PININ_HUMAN
ID PININ_HUMAN Reviewed; 717 AA.
AC Q9H307; B4DZX8; O60899; Q53EM7; Q6P5X4; Q7KYL1; Q99738; Q9UHZ9; Q9UQR9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 5.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Pinin;
DE AltName: Full=140 kDa nuclear and cell adhesion-related phosphoprotein;
DE AltName: Full=Desmosome-associated protein;
DE AltName: Full=Domain-rich serine protein;
DE Short=DRS protein;
DE Short=DRSP;
DE AltName: Full=Melanoma metastasis clone A protein;
DE AltName: Full=Nuclear protein SDK3;
DE AltName: Full=SR-like protein;
GN Name=PNN; Synonyms=DRS, MEMA;
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], PROTEIN SEQUENCE OF 44-50; 213-228 AND 537-553,
RP PUTATIVE FUNCTION IN EPITHELIA MAINTENANCE, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=8922384; DOI=10.1083/jcb.135.4.1027;
RA Ouyang P., Sugrue S.P.;
RT "Characterization of pinin, a novel protein associated with the desmosome-
RT intermediate filament complex.";
RL J. Cell Biol. 135:1027-1042(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PUTATIVE FUNCTION.
RX PubMed=10645008; DOI=10.1038/sj.onc.1203328;
RA Shi Y., Ouyang P., Sugrue S.P.;
RT "Characterization of the gene encoding pinin/DRS/memA and evidence for its
RT potential tumor suppressor function.";
RL Oncogene 19:289-297(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-671.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [6]
RP PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-717, VARIANT GLY-671, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Melanoma;
RX PubMed=10095061; DOI=10.1016/s0167-4781(99)00012-3;
RA Degen W.G.J., Agterbos M.A., Muyrers J.P.P., Bloemers H.P.J., Swart G.W.M.;
RT "memA/DRS, a putative mediator of multiprotein complexes, is overexpressed
RT in the metastasizing human melanoma cell lines BLM and MV3.";
RL Biochim. Biophys. Acta 1444:384-394(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-717, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Keratinocyte;
RX PubMed=9447706; DOI=10.1046/j.1432-0436.1997.6230119.x;
RA Brandner J., Reidenbach S., Franke W.W.;
RT "Evidence that 'pinin', reportedly a differentiation-specific desmosomal
RT protein, is actually a widespread nuclear protein.";
RL Differentiation 62:119-127(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 105-717.
RC TISSUE=Thymus;
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 [10]
RP SUBCELLULAR LOCATION.
RX PubMed=10486276; DOI=10.1006/bbrc.1999.1353;
RA Ouyang P.;
RT "Antibodies differentiate desmosome-form and nucleus-form pinin: evidence
RT that pinin is a moonlighting protein with dual location at the desmosome
RT and within the nucleus.";
RL Biochem. Biophys. Res. Commun. 263:192-200(1999).
RN [11]
RP INTERACTION WITH KRT8; KRT18 AND KRT19, AND MUTAGENESIS OF LEU-8 AND
RP LEU-19.
RX PubMed=10809736; DOI=10.1074/jbc.275.20.14910;
RA Shi J., Sugrue S.P.;
RT "Dissection of protein linkage between keratins and pinin, a protein with
RT dual location at desmosome-intermediate filament complex and in the
RT nucleus.";
RL J. Biol. Chem. 275:14910-14915(2000).
RN [12]
RP FUNCTION IN PRE-MRNA SPLICING, AND SUBCELLULAR LOCATION.
RX PubMed=12051732; DOI=10.1016/s0006-291x(02)00495-3;
RA Wang P., Lou P.-J., Leu S., Ouyang P.;
RT "Modulation of alternative pre-mRNA splicing in vivo by pinin.";
RL Biochem. Biophys. Res. Commun. 294:448-455(2002).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [14]
RP INTERACTION WITH PS1D/PNO40.
RX PubMed=12893261; DOI=10.1016/s0006-291x(03)01208-7;
RA Chang W.-L., Lee D.-C., Leu S., Huang Y.-M., Lu M.-C., Ouyang P.;
RT "Molecular characterization of a novel nucleolar protein, pNO40.";
RL Biochem. Biophys. Res. Commun. 307:569-577(2003).
