Full text data of PIP
PIP
(GCDFP15, GPIP4)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Prolactin-inducible protein (Gross cystic disease fluid protein 15; GCDFP-15; Prolactin-induced protein; Secretory actin-binding protein; SABP; gp17; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Prolactin-inducible protein (Gross cystic disease fluid protein 15; GCDFP-15; Prolactin-induced protein; Secretory actin-binding protein; SABP; gp17; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00022974
IPI00022974 Prolactin Prolactin membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 4 n/a n/a extracellular binds RBC n/a found at its expected molecular weight found at molecular weight
IPI00022974 Prolactin Prolactin membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 4 n/a n/a extracellular binds RBC n/a found at its expected molecular weight found at molecular weight
UniProt
P12273
ID PIP_HUMAN Reviewed; 146 AA.
AC P12273; A0A963; A0A9C3; A0A9F3; A4D2I1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1989, sequence version 1.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Prolactin-inducible protein;
DE AltName: Full=Gross cystic disease fluid protein 15;
DE Short=GCDFP-15;
DE AltName: Full=Prolactin-induced protein;
DE AltName: Full=Secretory actin-binding protein;
DE Short=SABP;
DE AltName: Full=gp17;
DE Flags: Precursor;
GN Name=PIP; Synonyms=GCDFP15, GPIP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3667631;
RA Murphy L.C., Tsuyuki D., Myal Y., Shiu R.P.C.;
RT "Isolation and sequencing of a cDNA clone for a prolactin-inducible
RT protein (PIP). Regulation of PIP gene expression in the human breast
RT cancer cell line, T-47D.";
RL J. Biol. Chem. 262:15236-15241(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1955075; DOI=10.1016/0303-7207(91)90153-J;
RA Myal Y., Iwasiow B., Tsuyuki D., Wong P., Shiu R.P.C.;
RT "The prolactin-inducible protein (PIP/GCDFP-15) gene: cloning,
RT structure and regulation.";
RL Mol. Cell. Endocrinol. 80:165-175(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seminal vesicle;
RX PubMed=9218538; DOI=10.1007/s002510050215;
RA Autiero M., Bouchier C., Basmaciogullari S., Zaborski P.,
RA el Marhomy S., Martin M., Guardiola J., Piatier-Tonneau D.;
RT "Isolation from a human seminal vesicle library of the cDNA for gp17,
RT a CD4 binding factor.";
RL Immunogenetics 46:345-348(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 29-146, DISULFIDE BONDS, AND GLYCOSYLATION AT
RP ASN-105.
RX PubMed=2013294; DOI=10.1111/j.1432-1033.1991.tb15873.x;
RA Schaller J., Akiyama K., Kimura H., Hess D., Affolter M., Rickli E.E.;
RT "Primary structure of a new actin-binding protein from human seminal
RT plasma.";
RL Eur. J. Biochem. 196:743-750(1991).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-146.
RX PubMed=16949771; DOI=10.1016/j.gene.2006.07.014;
RA Kitano T., Tian W., Umetsu K., Yuasa I., Yamazaki K., Saitou N.,
RA Osawa M.;
RT "Origin and evolution of gene for prolactin-induced protein.";
RL Gene 383:64-70(2006).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105, AND MASS
RP SPECTROMETRY.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
RA Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by
RT glycoprotein capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105, AND MASS
RP SPECTROMETRY.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 29-146 IN COMPLEX WITH AZGP1,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-105.
RX PubMed=18930737; DOI=10.1016/j.jmb.2008.09.072;
RA Hassan M.I., Bilgrami S., Kumar V., Singh N., Yadav S., Kaur P.,
RA Singh T.P.;
RT "Crystal structure of the novel complex formed between zinc alpha2-
RT glycoprotein (ZAG) and prolactin-inducible protein (PIP) from human
RT seminal plasma.";
RL J. Mol. Biol. 384:663-672(2008).
CC -!- SUBUNIT: Monomer. Interacts with AZGP1.
CC -!- INTERACTION:
CC Q9UHQ7:WBP5; NbExp=1; IntAct=EBI-1049746, EBI-1051372;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in pathological conditions of the
CC mammary gland and in several exocrine tissues, such as the
CC lacrimal, salivary, and sweat glands.
CC -!- INDUCTION: By prolactin and androgen; inhibited by estrogen.
CC -!- SIMILARITY: Belongs to the PIP family.
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DR EMBL; J03460; AAA60091.1; -; mRNA.
DR EMBL; X51501; CAA35870.1; -; Genomic_DNA.
DR EMBL; X51502; CAA35870.1; JOINED; Genomic_DNA.
DR EMBL; X51504; CAA35870.1; JOINED; Genomic_DNA.
DR EMBL; Y10179; CAA71252.1; -; mRNA.
DR EMBL; AK312227; BAG35160.1; -; mRNA.
DR EMBL; CH236959; EAL23781.1; -; Genomic_DNA.
DR EMBL; CH471198; EAW51887.1; -; Genomic_DNA.
DR EMBL; BC010950; AAH10950.1; -; mRNA.
DR EMBL; BC010951; AAH10951.1; -; mRNA.
DR EMBL; AB267097; BAF35627.1; -; Genomic_DNA.
DR EMBL; AB267098; BAF35628.1; -; Genomic_DNA.
DR EMBL; AB267099; BAF35629.1; -; Genomic_DNA.
