ID   GANP_HUMAN              Reviewed;        1980 AA.
AC   O60318; C9JL56; Q2M3C1; Q6PJP6; Q9BSY5; Q9UMT4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Germinal-center associated nuclear protein;
DE            Short=GANP;
DE            EC=2.3.1.48 {ECO:0000269|PubMed:23652018};
DE   AltName: Full=80 kDa MCM3-associated protein;
DE   AltName: Full=MCM3 acetylating protein;
DE            Short=MCM3AP;
DE            EC=2.3.1.-;
DE   AltName: Full=MCM3 acetyltransferase;
GN   Name=MCM3AP; Synonyms=GANP, KIAA0572, MAP80;
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], AND TISSUE SPECIFICITY.
RX   PubMed=11024281; DOI=10.1016/s0378-1119(00)00336-x;
RA   Abe E., Kuwahara K., Yoshida M., Suzuki M., Terasaki H., Matsuo Y.,
RA   Takahashi E., Sakaguchi N.;
RT   "Structure, expression, and chromosomal localization of the human gene
RT   encoding a germinal center-associated nuclear protein (GANP) that
RT   associates with MCM3 involved in the initiation of DNA replication.";
RL   Gene 255:219-227(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-102; VAL-288; LEU-333;
RP   LEU-413; LEU-1051; MET-1062; TRP-1314; GLU-1449; ILE-1576; THR-1795;
RP   ARG-1870 AND VAL-1941.
RG   NIEHS SNPs program;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-102.
RC   TISSUE=Brain;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-1980.
RC   TISSUE=Brain;
RX   PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA   Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA   Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. IX. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:31-39(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1260-1980, AND INTERACTION WITH MCM3.
RX   PubMed=9712829; DOI=10.1074/jbc.273.35.22177;
RA   Takei Y., Tsujimoto G.;
RT   "Identification of a novel MCM3-associated protein that facilitates MCM3
RT   nuclear localization.";
RL   J. Biol. Chem. 273:22177-22180(1998).
RN   [7]
RP   FUNCTION (ISOFORM MCM3AP), INTERACTION WITH MCM3, AND MUTAGENESIS OF
RP   1730-HIS--GLY-1733.
RX   PubMed=11258703; DOI=10.1093/embo-reports/kve026;
RA   Takei Y., Swietlik M., Tanoue A., Tsujimoto G., Kouzarides T., Laskey R.;
RT   "MCM3AP, a novel acetyltransferase that acetylates replication protein
RT   MCM3.";
RL   EMBO Rep. 2:119-123(2001).
RN   [8]
RP   FUNCTION (ISOFORM MCM3AP), INTERACTION WITH MCM3, SUBCELLULAR LOCATION
RP   (ISOFORM MCM3AP), AND MUTAGENESIS OF 1496-LEU--LEU-1501 AND
RP   1730-HIS--GLY-1733.
RX   PubMed=12226073; DOI=10.1074/jbc.c200442200;
RA   Takei Y., Assenberg M., Tsujimoto G., Laskey R.;
RT   "The MCM3 acetylase MCM3AP inhibits initiation, but not elongation, of DNA
RT   replication via interaction with MCM3.";
RL   J. Biol. Chem. 277:43121-43125(2002).
RN   [9]
RP   INTERACTION WITH NR3C1.
RX   PubMed=16914116; DOI=10.1016/j.bbrc.2006.07.182;
RA   Osman W., Laine S., Zilliacus J.;
RT   "Functional interaction between the glucocorticoid receptor and
RT   GANP/MCM3AP.";
RL   Biochem. Biophys. Res. Commun. 348:1239-1244(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, AND IDENTIFICATION BY
RP   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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, 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   [13]
RP   FUNCTION (ISOFORM GANP), SUBCELLULAR LOCATION, FG-REPEATS, AND INTERACTION
RP   WITH NUP153; NXF1 AND RANBP2.
RX   PubMed=20005110; DOI=10.1016/j.cub.2009.10.078;
RA   Wickramasinghe V.O., McMurtrie P.I., Mills A.D., Takei Y., Penrhyn-Lowe S.,
RA   Amagase Y., Main S., Marr J., Stewart M., Laskey R.A.;
RT   "mRNA export from mammalian cell nuclei is dependent on GANP.";
RL   Curr. Biol. 20:25-31(2010).