RN [15]
RP IDENTIFICATION IN A COMPLEX WITH SR PROTEINS, INTERACTION WITH PNISR; SFRS4
RP AND SRRM2, AND SUBCELLULAR LOCATION.
RX PubMed=14578391; DOI=10.1167/iovs.03-0240;
RA Zimowska G., Shi J., Munguba G., Jackson M.R., Alpatov R., Simmons M.N.,
RA Shi Y., Sugrue S.P.;
RT "Pinin/DRS/memA interacts with SRp75, SRm300 and SRrp130 in corneal
RT epithelial cells.";
RL Invest. Ophthalmol. Vis. Sci. 44:4715-4723(2003).
RN [16]
RP FUNCTION IN PRE-MRNA SPLICING, IDENTIFICATION IN A MRNP COMPLEX WITH RNPS1,
RP INTERACTION WITH RNPS1, AND SUBCELLULAR LOCATION.
RX PubMed=14517304; DOI=10.1128/mcb.23.20.7363-7376.2003;
RA Li C., Lin R.-I., Lai M.-C., Ouyang P., Tarn W.-Y.;
RT "Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA
RT processing and export via interaction with RNPS1.";
RL Mol. Cell. Biol. 23:7363-7376(2003).
RN [17]
RP INTERACTION WITH PPIG, AND SUBCELLULAR LOCATION.
RX PubMed=15358154; DOI=10.1016/j.bbrc.2004.07.013;
RA Lin C.L., Leu S., Lu M.C., Ouyang P.;
RT "Over-expression of SR-cyclophilin, an interaction partner of nuclear
RT pinin, releases SR family splicing factors from nuclear speckles.";
RL Biochem. Biophys. Res. Commun. 321:638-647(2004).
RN [18]
RP INTERACTION WITH RNPS1.
RX PubMed=14729963; DOI=10.1128/mcb.24.3.1174-1187.2004;
RA Sakashita E., Tatsumi S., Werner D., Endo H., Mayeda A.;
RT "Human RNPS1 and its associated factors: a versatile alternative pre-mRNA
RT splicing regulator in vivo.";
RL Mol. Cell. Biol. 24:1174-1187(2004).
RN [19]
RP FUNCTION IN TRANSCRIPTIONAL ACTIVATION, DNA-BINDING, INTERACTION WITH CTBP1
RP AND CTBP2, AND MUTAGENESIS OF 502-PRO-GLU-503.
RX PubMed=15542832; DOI=10.1128/mcb.24.23.10223-10235.2004;
RA Alpatov R., Munguba G.C., Caton P., Joo J.H., Shi Y., Shi Y., Hunt M.E.,
RA Sugrue S.P.;
RT "Nuclear speckle-associated protein Pnn/DRS binds to the transcriptional
RT corepressor CtBP and relieves CtBP-mediated repression of the E-cadherin
RT gene.";
RL Mol. Cell. Biol. 24:10223-10235(2004).
RN [20]
RP FUNCTION IN CELL-CELL ADHESION, AND SUBCELLULAR LOCATION.
RX PubMed=15735603;
RA Joo J.-H., Alpatov R., Munguba G.C., Jackson M.R., Hunt M.E., Sugrue S.P.;
RT "Reduction of Pnn by RNAi induces loss of cell-cell adhesion between human
RT corneal epithelial cells.";
RL Mol. Vis. 11:133-142(2005).
RN [21]
RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16314458; DOI=10.1261/rna.2155905;
RA Tange T.O., Shibuya T., Jurica M.S., Moore M.J.;
RT "Biochemical analysis of the EJC reveals two new factors and a stable
RT tetrameric protein core.";
RL RNA 11:1869-1883(2005).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-347 AND SER-381, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-100; SER-375 AND
RP SER-552, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-238, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-96; SER-100; SER-114;
RP SER-115; THR-124; SER-347; SER-381; SER-450 AND SER-552, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-66; SER-100; SER-347;
RP SER-450; SER-658; SER-692 AND SER-695, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [32]
RP IDENTIFICATION IN THE PSAP COMPLEX, AND FUNCTION OF THE PSAP COMPLEX.