DR EMBL; AB267100; BAF35630.1; -; Genomic_DNA.
DR EMBL; AB267101; BAF35631.1; -; Genomic_DNA.
DR EMBL; AB267102; BAF35632.1; -; Genomic_DNA.
DR EMBL; AB267103; BAF35633.1; -; Genomic_DNA.
DR EMBL; AB267104; BAF35634.1; -; Genomic_DNA.
DR EMBL; AB267105; BAF35635.1; -; Genomic_DNA.
DR EMBL; AB267106; BAF35636.1; -; Genomic_DNA.
DR EMBL; AB267107; BAF35637.1; -; Genomic_DNA.
DR EMBL; AB267108; BAF35638.1; -; Genomic_DNA.
DR EMBL; AB267109; BAF35639.1; -; Genomic_DNA.
DR EMBL; AB267110; BAF35640.1; -; Genomic_DNA.
DR EMBL; AB267111; BAF35641.1; -; Genomic_DNA.
DR EMBL; AB267112; BAF35642.1; -; Genomic_DNA.
DR EMBL; AB267113; BAF35643.1; -; Genomic_DNA.
DR EMBL; AB267114; BAF35644.1; -; Genomic_DNA.
DR EMBL; AB267115; BAF35645.1; -; Genomic_DNA.
DR EMBL; AB267116; BAF35646.1; -; Genomic_DNA.
DR EMBL; AB267117; BAF35647.1; -; Genomic_DNA.
DR EMBL; AB267118; BAF35648.1; -; Genomic_DNA.
DR EMBL; AB267119; BAF35649.1; -; Genomic_DNA.
DR EMBL; AB267120; BAF35650.1; -; Genomic_DNA.
DR EMBL; AB267121; BAF35651.1; -; Genomic_DNA.
DR EMBL; AB267122; BAF35652.1; -; Genomic_DNA.
DR EMBL; AB267123; BAF35653.1; -; Genomic_DNA.
DR EMBL; AB267124; BAF35654.1; -; Genomic_DNA.
DR EMBL; AB267125; BAF35655.1; -; Genomic_DNA.
DR EMBL; AB267126; BAF35656.1; -; Genomic_DNA.
DR EMBL; AB267127; BAF35657.1; -; Genomic_DNA.
DR EMBL; AB267128; BAF35658.1; -; Genomic_DNA.
DR EMBL; AB267129; BAF35659.1; -; Genomic_DNA.
DR EMBL; AB267130; BAF35660.1; -; Genomic_DNA.
DR EMBL; AB267131; BAF35661.1; -; Genomic_DNA.
DR EMBL; AB267132; BAF35662.1; -; Genomic_DNA.
DR EMBL; AB267133; BAF35663.1; -; Genomic_DNA.
DR EMBL; AB267134; BAF35664.1; -; Genomic_DNA.
DR EMBL; AB267135; BAF35665.1; -; Genomic_DNA.
DR EMBL; AB267136; BAF35666.1; -; Genomic_DNA.
DR EMBL; AB267137; BAF35667.1; -; Genomic_DNA.
DR EMBL; AB267138; BAF35668.1; -; Genomic_DNA.
DR EMBL; AB267139; BAF35669.1; -; Genomic_DNA.
DR EMBL; AB267140; BAF35670.1; -; Genomic_DNA.
DR EMBL; AB267141; BAF35671.1; -; Genomic_DNA.
DR EMBL; AB267142; BAF35672.1; -; Genomic_DNA.
DR EMBL; AB267143; BAF35673.1; -; Genomic_DNA.
DR EMBL; AB267144; BAF35674.1; -; Genomic_DNA.
DR EMBL; AB267145; BAF35675.1; -; Genomic_DNA.
DR EMBL; AB267146; BAF35676.1; -; Genomic_DNA.
DR EMBL; AB267147; BAF35677.1; -; Genomic_DNA.
DR EMBL; AB267148; BAF35678.1; -; Genomic_DNA.
DR EMBL; AB267149; BAF35679.1; -; Genomic_DNA.
DR EMBL; AB267150; BAF35680.1; -; Genomic_DNA.
DR EMBL; AB267151; BAF35681.1; -; Genomic_DNA.
DR EMBL; AB267152; BAF35682.1; -; Genomic_DNA.
DR EMBL; AB267153; BAF35683.1; -; Genomic_DNA.
DR EMBL; AB267154; BAF35684.1; -; Genomic_DNA.
DR EMBL; AB267155; BAF35685.1; -; Genomic_DNA.
DR EMBL; AB267156; BAF35686.1; -; Genomic_DNA.
DR EMBL; AB267157; BAF35687.1; -; Genomic_DNA.
DR EMBL; AB267158; BAF35688.1; -; Genomic_DNA.
DR EMBL; AB267159; BAF35689.1; -; Genomic_DNA.
DR EMBL; AB267160; BAF35690.1; -; Genomic_DNA.
DR EMBL; AB267161; BAF35691.1; -; Genomic_DNA.
DR EMBL; AB267162; BAF35692.1; -; Genomic_DNA.
DR EMBL; AB267163; BAF35693.1; -; Genomic_DNA.
DR EMBL; AB267164; BAF35694.1; -; Genomic_DNA.
DR EMBL; AB267165; BAF35695.1; -; Genomic_DNA.
DR EMBL; AB267166; BAF35696.1; -; Genomic_DNA.