RN   [14]
RP   FUNCTION (ISOFORM GANP).
RX   PubMed=20384790; DOI=10.1111/j.1365-2443.2010.01396.x;
RA   Okamoto N., Kuwahara K., Ohta K., Kitabatake M., Takagi K., Mizuta H.,
RA   Kondo E., Sakaguchi N.;
RT   "Germinal center-associated nuclear protein (GANP) is involved in mRNA
RT   export of Shugoshin-1 required for centromere cohesion and in sister-
RT   chromatid exchange.";
RL   Genes Cells 15:471-484(2010).
RN   [15]
RP   INTERACTION WITH AICDA.
RX   PubMed=20507984; DOI=10.1074/jbc.m110.131441;
RA   Maeda K., Singh S.K., Eda K., Kitabatake M., Pham P., Goodman M.F.,
RA   Sakaguchi N.;
RT   "GANP-mediated recruitment of activation-induced cytidine deaminase to cell
RT   nuclei and to immunoglobulin variable region DNA.";
RL   J. Biol. Chem. 285:23945-23953(2010).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, AND IDENTIFICATION BY
RP   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   [17]
RP   ALTERNATIVE PROMOTER USAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=21195085; DOI=10.1016/j.jmb.2010.12.035;
RA   Wickramasinghe V.O., McMurtrie P.I., Marr J., Amagase Y., Main S.,
RA   Mills A.D., Laskey R.A., Takei Y.;
RT   "MCM3AP is transcribed from a promoter within an intron of the overlapping
RT   gene for GANP.";
RL   J. Mol. Biol. 406:355-361(2011).
RN   [18]
RP   IDENTIFICATION BY MASS 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   [19]
RP   FUNCTION (ISOFORM GANP), IDENTIFICATION IN THE TREX-2 COMPLEX, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=23591820; DOI=10.1242/jcs.118000;
RA   Umlauf D., Bonnet J., Waharte F., Fournier M., Stierle M., Fischer B.,
RA   Brino L., Devys D., Tora L.;
RT   "The human TREX-2 complex is stably associated with the nuclear pore
RT   basket.";
RL   J. Cell Sci. 126:2656-2667(2013).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-538 AND SER-557, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [21]
RP   FUNCTION, INTERACTION WITH DDX21; DDX39A; DHX9; NUP62; NUP153; POLR2A;
RP   SUPT5H AND TOP2A, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX   PubMed=23652018; DOI=10.1038/ncomms2823;
RA   Singh S.K., Maeda K., Eid M.M., Almofty S.A., Ono M., Pham P.,
RA   Goodman M.F., Sakaguchi N.;
RT   "GANP regulates recruitment of AID to immunoglobulin variable regions by
RT   modulating transcription and nucleosome occupancy.";
RL   Nat. Commun. 4:1830-1830(2013).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1163-1235 IN COMPLEX WITH ENY2,
RP   FUNCTION (ISOFORM GANP), IDENTIFICATION IN THE TREX-2 COMPLEX, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=22307388; DOI=10.1093/nar/gks059;
RA   Jani D., Lutz S., Hurt E., Laskey R.A., Stewart M., Wickramasinghe V.O.;
RT   "Functional and structural characterization of the mammalian TREX-2 complex
RT   that links transcription with nuclear messenger RNA export.";
RL   Nucleic Acids Res. 40:4562-4573(2012).
RN   [23]
RP   VARIANTS [LARGE SCALE ANALYSIS] VAL-409 AND ILE-1576.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [24]
RP   INVOLVEMENT IN PNRIID, AND VARIANT PNRIID LYS-915.
RX   PubMed=24123876; DOI=10.1136/jmedgenet-2013-101644;
RA   Schuurs-Hoeijmakers J.H., Vulto-van Silfhout A.T., Vissers L.E.,
RA   van de Vondervoort I.I., van Bon B.W., de Ligt J., Gilissen C.,
RA   Hehir-Kwa J.Y., Neveling K., del Rosario M., Hira G., Reitano S.,
RA   Vitello A., Failla P., Greco D., Fichera M., Galesi O., Kleefstra T.,
RA   Greally M.T., Ockeloen C.W., Willemsen M.H., Bongers E.M., Janssen I.M.,
RA   Pfundt R., Veltman J.A., Romano C., Willemsen M.A., van Bokhoven H.,
RA   Brunner H.G., de Vries B.B., de Brouwer A.P.;
RT   "Identification of pathogenic gene variants in small families with
RT   intellectually disabled siblings by exome sequencing.";
RL   J. Med. Genet. 50:802-811(2013).