RX PubMed=22388736; DOI=10.1038/nsmb.2242;
RA Murachelli A.G., Ebert J., Basquin C., Le Hir H., Conti E.;
RT "The structure of the ASAP core complex reveals the existence of a Pinin-
RT containing PSAP complex.";
RL Nat. Struct. Mol. Biol. 19:378-386(2012).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-66; SER-100; SER-347;
RP SER-381; SER-450 AND SER-552, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-100 AND SER-347, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109 AND LYS-157, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [36]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-157, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [37]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-157, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-157; LYS-304; LYS-528
RP AND LYS-553, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [39]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-121; LYS-137; LYS-155;
RP LYS-157; LYS-228; LYS-280; LYS-304; LYS-311; LYS-359; LYS-365; LYS-528;
RP LYS-536 AND LYS-553, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Transcriptional activator binding to the E-box 1 core
CC sequence of the E-cadherin promoter gene; the core-binding sequence is
CC 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription
CC repression. Auxiliary component of the splicing-dependent multiprotein
CC exon junction complex (EJC) deposited at splice junction on mRNAs. The
CC EJC is a dynamic structure consisting of core proteins and several
CC peripheral nuclear and cytoplasmic associated factors that join the
CC complex only transiently either during EJC assembly or during
CC subsequent mRNA metabolism. Participates in the regulation of
CC alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt
CC upstream of the 5'-splice sites. Component of the PSAP complex which
CC binds RNA in a sequence-independent manner and is proposed to be
CC recruited to the EJC prior to or during the splicing process and to
CC regulate specific excision of introns in specific transcription
CC subsets. Involved in the establishment and maintenance of epithelia
CC cell-cell adhesion. Potential tumor suppressor for renal cell
CC carcinoma. {ECO:0000269|PubMed:12051732, ECO:0000269|PubMed:14517304,
CC ECO:0000269|PubMed:15542832, ECO:0000269|PubMed:15735603,
CC ECO:0000269|PubMed:22388736}.
CC -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex
CC (EJC). Found in a complex with SR proteins. Found in a mRNP complex
CC with RNPS1. Component of the PSAP complex consisting of RNPS1, SAP18
CC and PNN. Interacts with PNISR, CTBP1, CTBP2, KRT8, KRT18, KRT19,
CC PS1D/PNO40, PPIG, RNPS1, SFRS4 and SRRM2. Identified in the spliceosome
CC C complex. {ECO:0000269|PubMed:10809736, ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:12893261, ECO:0000269|PubMed:14517304,
CC ECO:0000269|PubMed:14578391, ECO:0000269|PubMed:14729963,
CC ECO:0000269|PubMed:15358154, ECO:0000269|PubMed:15542832,
CC ECO:0000269|PubMed:16314458, ECO:0000269|PubMed:22388736}.
CC -!- INTERACTION:
CC Q9H307; Q9UKV3: ACIN1; NbExp=2; IntAct=EBI-681904, EBI-396258;
CC Q9H307; P68400: CSNK2A1; NbExp=2; IntAct=EBI-681904, EBI-347804;
CC Q9H307; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-681904, EBI-3044087;
CC Q9H307; Q15287-1: RNPS1; NbExp=3; IntAct=EBI-681904, EBI-15972541;
CC Q9H307; O00422: SAP18; NbExp=2; IntAct=EBI-681904, EBI-1044156;
CC Q9H307; Q13573: SNW1; NbExp=3; IntAct=EBI-681904, EBI-632715;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle. Cell junction, desmosome.
CC Note=Cell-cell contact area, predominantly desmosome of intercellular
CC adherens junction. Not a nucleocytoplasmic shuttling protein.
CC -!- TISSUE SPECIFICITY: Expressed in placenta, lung, liver, kidney,
CC pancreas, spleen, thymus, prostate, testis, ovary, small intestine,
CC colon, heart, epidermis, esophagus, brain and smooth and skeletal
CC muscle. Expressed strongly in melanoma metastasis lesions and advanced
CC primary tumors. {ECO:0000269|PubMed:10095061,
CC ECO:0000269|PubMed:8922384, ECO:0000269|PubMed:9447706}.
CC -!- SIMILARITY: Belongs to the pinin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA70874.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U77718; AAB48304.1; -; mRNA.
DR EMBL; AF195139; AAG33941.1; -; Genomic_DNA.