DR EMBL; AB267167; BAF35697.1; -; Genomic_DNA.
DR EMBL; AB267168; BAF35698.1; -; Genomic_DNA.
DR EMBL; AB267169; BAF35699.1; -; Genomic_DNA.
DR EMBL; AB267170; BAF35700.1; -; Genomic_DNA.
DR EMBL; AB267171; BAF35701.1; -; Genomic_DNA.
DR EMBL; AB267172; BAF35702.1; -; Genomic_DNA.
DR EMBL; AB267173; BAF35703.1; -; Genomic_DNA.
DR EMBL; AB267174; BAF35704.1; -; Genomic_DNA.
DR EMBL; AB267175; BAF35705.1; -; Genomic_DNA.
DR EMBL; AB267176; BAF35706.1; -; Genomic_DNA.
DR EMBL; AB267177; BAF35707.1; -; Genomic_DNA.
DR EMBL; AB267178; BAF35708.1; -; Genomic_DNA.
DR EMBL; AB267179; BAF35709.1; -; Genomic_DNA.
DR EMBL; AB267180; BAF35710.1; -; Genomic_DNA.
DR EMBL; AB267181; BAF35711.1; -; Genomic_DNA.
DR EMBL; AB267182; BAF35712.1; -; Genomic_DNA.
DR EMBL; AB267183; BAF35713.1; -; Genomic_DNA.
DR EMBL; AB267184; BAF35714.1; -; Genomic_DNA.
DR EMBL; AB267185; BAF35715.1; -; Genomic_DNA.
DR EMBL; AB267186; BAF35716.1; -; Genomic_DNA.
DR EMBL; AB267187; BAF35717.1; -; Genomic_DNA.
DR EMBL; AB267188; BAF35718.1; -; Genomic_DNA.
DR EMBL; AB267189; BAF35719.1; -; Genomic_DNA.
DR EMBL; AB267190; BAF35720.1; -; Genomic_DNA.
DR EMBL; AB267191; BAF35721.1; -; Genomic_DNA.
DR EMBL; AB267192; BAF35722.1; -; Genomic_DNA.
DR EMBL; AB267193; BAF35723.1; -; Genomic_DNA.
DR EMBL; AB267194; BAF35724.1; -; Genomic_DNA.
DR EMBL; AB267195; BAF35725.1; -; Genomic_DNA.
DR EMBL; AB267196; BAF35726.1; -; Genomic_DNA.
DR EMBL; AB267197; BAF35727.1; -; Genomic_DNA.
DR EMBL; AB267198; BAF35728.1; -; Genomic_DNA.
DR EMBL; AB267199; BAF35729.1; -; Genomic_DNA.
DR EMBL; AB267200; BAF35730.1; -; Genomic_DNA.
DR EMBL; AB267201; BAF35731.1; -; Genomic_DNA.
DR EMBL; AB267202; BAF35732.1; -; Genomic_DNA.
DR EMBL; AB267203; BAF35733.1; -; Genomic_DNA.
DR EMBL; AB267204; BAF35734.1; -; Genomic_DNA.
DR EMBL; AB267205; BAF35735.1; -; Genomic_DNA.
DR EMBL; AB267206; BAF35736.1; -; Genomic_DNA.
DR EMBL; AB267207; BAF35737.1; -; Genomic_DNA.
DR EMBL; AB267208; BAF35738.1; -; Genomic_DNA.
DR EMBL; AB267209; BAF35739.1; -; Genomic_DNA.
DR EMBL; AB267210; BAF35740.1; -; Genomic_DNA.
DR EMBL; AB267211; BAF35741.1; -; Genomic_DNA.
DR EMBL; AB267212; BAF35742.1; -; Genomic_DNA.
DR EMBL; AB267213; BAF35743.1; -; Genomic_DNA.
DR EMBL; AB267214; BAF35744.1; -; Genomic_DNA.
DR EMBL; AB267215; BAF35745.1; -; Genomic_DNA.
DR EMBL; AB267216; BAF35746.1; -; Genomic_DNA.
DR PIR; I37432; SQHUAC.
DR RefSeq; NP_002643.1; NM_002652.2.
DR UniGene; Hs.99949; -.
DR PDB; 3ES6; X-ray; 3.23 A; B=29-146.
DR PDBsum; 3ES6; -.
DR ProteinModelPortal; P12273; -.
DR SMR; P12273; 29-146.
DR IntAct; P12273; 13.
DR STRING; 9606.ENSP00000291009; -.
DR PhosphoSite; P12273; -.
DR DMDM; 134170; -.
DR PaxDb; P12273; -.
DR PeptideAtlas; P12273; -.
DR PRIDE; P12273; -.
DR DNASU; 5304; -.
DR Ensembl; ENST00000291009; ENSP00000291009; ENSG00000159763.
DR GeneID; 5304; -.
DR KEGG; hsa:5304; -.
DR UCSC; uc003wcf.1; human.
DR CTD; 5304; -.
DR GeneCards; GC07P142829; -.
DR HGNC; HGNC:8993; PIP.
DR HPA; CAB002661; -.
DR HPA; HPA009177; -.
DR MIM; 176720; gene.
DR neXtProt; NX_P12273; -.
DR PharmGKB; PA33326; -.
DR eggNOG; NOG39870; -.
DR HOGENOM; HOG000253013; -.
DR HOVERGEN; HBG065978; -.