RN   [25]
RP   INVOLVEMENT IN PNRIID, VARIANTS PNRIID THR-762; ASP-867; 889-TYR--ILE-1980
RP   DEL; MET-1272; 1478-SER--ILE-1980 DEL AND LYS-1577, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=28633435; DOI=10.1093/brain/awx138;
RA   Ylikallio E., Woldegebriel R., Tumiati M., Isohanni P., Ryan M.M.,
RA   Stark Z., Walsh M., Sawyer S.L., Bell K.M., Oshlack A., Lockhart P.J.,
RA   Shcherbii M., Estrada-Cuzcano A., Atkinson D., Hartley T., Tetreault M.,
RA   Cuppen I., van der Pol W.L., Candayan A., Battaloglu E., Parman Y.,
RA   van Gassen K.L.I., van den Boogaard M.H., Boycott K.M., Kauppi L.,
RA   Jordanova A., Loennqvist T., Tyynismaa H.;
RT   "MCM3AP in recessive Charcot-Marie-Tooth neuropathy and mild intellectual
RT   disability.";
RL   Brain 140:2093-2103(2017).
RN   [26]
RP   INVOLVEMENT IN PNRIID, AND VARIANTS PNRIID HIS-878; PRO-951 AND
RP   1804-GLN--ILE-1980 DEL.
RX   PubMed=28969388; DOI=10.1093/brain/awx222;
RA   Karakaya M., Mazaheri N., Polat I., Bharucha-Goebel D., Donkervoort S.,
RA   Maroofian R., Shariati G., Hoelker I., Monaghan K., Winchester S., Zori R.,
RA   Galehdari H., Boennemann C.G., Yis U., Wirth B.;
RT   "Biallelic MCM3AP mutations cause Charcot-Marie-Tooth neuropathy with
RT   variable clinical presentation.";
RL   Brain 140:E65-E65(2017).
RN   [27]
RP   INVOLVEMENT IN PNRIID, AND VARIANT PNRIID SER-870.
RX   PubMed=29982295; DOI=10.1093/brain/awy184;
RA   Kennerson M.L., Corbett A.C., Ellis M., Perez-Siles G., Nicholson G.A.;
RT   "A novel MCM3AP mutation in a Lebanese family with recessive Charcot-Marie-
RT   Tooth neuropathy.";
RL   Brain 141:E66-E66(2018).
CC   -!- FUNCTION: [Isoform GANP]: As a component of the TREX-2 complex,
CC       involved in the export of mRNAs to the cytoplasm through the nuclear
CC       pores (PubMed:20005110, PubMed:20384790, PubMed:23591820,
CC       PubMed:22307388). Through the acetylation of histones, affects the
CC       assembly of nucleosomes at immunoglobulin variable region genes and
CC       promotes the recruitment and positioning of transcription complex to
CC       favor DNA cytosine deaminase AICDA/AID targeting, hence promoting
CC       somatic hypermutations (PubMed:23652018). {ECO:0000269|PubMed:20005110,
CC       ECO:0000269|PubMed:20384790, ECO:0000269|PubMed:22307388,
CC       ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:23652018}.
CC   -!- FUNCTION: [Isoform MCM3AP]: Binds to and acetylates the replication
CC       protein MCM3. Plays a role in the initiation of DNA replication and
CC       participates in controls that ensure that DNA replication initiates
CC       only once per cell cycle (PubMed:11258703, PubMed:12226073). Through
CC       the acetylation of histones, affects the assembly of nucleosomes at
CC       immunoglobulin variable region genes and promotes the recruitment and
CC       positioning of transcription complex to favor DNA cytosine deaminase
CC       AICDA/AID targeting, hence promoting somatic hypermutations
CC       (PubMed:23652018). {ECO:0000269|PubMed:11258703,
CC       ECO:0000269|PubMed:12226073, ECO:0000269|PubMed:23652018}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC         Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000269|PubMed:23652018};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC         Evidence={ECO:0000269|PubMed:23652018};
CC   -!- SUBUNIT: Isoform GANP: Component of the nuclear pore complex (NPC)-
CC       associated TREX-2 complex (transcription and export complex 2),
CC       composed of at least GANP, 2 copies of ENY2, PCID2, SEM1/DSS1, and
CC       either centrin CETN2 or centrin CETN3. The TREX-2 complex also
CC       associates with ALYREF/ALY (PubMed:23591820, PubMed:22307388).
