218538 [NCBI, ExPASy, EBI, Israel, Japan]
Autiero M., Bouchier C., Basmaciogullari S., Zaborski P., el Marhomy S., Martin M., Guardiola J., Piatier-Tonneau D.;
"Isolation from a human seminal vesicle library of the cDNA for gp17, a CD4 binding factor.";
Immunogenetics 46:345-348(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 29-146, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-105.
DOI=10.1111/j.1432-1033.1991.tb15873.x; PubMed=2013294 [NCBI, ExPASy, EBI, Israel, Japan]
Schaller J., Akiyama K., Kimura H., Hess D., Affolter M., Rickli E.E.;
"Primary structure of a new actin-binding protein from human seminal plasma.";
Eur. J. Biochem. 196:743-750(1991).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105, AND MASS SPECTROMETRY.
TISSUE=Saliva;
DOI=10.1021/pr050492k; PubMed=16740002 [NCBI, ExPASy, EBI, Israel, Japan]
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.";
J. Proteome Res. 5:1493-1503(2006).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105, AND MASS SPECTROMETRY.
TISSUE=Milk;
DOI=10.1002/pmic.200701057; PubMed=18780401 [NCBI, ExPASy, EBI, Israel, Japan]
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
[8]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 29-146 IN COMPLEX WITH AZGP1, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-105.
DOI=10.1016/j.jmb.2008.09.072; PubMed=18930737 [NCBI, ExPASy, EBI, Israel, Japan]
Hassan M.I., Bilgrami S., Kumar V., Singh N., Yadav S., Kaur P., Singh T.P.;
"Crystal structure of the novel complex formed between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP) from human seminal plasma.";
J. Mol. Biol. 384:663-672(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J03460; AAA60091.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X51501; CAA35870.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X51502; CAA35870.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X51504; CAA35870.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y10179; CAA71252.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010950; AAH10950.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010951; AAH10951.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00022974; -.
PIR I37432; SQHUAC.
RefSeq NP_002643.1; -.
UniGene Hs.99949
3D structure databases
PDB
3ES6; X-ray; 3.23 A; B=29-146.[ExPASy / RCSB / EBI]
PDBsum 3ES6; -.
ModBase P12273.
Protein-protein interaction databases
IntAct P12273; 2.
PTM databases
PhosphoSite P12273; -.
Organism-specific databases
GeneCards GC07P142539; -.
H-InvDB HIX0007165; -.
HGNC HGNC:8993; PIP.
GenAtlas PIP.
HPA CAB002661; -.
HPA009177; -.
MIM 176720; gene. [NCBI / EBI]
PharmGKB PA142672601; -.
Gene expression databases
ArrayExpress P12273; -.
Bgee P12273; -.
CleanEx HS_PIP; -.
GermOnline ENSG00000159763; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0003779; Molecular function: actin binding (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR007990; SV_autoAg.
Graphical view of domain structure.
PANTHER PTHR15096; SV_autoAg; 1.
Pfam PF05326; SVA; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF002572; PIP-GCDFP-15; 1.
ProDom PD021604; SV_autoAg; 1.
[Domain structure / List of seq. sharing at least 1 domain]
Proteomic databases
PeptideAtlas P12273; -.
PRIDE P12273; -.
Genome annotation databases
Ensembl ENSG00000159763; Homo sapiens. [Contig view]
GeneID 5304; -.
KEGG hsa:5304; -.
Phylogenomic databases
HOGENOM P12273; -.
HOVERGEN P12273; -.
OMA P12273; RELGICP.
Other
NextBio 20502; -.
SOURCE PIP; Homo sapiens.
ProtoNet P12273.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Actin-binding; Direct protein sequencing; Disulfide bond; Glycoprotein; Pyrrolidone carboxylic acid; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    28  28      
CHAIN   29   146  118     Prolactin-inducible protein. PRO_0000024288
MOD_RES   29    29        Pyrrolidone carboxylic acid. 
CARBOHYD   105   105        N-linked (GlcNAc...). 
DISULFID   65    91         
DISULFID   89   123         
STRAND   36    38  3      
STRAND   44    46  3      
STRAND   52    60  9      
STRAND   66    76  11      
HELIX   80    83  4      
STRAND   86    90  5      
STRAND   92    94  3      
STRAND   96   102  7      
STRAND   108   116  9      
STRAND   120   123  4      
HELIX   124   126  3      
STRAND   129   133  5      
STRAND   140   145  6      
Sequence information
Length: 146 AA [This is the length of the unprocessed precursor] Molecular weight: 16572 Da [This is the MW of the unprocessed precursor] CRC64: 93F3DA201133F03C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRLLQLLFRA SPATLLLVLC LQLGANKAQD NTRKIIIKNF DIPKSVRPND EVTAVLAVQT 

        70         80         90        100        110        120 
ELKECMVVKT YLISSIPLQG AFNYKYTACL CDDNPKTFYW DFYTNRTVQI AAVVDVIREL 

       130        140 
GICPDDAAVI PIKNNRFYTI EILKVE 

P12273 in FASTA format

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