DR InParanoid; P12273; -.
DR OMA; RECMVIK; -.
DR OrthoDB; EOG72VH8B; -.
DR PhylomeDB; P12273; -.
DR EvolutionaryTrace; P12273; -.
DR GeneWiki; Prolactin-induced_protein; -.
DR GenomeRNAi; 5304; -.
DR NextBio; 20502; -.
DR PRO; PR:P12273; -.
DR Bgee; P12273; -.
DR CleanEx; HS_PIP; -.
DR Genevestigator; P12273; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0003779; F:actin binding; NAS:UniProtKB.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR007990; SV_autoAg.
DR PANTHER; PTHR15096; PTHR15096; 1.
DR Pfam; PF05326; SVA; 1.
DR PIRSF; PIRSF002572; PIP-GCDFP-15; 1.
DR ProDom; PD021604; SV_autoAg; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1 28
FT CHAIN 29 146 Prolactin-inducible protein.
FT /FTId=PRO_0000024288.
FT MOD_RES 29 29 Pyrrolidone carboxylic acid.
FT CARBOHYD 105 105 N-linked (GlcNAc...).
FT DISULFID 65 91
FT DISULFID 89 123
FT STRAND 44 46
FT STRAND 52 60
FT STRAND 66 76
FT HELIX 81 83
FT STRAND 85 90
FT STRAND 92 94
FT STRAND 96 102
FT STRAND 108 116
FT STRAND 120 123
FT HELIX 124 126
FT STRAND 136 145
SQ SEQUENCE 146 AA; 16572 MW; 93F3DA201133F03C CRC64;
MRLLQLLFRA SPATLLLVLC LQLGANKAQD NTRKIIIKNF DIPKSVRPND EVTAVLAVQT
ELKECMVVKT YLISSIPLQG AFNYKYTACL CDDNPKTFYW DFYTNRTVQI AAVVDVIREL
GICPDDAAVI PIKNNRFYTI EILKVE
//
ID PIP_HUMAN Reviewed; 146 AA.
AC P12273; A0A963; A0A9C3; A0A9F3; A4D2I1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1989, sequence version 1.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Prolactin-inducible protein;
DE AltName: Full=Gross cystic disease fluid protein 15;
DE Short=GCDFP-15;
DE AltName: Full=Prolactin-induced protein;
DE AltName: Full=Secretory actin-binding protein;
DE Short=SABP;
DE AltName: Full=gp17;
DE Flags: Precursor;
GN Name=PIP; Synonyms=GCDFP15, GPIP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3667631;
RA Murphy L.C., Tsuyuki D., Myal Y., Shiu R.P.C.;
RT "Isolation and sequencing of a cDNA clone for a prolactin-inducible
RT protein (PIP). Regulation of PIP gene expression in the human breast
RT cancer cell line, T-47D.";
RL J. Biol. Chem. 262:15236-15241(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1955075; DOI=10.1016/0303-7207(91)90153-J;
RA Myal Y., Iwasiow B., Tsuyuki D., Wong P., Shiu R.P.C.;
RT "The prolactin-inducible protein (PIP/GCDFP-15) gene: cloning,
RT structure and regulation.";
RL Mol. Cell. Endocrinol. 80:165-175(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seminal vesicle;
RX PubMed=9218538; DOI=10.1007/s002510050215;
RA Autiero M., Bouchier C., Basmaciogullari S., Zaborski P.,
RA el Marhomy S., Martin M., Guardiola J., Piatier-Tonneau D.;
RT "Isolation from a human seminal vesicle library of the cDNA for gp17,
RT a CD4 binding factor.";
RL Immunogenetics 46:345-348(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 29-146, DISULFIDE BONDS, AND GLYCOSYLATION AT
RP ASN-105.
RX PubMed=2013294; DOI=10.1111/j.1432-1033.1991.tb15873.x;
RA Schaller J., Akiyama K., Kimura H., Hess D., Affolter M., Rickli E.E.;
RT "Primary structure of a new actin-binding protein from human seminal
RT plasma.";
RL Eur. J. Biochem. 196:743-750(1991).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-146.
RX PubMed=16949771; DOI=10.1016/j.gene.2006.07.014;
RA Kitano T., Tian W., Umetsu K., Yuasa I., Yamazaki K., Saitou N.,
RA Osawa M.;
RT "Origin and evolution of gene for prolactin-induced protein.";
RL Gene 383:64-70(2006).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105, AND MASS
RP SPECTROMETRY.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
RA Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by
RT glycoprotein capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105, AND MASS
RP SPECTROMETRY.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 29-146 IN COMPLEX WITH AZGP1,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-105.
RX PubMed=18930737; DOI=10.1016/j.jmb.2008.09.072;
RA Hassan M.I., Bilgrami S., Kumar V., Singh N., Yadav S., Kaur P.,
RA Singh T.P.;
RT "Crystal structure of the novel complex formed between zinc alpha2-
RT glycoprotein (ZAG) and prolactin-inducible protein (PIP) from human
RT seminal plasma.";
RL J. Mol. Biol. 384:663-672(2008).
CC -!- SUBUNIT: Monomer. Interacts with AZGP1.
CC -!- INTERACTION:
CC Q9UHQ7:WBP5; NbExp=1; IntAct=EBI-1049746, EBI-1051372;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in pathological conditions of the
CC mammary gland and in several exocrine tissues, such as the
CC lacrimal, salivary, and sweat glands.