CC       Interacts with RNA polymerase II subunit POLR2A and with the
CC       transcription elongation factor SUPT5H/SPT5 (PubMed:23652018,
CC       PubMed:22307388). Interacts (via FG-repeats) with NXF1; this
CC       interaction is not mediated by RNA (PubMed:20005110). Isoform GANP
CC       interacts with nuclear envelope proteins NUP62, NUP153 and
CC       RANBP2/NUP358; interaction with NUP153 is required for full
CC       localization at the nuclear pore complex (PubMed:20005110,
CC       PubMed:23652018). Interacts with several RNA helicases, including DHX9,
CC       DDX21, and DDX39A/DDX39, and with DNA topoisomerase TOP2A
CC       (PubMed:23652018). Directly interacts with AICDA/AID (PubMed:20507984).
CC       Interacts with the glucocorticoid receptor NR3C1 (PubMed:16914116).
CC       Isoform MCM3AP: Interacts with the glucocorticoid receptor NR3C1
CC       (PubMed:16914116). Interacts with MCM3; this interaction leads to MCM3
CC       acetylation (PubMed:9712829, PubMed:11258703, PubMed:12226073).
CC       {ECO:0000269|PubMed:11258703, ECO:0000269|PubMed:12226073,
CC       ECO:0000269|PubMed:16914116, ECO:0000269|PubMed:20005110,
CC       ECO:0000269|PubMed:20507984, ECO:0000269|PubMed:22307388,
CC       ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:23652018,
CC       ECO:0000269|PubMed:9712829}.
CC   -!- SUBCELLULAR LOCATION: [Isoform GANP]: Nucleus envelope
CC       {ECO:0000269|PubMed:20005110, ECO:0000269|PubMed:21195085,
CC       ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820,
CC       ECO:0000269|PubMed:28633435}. Nucleus, nuclear pore complex
CC       {ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820}. Nucleus,
CC       nucleoplasm {ECO:0000269|PubMed:20005110}. Chromosome
CC       {ECO:0000269|PubMed:23652018}. Note=Predominantly located at the
CC       nuclear envelope, facing the nucleus interior (PubMed:20005110,
CC       PubMed:21195085, PubMed:23591820). Localization at the nuclear pore
CC       complex requires NUP153, TPR and ALYREF/ALY (PubMed:23591820,
CC       PubMed:22307388). Also found associated with chromatin
CC       (PubMed:23652018). In B-cells, targeted to the immunoglobulin variable
CC       region genes (PubMed:23652018). {ECO:0000269|PubMed:20005110,
CC       ECO:0000269|PubMed:21195085, ECO:0000269|PubMed:22307388,
CC       ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:23652018}.
CC   -!- SUBCELLULAR LOCATION: [Isoform MCM3AP]: Cytoplasm
CC       {ECO:0000269|PubMed:12226073, ECO:0000269|PubMed:21195085}. Nucleus
CC       {ECO:0000269|PubMed:12226073, ECO:0000269|PubMed:21195085}.
CC       Note=Translocates into the nucleus in the presence of MCM3
CC       (PubMed:12226073). Associates with chromatin possibly through
CC       interaction with MCM3 (PubMed:12226073). {ECO:0000269|PubMed:12226073}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=GANP;
CC         IsoId=O60318-1; Sequence=Displayed;
CC       Name=MCM3AP; Synonyms=80 kDa MCM3-associated protein;
CC         IsoId=O60318-2; Sequence=VSP_053438;
CC   -!- TISSUE SPECIFICITY: Widely expressed (PubMed:11024281). Up-regulated in
CC       germinal center B-cells in tonsils (at protein level)
CC       (PubMed:11024281). {ECO:0000269|PubMed:11024281}.