DR EMBL; AF112222; AAF17209.1; -; mRNA.
DR EMBL; AK223612; BAD97332.1; -; mRNA.
DR EMBL; BC062602; AAH62602.1; -; mRNA.
DR EMBL; Y09703; CAA70874.1; ALT_FRAME; mRNA.
DR EMBL; Y10351; CAA71377.1; -; mRNA.
DR EMBL; AK303136; BAG64240.1; -; mRNA.
DR CCDS; CCDS9671.1; -.
DR RefSeq; NP_002678.2; NM_002687.3.
DR AlphaFoldDB; Q9H307; -.
DR SMR; Q9H307; -.
DR BioGRID; 111412; 231.
DR CORUM; Q9H307; -.
DR DIP; DIP-32950N; -.
DR IntAct; Q9H307; 118.
DR MINT; Q9H307; -.
DR STRING; 9606.ENSP00000216832; -.
DR MoonProt; Q9H307; -.
DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR GlyGen; Q9H307; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H307; -.
DR MetOSite; Q9H307; -.
DR PhosphoSitePlus; Q9H307; -.
DR SwissPalm; Q9H307; -.
DR BioMuta; PNN; -.
DR DMDM; 73921750; -.
DR EPD; Q9H307; -.
DR jPOST; Q9H307; -.
DR MassIVE; Q9H307; -.
DR MaxQB; Q9H307; -.
DR PaxDb; Q9H307; -.
DR PeptideAtlas; Q9H307; -.
DR PRIDE; Q9H307; -.
DR Antibodypedia; 55; 276 antibodies from 32 providers.
DR DNASU; 5411; -.
DR Ensembl; ENST00000216832.9; ENSP00000216832.4; ENSG00000100941.9.
DR GeneID; 5411; -.
DR KEGG; hsa:5411; -.
DR MANE-Select; ENST00000216832.9; ENSP00000216832.4; NM_002687.4; NP_002678.3.
DR UCSC; uc001wuw.5; human.
DR CTD; 5411; -.
DR DisGeNET; 5411; -.
DR GeneCards; PNN; -.
DR HGNC; HGNC:9162; PNN.
DR HPA; ENSG00000100941; Low tissue specificity.
DR MIM; 603154; gene.
DR neXtProt; NX_Q9H307; -.
DR OpenTargets; ENSG00000100941; -.
DR PharmGKB; PA33484; -.
DR VEuPathDB; HostDB:ENSG00000100941; -.
DR eggNOG; KOG3756; Eukaryota.
DR GeneTree; ENSGT00730000111160; -.
DR HOGENOM; CLU_025370_0_0_1; -.
DR InParanoid; Q9H307; -.
DR OMA; PERKDFP; -.
DR OrthoDB; 881609at2759; -.
DR PhylomeDB; Q9H307; -.
DR TreeFam; TF331859; -.
DR PathwayCommons; Q9H307; -.
DR SignaLink; Q9H307; -.
DR BioGRID-ORCS; 5411; 652 hits in 1083 CRISPR screens.
DR ChiTaRS; PNN; human.
DR GeneWiki; Pinin; -.
DR GenomeRNAi; 5411; -.
DR Pharos; Q9H307; Tbio.
DR PRO; PR:Q9H307; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9H307; protein.
DR Bgee; ENSG00000100941; Expressed in tendon of biceps brachii and 208 other tissues.
DR ExpressionAtlas; Q9H307; baseline and differential.
DR Genevisible; Q9H307; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005882; C:intermediate filament; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR InterPro; IPR039853; Pinin.
DR InterPro; IPR006786; Pinin_SDK_MemA.
DR InterPro; IPR006787; Pinin_SDK_N.
DR PANTHER; PTHR12707; PTHR12707; 1.
DR Pfam; PF04696; Pinin_SDK_memA; 1.