CC -!- INDUCTION: By prolactin and androgen; inhibited by estrogen.
CC -!- SIMILARITY: Belongs to the PIP family.
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DR EMBL; J03460; AAA60091.1; -; mRNA.
DR EMBL; X51501; CAA35870.1; -; Genomic_DNA.
DR EMBL; X51502; CAA35870.1; JOINED; Genomic_DNA.
DR EMBL; X51504; CAA35870.1; JOINED; Genomic_DNA.
DR EMBL; Y10179; CAA71252.1; -; mRNA.
DR EMBL; AK312227; BAG35160.1; -; mRNA.
DR EMBL; CH236959; EAL23781.1; -; Genomic_DNA.
DR EMBL; CH471198; EAW51887.1; -; Genomic_DNA.
DR EMBL; BC010950; AAH10950.1; -; mRNA.
DR EMBL; BC010951; AAH10951.1; -; mRNA.
DR EMBL; AB267097; BAF35627.1; -; Genomic_DNA.
DR EMBL; AB267098; BAF35628.1; -; Genomic_DNA.
DR EMBL; AB267099; BAF35629.1; -; Genomic_DNA.
DR EMBL; AB267100; BAF35630.1; -; Genomic_DNA.
DR EMBL; AB267101; BAF35631.1; -; Genomic_DNA.
DR EMBL; AB267102; BAF35632.1; -; Genomic_DNA.
DR EMBL; AB267103; BAF35633.1; -; Genomic_DNA.
DR EMBL; AB267104; BAF35634.1; -; Genomic_DNA.
DR EMBL; AB267105; BAF35635.1; -; Genomic_DNA.
DR EMBL; AB267106; BAF35636.1; -; Genomic_DNA.
DR EMBL; AB267107; BAF35637.1; -; Genomic_DNA.
DR EMBL; AB267108; BAF35638.1; -; Genomic_DNA.
DR EMBL; AB267109; BAF35639.1; -; Genomic_DNA.
DR EMBL; AB267110; BAF35640.1; -; Genomic_DNA.
DR EMBL; AB267111; BAF35641.1; -; Genomic_DNA.
DR EMBL; AB267112; BAF35642.1; -; Genomic_DNA.
DR EMBL; AB267113; BAF35643.1; -; Genomic_DNA.
DR EMBL; AB267114; BAF35644.1; -; Genomic_DNA.
DR EMBL; AB267115; BAF35645.1; -; Genomic_DNA.
DR EMBL; AB267116; BAF35646.1; -; Genomic_DNA.
DR EMBL; AB267117; BAF35647.1; -; Genomic_DNA.
DR EMBL; AB267118; BAF35648.1; -; Genomic_DNA.
DR EMBL; AB267119; BAF35649.1; -; Genomic_DNA.
DR EMBL; AB267120; BAF35650.1; -; Genomic_DNA.
DR EMBL; AB267121; BAF35651.1; -; Genomic_DNA.
DR EMBL; AB267122; BAF35652.1; -; Genomic_DNA.
DR EMBL; AB267123; BAF35653.1; -; Genomic_DNA.
DR EMBL; AB267124; BAF35654.1; -; Genomic_DNA.
DR EMBL; AB267125; BAF35655.1; -; Genomic_DNA.
DR EMBL; AB267126; BAF35656.1; -; Genomic_DNA.
DR EMBL; AB267127; BAF35657.1; -; Genomic_DNA.
DR EMBL; AB267128; BAF35658.1; -; Genomic_DNA.
DR EMBL; AB267129; BAF35659.1; -; Genomic_DNA.
DR EMBL; AB267130; BAF35660.1; -; Genomic_DNA.
DR EMBL; AB267131; BAF35661.1; -; Genomic_DNA.
DR EMBL; AB267132; BAF35662.1; -; Genomic_DNA.
DR EMBL; AB267133; BAF35663.1; -; Genomic_DNA.
DR EMBL; AB267134; BAF35664.1; -; Genomic_DNA.
DR EMBL; AB267135; BAF35665.1; -; Genomic_DNA.
DR EMBL; AB267136; BAF35666.1; -; Genomic_DNA.
DR EMBL; AB267137; BAF35667.1; -; Genomic_DNA.
DR EMBL; AB267138; BAF35668.1; -; Genomic_DNA.
DR EMBL; AB267139; BAF35669.1; -; Genomic_DNA.
DR EMBL; AB267140; BAF35670.1; -; Genomic_DNA.
DR EMBL; AB267141; BAF35671.1; -; Genomic_DNA.
DR EMBL; AB267142; BAF35672.1; -; Genomic_DNA.
DR EMBL; AB267143; BAF35673.1; -; Genomic_DNA.
DR EMBL; AB267144; BAF35674.1; -; Genomic_DNA.
DR EMBL; AB267145; BAF35675.1; -; Genomic_DNA.
DR EMBL; AB267146; BAF35676.1; -; Genomic_DNA.
DR EMBL; AB267147; BAF35677.1; -; Genomic_DNA.
DR EMBL; AB267148; BAF35678.1; -; Genomic_DNA.
DR EMBL; AB267149; BAF35679.1; -; Genomic_DNA.
DR EMBL; AB267150; BAF35680.1; -; Genomic_DNA.
DR EMBL; AB267151; BAF35681.1; -; Genomic_DNA.