CC   -!- DISEASE: Peripheral neuropathy, autosomal recessive, with or without
CC       impaired intellectual development (PNRIID) [MIM:618124]: An autosomal
CC       recessive disorder characterized by early childhood-onset of peripheral
CC       sensorimotor neuropathy, progressive distal muscle weakness, atrophy in
CC       hands and feet, and gait difficulties, often with loss of ambulation.
CC       Most affected individuals also have impaired intellectual development,
CC       although some have normal cognition. Additional features may include
CC       eye movement abnormalities, claw hands, foot deformities, and
CC       scoliosis. {ECO:0000269|PubMed:24123876, ECO:0000269|PubMed:28633435,
CC       ECO:0000269|PubMed:28969388, ECO:0000269|PubMed:29982295}. Note=The
CC       disease is caused by variants affecting distinct genetic loci,
CC       including the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform MCM3AP]: Produced via an alternative promoter
CC       within an intron of GANP. MCM3AP promoter elements are poorly conserved
CC       in mice, suggesting that the regulation of MCM3AP may be human
CC       specific. {ECO:0000269|PubMed:21195085}.
CC   -!- SIMILARITY: Belongs to the SAC3 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/mcm3ap/";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ010089; CAB52687.1; -; mRNA.
DR   EMBL; AY590469; AAS89300.1; -; Genomic_DNA.
DR   EMBL; AP000471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC013285; AAH13285.2; -; mRNA.
DR   EMBL; BC004497; AAH04497.2; -; mRNA.
DR   EMBL; BC104958; AAI04959.1; -; mRNA.
DR   EMBL; BC104960; AAI04961.1; -; mRNA.
DR   EMBL; AB011144; BAA25498.1; -; mRNA.
DR   EMBL; AB005543; BAA25170.1; -; mRNA.
DR   CCDS; CCDS13734.1; -. [O60318-1]
DR   PIR; T00339; T00339.
DR   RefSeq; NP_003897.2; NM_003906.4. [O60318-1]
DR   RefSeq; XP_005261260.1; XM_005261203.4. [O60318-1]
DR   RefSeq; XP_005261261.1; XM_005261204.4. [O60318-1]
DR   RefSeq; XP_005261262.1; XM_005261205.3. [O60318-1]
DR   PDB; 4DHX; X-ray; 2.10 A; A/D=1163-1235.
DR   PDBsum; 4DHX; -.
DR   AlphaFoldDB; O60318; -.
DR   SMR; O60318; -.
DR   BioGRID; 114406; 140.
DR   ComplexPortal; CPX-2477; TREX-2 transcription-export complex, CETN2 variant.
DR   ComplexPortal; CPX-7281; TREX-2 transcription-export complex, CETN3 variant.
DR   DIP; DIP-31696N; -.
DR   IntAct; O60318; 47.
DR   MINT; O60318; -.
DR   STRING; 9606.ENSP00000291688; -.
DR   TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR   GlyCosmos; O60318; 12 sites, 2 glycans.
DR   GlyGen; O60318; 14 sites, 2 O-linked glycans (14 sites).
DR   iPTMnet; O60318; -.
DR   PhosphoSitePlus; O60318; -.
DR   SwissPalm; O60318; -.
DR   BioMuta; MCM3AP; -.
DR   EPD; O60318; -.
DR   jPOST; O60318; -.
DR   MassIVE; O60318; -.
DR   MaxQB; O60318; -.
DR   PaxDb; 9606-ENSP00000380820; -.
DR   PeptideAtlas; O60318; -.
DR   ProteomicsDB; 10659; -.
DR   ProteomicsDB; 49343; -. [O60318-1]
DR   Pumba; O60318; -.
DR   Antibodypedia; 10636; 274 antibodies from 33 providers.
DR   DNASU; 8888; -.
DR   Ensembl; ENST00000291688.6; ENSP00000291688.1; ENSG00000160294.11. [O60318-1]
DR   Ensembl; ENST00000397708.1; ENSP00000380820.1; ENSG00000160294.11. [O60318-1]
DR   GeneID; 8888; -.
DR   KEGG; hsa:8888; -.
DR   MANE-Select; ENST00000291688.6; ENSP00000291688.1; NM_003906.5; NP_003897.2.
DR   UCSC; uc002zir.3; human. [O60318-1]
DR   AGR; HGNC:6946; -.
DR   CTD; 8888; -.
DR   DisGeNET; 8888; -.
DR   GeneCards; MCM3AP; -.