DR Pfam; PF04697; Pinin_SDK_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cell junction; Coiled coil;
KW Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome; Transcription; Transcription regulation;
KW Tumor suppressor; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330"
FT CHAIN 2..717
FT /note="Pinin"
FT /id="PRO_0000190242"
FT REGION 2..284
FT /note="Necessary for interaction with RNPS1"
FT REGION 2..167
FT /note="Necessary for mediating alternative 5' splicing"
FT REGION 2..98
FT /note="Necessary for interactions with KRT8, KRT18 and
FT KRT19"
FT REGION 46..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..284
FT /note="Sufficient for PSAP complex assembly"
FT REGION 279..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..717
FT /note="Necessary for interaction with PPIG"
FT /evidence="ECO:0000269|PubMed:15358154"
FT COILED 2..32
FT /evidence="ECO:0000255"
FT COILED 163..234
FT /evidence="ECO:0000255"
FT COILED 287..379
FT /evidence="ECO:0000255"
FT COILED 446..467
FT /evidence="ECO:0000255"
FT COMPBIAS 82..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..572
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..652
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 54
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35691"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 238
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 238
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O35691"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35691"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 155
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 311
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 359
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 365
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 528
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 536
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 553
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VARIANT 671
FT /note="S -> G (in dbSNP:rs13021)"
FT /evidence="ECO:0000269|PubMed:10095061, ECO:0000269|Ref.4"
FT /id="VAR_023368"
FT MUTAGEN 8
FT /note="L->P: Abolishes interaction with KRT18."
FT /evidence="ECO:0000269|PubMed:10809736"
FT MUTAGEN 19
FT /note="L->P: Abolishes interaction with KRT18."
FT /evidence="ECO:0000269|PubMed:10809736"
FT MUTAGEN 502..503
FT /note="PE->AA: Abolishes interaction with CTBP1 and shows
FT moderate relief of CTBP1-mediated repression."
FT /evidence="ECO:0000269|PubMed:15542832"
FT CONFLICT 69
FT /note="Missing (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="K -> N (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="E -> D (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="Q -> H (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="E -> V (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="A -> G (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 402..403
FT /note="DQ -> EE (in Ref. 2; AAG33941)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="T -> S (in Ref. 9; BAG64240 and 7; CAA70874)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="E -> D (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="P -> A (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 491..492
FT /note="QP -> EPQPQLQPEPAQPQLQSQPQLQLQSQCHA (in Ref. 1; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="Q -> H (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="Q -> H (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="L -> F (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="P -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="E -> D (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="T -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="P -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="E -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 553..557
FT /note="KSKTK -> ESETN (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="A -> T (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 569..571
FT /note="KTS -> RTT (in Ref. 1; AAB48304)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="S -> G (in Ref. 3; AAF17209 and 8; CAA71377)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="S -> SST (in Ref. 7; CAA70874)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="H -> P (in Ref. 2; AAG33941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 717 AA; 81628 MW; 1F24D3F12E053C8F CRC64;
MAVAVRTLQE QLEKAKESLK NVDENIRKLT GRDPNDVRPI QARLLALSGP GGGRGRGSLL
LRRGFSDSGG GPPAKQRDLE GAVSRLGGER RTRRESRQES DPEDDDVKKP ALQSSVVATS
KERTRRDLIQ DQNMDEKGKQ RNRRIFGLLM GTLQKFKQES TVATERQKRR QEIEQKLEVQ
AEEERKQVEN ERRELFEERR AKQTELRLLE QKVELAQLQE EWNEHNAKII KYIRTKTKPH
LFYIPGRMCP ATQKLIEESQ RKMNALFEGR RIEFAEQINK MEARPRRQSM KEKEHQVVRN
EEQKAEQEEG KVAQREEELE ETGNQHNDVE IEEAGEEEEK EIAIVHSDAE KEQEEEEQKQ
EMEVKMEEET EVRESEKQQD SQPEEVMDVL EMVENVKHVI ADQEVMETNR VESVEPSENE
ASKELEPEME FEIEPDKECK TLSPGKENVS ALDMEKESEE KEEKESEPQP EPVAQPQPQS
QPQLQLQSQS QPVLQSQPPS QPEDLSLAVL QPTPQVTQEQ GHLLPERKDF PVESVKLTEV
PVEPVLTVHP ESKSKTKTRS RSRGRARNKT SKSRSRSSSS SSSSSSSTSS SSGSSSSSGS
SSSRSSSSSS SSTSGSSSRD SSSSTSSSSE SRSRSRGRGH NRDRKHRRSV DRKRRDTSGL
ERSHKSSKGG SSRDTKGSKD KNSRSDRKRS ISESSRSGKR SSRSERDRKS DRKDKRR