DR EMBL; AB267152; BAF35682.1; -; Genomic_DNA.
DR EMBL; AB267153; BAF35683.1; -; Genomic_DNA.
DR EMBL; AB267154; BAF35684.1; -; Genomic_DNA.
DR EMBL; AB267155; BAF35685.1; -; Genomic_DNA.
DR EMBL; AB267156; BAF35686.1; -; Genomic_DNA.
DR EMBL; AB267157; BAF35687.1; -; Genomic_DNA.
DR EMBL; AB267158; BAF35688.1; -; Genomic_DNA.
DR EMBL; AB267159; BAF35689.1; -; Genomic_DNA.
DR EMBL; AB267160; BAF35690.1; -; Genomic_DNA.
DR EMBL; AB267161; BAF35691.1; -; Genomic_DNA.
DR EMBL; AB267162; BAF35692.1; -; Genomic_DNA.
DR EMBL; AB267163; BAF35693.1; -; Genomic_DNA.
DR EMBL; AB267164; BAF35694.1; -; Genomic_DNA.
DR EMBL; AB267165; BAF35695.1; -; Genomic_DNA.
DR EMBL; AB267166; BAF35696.1; -; Genomic_DNA.
DR EMBL; AB267167; BAF35697.1; -; Genomic_DNA.
DR EMBL; AB267168; BAF35698.1; -; Genomic_DNA.
DR EMBL; AB267169; BAF35699.1; -; Genomic_DNA.
DR EMBL; AB267170; BAF35700.1; -; Genomic_DNA.
DR EMBL; AB267171; BAF35701.1; -; Genomic_DNA.
DR EMBL; AB267172; BAF35702.1; -; Genomic_DNA.
DR EMBL; AB267173; BAF35703.1; -; Genomic_DNA.
DR EMBL; AB267174; BAF35704.1; -; Genomic_DNA.
DR EMBL; AB267175; BAF35705.1; -; Genomic_DNA.
DR EMBL; AB267176; BAF35706.1; -; Genomic_DNA.
DR EMBL; AB267177; BAF35707.1; -; Genomic_DNA.
DR EMBL; AB267178; BAF35708.1; -; Genomic_DNA.
DR EMBL; AB267179; BAF35709.1; -; Genomic_DNA.
DR EMBL; AB267180; BAF35710.1; -; Genomic_DNA.
DR EMBL; AB267181; BAF35711.1; -; Genomic_DNA.
DR EMBL; AB267182; BAF35712.1; -; Genomic_DNA.
DR EMBL; AB267183; BAF35713.1; -; Genomic_DNA.
DR EMBL; AB267184; BAF35714.1; -; Genomic_DNA.
DR EMBL; AB267185; BAF35715.1; -; Genomic_DNA.
DR EMBL; AB267186; BAF35716.1; -; Genomic_DNA.
DR EMBL; AB267187; BAF35717.1; -; Genomic_DNA.
DR EMBL; AB267188; BAF35718.1; -; Genomic_DNA.
DR EMBL; AB267189; BAF35719.1; -; Genomic_DNA.
DR EMBL; AB267190; BAF35720.1; -; Genomic_DNA.
DR EMBL; AB267191; BAF35721.1; -; Genomic_DNA.
DR EMBL; AB267192; BAF35722.1; -; Genomic_DNA.
DR EMBL; AB267193; BAF35723.1; -; Genomic_DNA.
DR EMBL; AB267194; BAF35724.1; -; Genomic_DNA.
DR EMBL; AB267195; BAF35725.1; -; Genomic_DNA.
DR EMBL; AB267196; BAF35726.1; -; Genomic_DNA.
DR EMBL; AB267197; BAF35727.1; -; Genomic_DNA.
DR EMBL; AB267198; BAF35728.1; -; Genomic_DNA.
DR EMBL; AB267199; BAF35729.1; -; Genomic_DNA.
DR EMBL; AB267200; BAF35730.1; -; Genomic_DNA.
DR EMBL; AB267201; BAF35731.1; -; Genomic_DNA.
DR EMBL; AB267202; BAF35732.1; -; Genomic_DNA.
DR EMBL; AB267203; BAF35733.1; -; Genomic_DNA.
DR EMBL; AB267204; BAF35734.1; -; Genomic_DNA.
DR EMBL; AB267205; BAF35735.1; -; Genomic_DNA.
DR EMBL; AB267206; BAF35736.1; -; Genomic_DNA.
DR EMBL; AB267207; BAF35737.1; -; Genomic_DNA.
DR EMBL; AB267208; BAF35738.1; -; Genomic_DNA.
DR EMBL; AB267209; BAF35739.1; -; Genomic_DNA.
DR EMBL; AB267210; BAF35740.1; -; Genomic_DNA.
DR EMBL; AB267211; BAF35741.1; -; Genomic_DNA.
DR EMBL; AB267212; BAF35742.1; -; Genomic_DNA.
DR EMBL; AB267213; BAF35743.1; -; Genomic_DNA.
DR EMBL; AB267214; BAF35744.1; -; Genomic_DNA.
DR EMBL; AB267215; BAF35745.1; -; Genomic_DNA.
DR EMBL; AB267216; BAF35746.1; -; Genomic_DNA.
DR PIR; I37432; SQHUAC.
DR RefSeq; NP_002643.1; NM_002652.2.
DR UniGene; Hs.99949; -.
