PIP_HUMAN
ID PIP_HUMAN Reviewed; 146 AA.
AC P12273; A0A963; A0A9C3; A0A9F3; A4D2I1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 199.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3667631; DOI=10.1016/s0021-9258(18)48164-1;
RA Murphy L.C., Tsuyuki D., Myal Y., Shiu R.P.C.;
RT "Isolation and sequencing of a cDNA clone for a prolactin-inducible protein
RT (PIP). Regulation of PIP gene expression in the human breast cancer cell
RT 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, structure
RT 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., el Marhomy S.,
RA Martin M., Guardiola J., Piatier-Tonneau D.;
RT "Isolation from a human seminal vesicle library of the cDNA for gp17, a CD4
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., 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., Mural R.J.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 29-146, PYROGLUTAMATE FORMATION AT GLN-29, DISULFIDE
RP BONDS, AND GLYCOSYLATION AT 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 PROTEIN SEQUENCE OF 29-55 AND 127-146, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND PYROGLUTAMATE FORMATION AT GLN-29.
RC TISSUE=Tear;
RX PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
RA Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
RA Suarez T., Elortza F.;
RT "Human basal tear peptidome characterization by CID, HCD, and ETD followed
RT by in silico and in vitro analyses for antimicrobial peptide
RT identification.";
RL J. Proteome Res. 14:2649-2658(2015).
RN [10]
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., Osawa M.;
RT "Origin and evolution of gene for prolactin-induced protein.";
RL Gene 383:64-70(2006).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105.
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 [13]
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 seminal
RT plasma.";
RL J. Mol. Biol. 384:663-672(2008).
CC -!- SUBUNIT: Monomer. Interacts with AZGP1. {ECO:0000269|PubMed:18930737}.
CC -!- INTERACTION:
CC P12273; P50570-2: DNM2; NbExp=3; IntAct=EBI-1049746, EBI-10968534;
CC P12273; O14656-2: TOR1A; NbExp=3; IntAct=EBI-1049746, EBI-25847109;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in pathological conditions of the mammary
CC gland and in several exocrine tissues, such as the lacrimal, salivary,
CC and sweat glands.
CC -!- INDUCTION: By prolactin and androgen; inhibited by estrogen.
CC -!- SIMILARITY: Belongs to the PIP family. {ECO:0000305}.
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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 CCDS; CCDS34768.1; -.
DR PIR; I37432; SQHUAC.
DR RefSeq; NP_002643.1; NM_002652.2.
DR PDB; 3ES6; X-ray; 3.23 A; B=29-146.
DR PDBsum; 3ES6; -.
DR AlphaFoldDB; P12273; -.
DR SMR; P12273; -.
DR BioGRID; 111321; 179.
DR CORUM; P12273; -.
DR IntAct; P12273; 28.
DR MINT; P12273; -.
DR STRING; 9606.ENSP00000291009; -.
DR GlyConnect; 1636; 67 N-Linked glycans (1 site).
DR GlyGen; P12273; 1 site, 67 N-linked glycans (1 site).
DR iPTMnet; P12273; -.
DR PhosphoSitePlus; P12273; -.
DR SwissPalm; P12273; -.
DR BioMuta; PIP; -.
DR DMDM; 134170; -.
DR EPD; P12273; -.
DR jPOST; P12273; -.
DR MassIVE; P12273; -.
DR MaxQB; P12273; -.
DR PaxDb; P12273; -.
DR PeptideAtlas; P12273; -.
DR PRIDE; P12273; -.
DR ProteomicsDB; 52845; -.
DR Antibodypedia; 2216; 631 antibodies from 41 providers.
DR DNASU; 5304; -.
DR Ensembl; ENST00000291009.4; ENSP00000291009.3; ENSG00000159763.4.
DR GeneID; 5304; -.
DR KEGG; hsa:5304; -.
DR MANE-Select; ENST00000291009.4; ENSP00000291009.3; NM_002652.3; NP_002643.1.
DR UCSC; uc003wcf.2; human.
DR CTD; 5304; -.
DR DisGeNET; 5304; -.
DR GeneCards; PIP; -.
DR HGNC; HGNC:8993; PIP.
DR HPA; ENSG00000159763; Tissue enriched (salivary).
DR MIM; 176720; gene.
DR neXtProt; NX_P12273; -.
DR OpenTargets; ENSG00000159763; -.
DR PharmGKB; PA33326; -.
DR VEuPathDB; HostDB:ENSG00000159763; -.
DR eggNOG; ENOG502T2PG; Eukaryota.
DR GeneTree; ENSGT00390000002099; -.
DR HOGENOM; CLU_148761_0_0_1; -.
DR InParanoid; P12273; -.
DR OMA; ECMVIKT; -.
DR OrthoDB; 1459895at2759; -.
DR PhylomeDB; P12273; -.
DR TreeFam; TF336919; -.
DR PathwayCommons; P12273; -.
DR Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
DR SignaLink; P12273; -.
DR BioGRID-ORCS; 5304; 12 hits in 1056 CRISPR screens.
DR ChiTaRS; PIP; human.
DR EvolutionaryTrace; P12273; -.
DR GeneWiki; Prolactin-induced_protein; -.
DR GenomeRNAi; 5304; -.
DR Pharos; P12273; Tbio.
DR PRO; PR:P12273; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P12273; protein.
DR Bgee; ENSG00000159763; Expressed in seminal vesicle and 121 other tissues.
DR Genevisible; P12273; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; NAS:UniProtKB.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0019864; F:IgG binding; IDA:UniProtKB.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IDA:UniProtKB.
DR GO; GO:0070233; P:negative regulation of T cell apoptotic process; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR007990; PIP.
DR PANTHER; PTHR15096; PTHR15096; 1.
DR Pfam; PF05326; SVA; 1.
DR PIRSF; PIRSF002572; PIP-GCDFP-15; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:2013294,
FT ECO:0000269|PubMed:25946035"
FT CHAIN 29..146
FT /note="Prolactin-inducible protein"
FT /evidence="ECO:0000269|PubMed:2013294"
FT /id="PRO_0000024288"
FT MOD_RES 29
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2013294,
FT ECO:0000269|PubMed:25946035"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:18930737,
FT ECO:0000269|PubMed:2013294"
FT DISULFID 65..91
FT /evidence="ECO:0000269|PubMed:2013294"
FT DISULFID 89..123
FT /evidence="ECO:0000269|PubMed:2013294"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3ES6"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:3ES6"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:3ES6"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3ES6"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:3ES6"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3ES6"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:3ES6"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:3ES6"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:3ES6"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3ES6"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:3ES6"
SQ SEQUENCE 146 AA; 16572 MW; 93F3DA201133F03C CRC64;
MRLLQLLFRA SPATLLLVLC LQLGANKAQD NTRKIIIKNF DIPKSVRPND EVTAVLAVQT
ELKECMVVKT YLISSIPLQG AFNYKYTACL CDDNPKTFYW DFYTNRTVQI AAVVDVIREL
GICPDDAAVI PIKNNRFYTI EILKVE