DR PDB; 3ES6; X-ray; 3.23 A; B=29-146.
DR PDBsum; 3ES6; -.
DR ProteinModelPortal; P12273; -.
DR SMR; P12273; 29-146.
DR IntAct; P12273; 13.
DR STRING; 9606.ENSP00000291009; -.
DR PhosphoSite; P12273; -.
DR DMDM; 134170; -.
DR PaxDb; P12273; -.
DR PeptideAtlas; P12273; -.
DR PRIDE; P12273; -.
DR DNASU; 5304; -.
DR Ensembl; ENST00000291009; ENSP00000291009; ENSG00000159763.
DR GeneID; 5304; -.
DR KEGG; hsa:5304; -.
DR UCSC; uc003wcf.1; human.
DR CTD; 5304; -.
DR GeneCards; GC07P142829; -.
DR HGNC; HGNC:8993; PIP.
DR HPA; CAB002661; -.
DR HPA; HPA009177; -.
DR MIM; 176720; gene.
DR neXtProt; NX_P12273; -.
DR PharmGKB; PA33326; -.
DR eggNOG; NOG39870; -.
DR HOGENOM; HOG000253013; -.
DR HOVERGEN; HBG065978; -.
DR InParanoid; P12273; -.
DR OMA; RECMVIK; -.
DR OrthoDB; EOG72VH8B; -.
DR PhylomeDB; P12273; -.
DR EvolutionaryTrace; P12273; -.
DR GeneWiki; Prolactin-induced_protein; -.
DR GenomeRNAi; 5304; -.
DR NextBio; 20502; -.
DR PRO; PR:P12273; -.
DR Bgee; P12273; -.
DR CleanEx; HS_PIP; -.
DR Genevestigator; P12273; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0003779; F:actin binding; NAS:UniProtKB.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR007990; SV_autoAg.
DR PANTHER; PTHR15096; PTHR15096; 1.
DR Pfam; PF05326; SVA; 1.
DR PIRSF; PIRSF002572; PIP-GCDFP-15; 1.
DR ProDom; PD021604; SV_autoAg; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1 28
FT CHAIN 29 146 Prolactin-inducible protein.
FT /FTId=PRO_0000024288.
FT MOD_RES 29 29 Pyrrolidone carboxylic acid.
FT CARBOHYD 105 105 N-linked (GlcNAc...).
FT DISULFID 65 91
FT DISULFID 89 123
FT STRAND 44 46
FT STRAND 52 60
FT STRAND 66 76
FT HELIX 81 83
FT STRAND 85 90
FT STRAND 92 94
FT STRAND 96 102
FT STRAND 108 116
FT STRAND 120 123
FT HELIX 124 126
FT STRAND 136 145
SQ SEQUENCE 146 AA; 16572 MW; 93F3DA201133F03C CRC64;
MRLLQLLFRA SPATLLLVLC LQLGANKAQD NTRKIIIKNF DIPKSVRPND EVTAVLAVQT
ELKECMVVKT YLISSIPLQG AFNYKYTACL CDDNPKTFYW DFYTNRTVQI AAVVDVIREL
GICPDDAAVI PIKNNRFYTI EILKVE
//
MIM
176720
*RECORD*
*FIELD* NO
176720
*FIELD* TI
*176720 PROLACTIN-INDUCIBLE PROTEIN; PIP
;;GROSS CYSTIC DISEASE FLUID PROTEIN;;
GCDFP-15
read more*FIELD* TX
DESCRIPTION
The hormonally responsive prolactin-inducible protein (PIP) gene is
expressed in benign and malignant breast tumor tissues and in some
normal exocrine organs such as sweat, salivary, and lacrimal glands
(summary by Myal et al., 1991).
CLONING
Myal et al. (1991) reported the cloning and structure of the human PIP
gene and described potential mechanisms involved in its regulation by
hormones.
GENE STRUCTURE
Myal et al. (1991) found the entire PIP gene, 7 kb long, in a single
recombinant phage clone. The gene has 4 exons ranging from 106 bp to 223
bp in length.
MAPPING
Using DNA probes, Myal et al. (1989) mapped the PIP gene to 7q32-q36 by
a combination of Southern hybridization to DNA from human-hamster
somatic cell hybrids and in situ hybridization. Zelinski et al. (1991)
demonstrated that PIP is tightly linked to the Kell blood group locus
(110900); maximum lod = 9.12 at theta = 0.00.
CYTOGENETICS
Ciullo et al. (2002) showed that the region containing the PIP gene,
which is overexpressed in 80% of primary and metastatic breast cancers,
is duplicated in the breast carcinoma cell line T47D. The 2 copies are
organized as a large palindrome, lying 'in loco' on one chromosome 7.
The FRA7I fragile site lies 2 Mb telomeric to the PIP gene and sets the
distal end of the repeated sequence. Ciullo et al. (2002) proposed that
breakage at the FRA7I site was repaired by 1 cycle of the
breakage--fusion-bridge (BFB) cycle mechanism, resulting in
amplification of the PIP gene.
*FIELD* RF
1. Ciullo, M.; Debily, M.-A.; Rozier, L.; Autiero, M.; Billault, A.;
Mayau, V.; El Marhomy, S.; Guardiola, J.; Bernheim, A.; Coullin, P.;
Piatier-Tonneau, D.; Debatisse, M.: Initiation of the breakage--fusion-bridge
mechanism through common fragile site activation in human breast cancer
cells: the model of PIP gene duplication from a break at FRA7I. Hum.
Molec. Genet. 11: 2887-2894, 2002.
2. Myal, Y.; Gregory, C.; Wang, H.; Hamerton, J. L.; Shiu, R. P. C.
: The gene for prolactin-inducible protein (PIP), uniquely expressed
in exocrine organs, maps to chromosome 7. Somat. Cell Molec. Genet. 15:
265-270, 1989.
3. Myal, Y.; Robinson, D. B.; Iwasiow, B.; Tsuyuki, D.; Wong, P.;
Shiu, R. P. C.: The prolactin-inducible protein (PIP/GCDFP-15) gene:
cloning, structure and regulation. Molec. Cell. Endocr. 80: 165-175,
1991.
4. Zelinski, T.; Coghlan, G.; Myal, Y.; Shiu, R. P. C.; Philipps,
S.; White, L.; Lewis, M.: Genetic linkage between the Kell blood
group system and prolactin-inducible protein loci: provisional assignment
of KEL to chromosome 7. Ann. Hum. Genet. 55: 137-140, 1991.
*FIELD* CN
George E. Tiller - updated: 4/1/2004
*FIELD* CD
Victor A. McKusick: 7/11/1989
*FIELD* ED
alopez: 04/18/2011
tkritzer: 4/8/2004
terry: 4/1/2004
supermim: 3/16/1992
carol: 11/15/1991
carol: 9/12/1991
carol: 9/21/1990
supermim: 3/20/1990
ddp: 10/27/1989
*RECORD*
*FIELD* NO
176720
*FIELD* TI
*176720 PROLACTIN-INDUCIBLE PROTEIN; PIP
;;GROSS CYSTIC DISEASE FLUID PROTEIN;;
GCDFP-15
read more*FIELD* TX
DESCRIPTION
The hormonally responsive prolactin-inducible protein (PIP) gene is
expressed in benign and malignant breast tumor tissues and in some
normal exocrine organs such as sweat, salivary, and lacrimal glands
(summary by Myal et al., 1991).
CLONING
Myal et al. (1991) reported the cloning and structure of the human PIP
gene and described potential mechanisms involved in its regulation by
hormones.
GENE STRUCTURE
Myal et al. (1991) found the entire PIP gene, 7 kb long, in a single
recombinant phage clone. The gene has 4 exons ranging from 106 bp to 223
bp in length.
MAPPING
Using DNA probes, Myal et al. (1989) mapped the PIP gene to 7q32-q36 by
a combination of Southern hybridization to DNA from human-hamster
somatic cell hybrids and in situ hybridization. Zelinski et al. (1991)
demonstrated that PIP is tightly linked to the Kell blood group locus
(110900); maximum lod = 9.12 at theta = 0.00.
CYTOGENETICS
Ciullo et al. (2002) showed that the region containing the PIP gene,
which is overexpressed in 80% of primary and metastatic breast cancers,
is duplicated in the breast carcinoma cell line T47D. The 2 copies are
organized as a large palindrome, lying 'in loco' on one chromosome 7.
The FRA7I fragile site lies 2 Mb telomeric to the PIP gene and sets the
distal end of the repeated sequence. Ciullo et al. (2002) proposed that
breakage at the FRA7I site was repaired by 1 cycle of the
breakage--fusion-bridge (BFB) cycle mechanism, resulting in
amplification of the PIP gene.
*FIELD* RF
1. Ciullo, M.; Debily, M.-A.; Rozier, L.; Autiero, M.; Billault, A.;
Mayau, V.; El Marhomy, S.; Guardiola, J.; Bernheim, A.; Coullin, P.;
Piatier-Tonneau, D.; Debatisse, M.: Initiation of the breakage--fusion-bridge
mechanism through common fragile site activation in human breast cancer
cells: the model of PIP gene duplication from a break at FRA7I. Hum.
Molec. Genet. 11: 2887-2894, 2002.
2. Myal, Y.; Gregory, C.; Wang, H.; Hamerton, J. L.; Shiu, R. P. C.
: The gene for prolactin-inducible protein (PIP), uniquely expressed
in exocrine organs, maps to chromosome 7. Somat. Cell Molec. Genet. 15:
265-270, 1989.
3. Myal, Y.; Robinson, D. B.; Iwasiow, B.; Tsuyuki, D.; Wong, P.;
Shiu, R. P. C.: The prolactin-inducible protein (PIP/GCDFP-15) gene:
cloning, structure and regulation. Molec. Cell. Endocr. 80: 165-175,
1991.
4. Zelinski, T.; Coghlan, G.; Myal, Y.; Shiu, R. P. C.; Philipps,
S.; White, L.; Lewis, M.: Genetic linkage between the Kell blood
group system and prolactin-inducible protein loci: provisional assignment
of KEL to chromosome 7. Ann. Hum. Genet. 55: 137-140, 1991.
*FIELD* CN
George E. Tiller - updated: 4/1/2004
*FIELD* CD
Victor A. McKusick: 7/11/1989
*FIELD* ED
alopez: 04/18/2011
tkritzer: 4/8/2004
terry: 4/1/2004
supermim: 3/16/1992
carol: 11/15/1991
carol: 9/12/1991
carol: 9/21/1990
supermim: 3/20/1990
ddp: 10/27/1989