DR   GeneReviews; MCM3AP; -.
DR   HGNC; HGNC:6946; MCM3AP.
DR   HPA; ENSG00000160294; Low tissue specificity.
DR   MalaCards; MCM3AP; -.
DR   MIM; 603294; gene.
DR   MIM; 618124; phenotype.
DR   neXtProt; NX_O60318; -.
DR   OpenTargets; ENSG00000160294; -.
DR   PharmGKB; PA30692; -.
DR   VEuPathDB; HostDB:ENSG00000160294; -.
DR   eggNOG; KOG1860; Eukaryota.
DR   GeneTree; ENSGT00940000156322; -.
DR   HOGENOM; CLU_001842_1_0_1; -.
DR   InParanoid; O60318; -.
DR   OMA; DMTIFWH; -.
DR   OrthoDB; 91913at2759; -.
DR   PhylomeDB; O60318; -.
DR   TreeFam; TF105948; -.
DR   PathwayCommons; O60318; -.
DR   SignaLink; O60318; -.
DR   SIGNOR; O60318; -.
DR   BioGRID-ORCS; 8888; 808 hits in 1169 CRISPR screens.
DR   ChiTaRS; MCM3AP; human.
DR   GeneWiki; MCM3AP; -.
DR   GenomeRNAi; 8888; -.
DR   Pharos; O60318; Tbio.
DR   PRO; PR:O60318; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; O60318; Protein.
DR   Bgee; ENSG00000160294; Expressed in tendon of biceps brachii and 202 other cell types or tissues.
DR   ExpressionAtlas; O60318; baseline and differential.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0070390; C:transcription export complex 2; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR   GO; GO:0010484; F:histone H3 acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0034728; P:nucleosome organization; IDA:UniProtKB.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IDA:UniProtKB.
DR   CDD; cd12443; RRM_MCM3A_like; 1.
DR   Gene3D; 1.25.40.990; -; 1.
DR   Gene3D; 6.10.250.1340; -; 1.
DR   InterPro; IPR031910; GANP_CID_dom.
DR   InterPro; IPR031907; MCM3AP_GANP.
DR   InterPro; IPR034265; MCM3AP_RRM.
DR   InterPro; IPR031908; NupH_GANP.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR045107; SAC3/GANP/THP3.
DR   InterPro; IPR005062; SAC3/GANP/THP3_conserved.
DR   PANTHER; PTHR12436; 80 KDA MCM3-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR12436:SF3; GERMINAL-CENTER ASSOCIATED NUCLEAR PROTEIN; 1.
DR   Pfam; PF16766; CID_GANP; 1.
DR   Pfam; PF16769; MCM3AP_GANP; 1.
DR   Pfam; PF16768; NupH_GANP; 1.
DR   Pfam; PF03399; SAC3_GANP; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50250; PCI; 1.
DR   Genevisible; O60318; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Acyltransferase; Alternative promoter usage;
KW   Chromosome; Coiled coil; Cytoplasm; Immunity; Intellectual disability;
KW   Methylation; mRNA transport; Neuropathy; Nuclear pore complex; Nucleus;
KW   Phosphoprotein; Protein transport; Reference proteome; Transferase;
KW   Translocation; Transport.
FT   CHAIN           1..1980
FT                   /note="Germinal-center associated nuclear protein"
FT                   /id="PRO_0000096284"
FT   DOMAIN          775..958
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          33..340
FT                   /note="FG-repeats"
FT   REGION          212..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..1003
FT                   /note="Interaction with PCID2 and SEM1"
FT                   /evidence="ECO:0000269|PubMed:22307388"
FT   REGION          998..1038
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1162..1256
FT                   /note="CID"
FT   REGION          1162..1200
FT                   /note="Interaction with ENY2"
FT                   /evidence="ECO:0000269|PubMed:22307388"
FT   REGION          1207..1235
FT                   /note="Interaction with ENY2"
FT                   /evidence="ECO:0000269|PubMed:22307388"
FT   REGION          1236..1256
FT                   /note="Interaction with Centrin"
FT                   /evidence="ECO:0000269|PubMed:22307388"
FT   REGION          1658..1790
FT                   /note="Acetyltransferase"
FT   COILED          1133..1170
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..526
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         32
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUU9"
FT   MOD_RES         430
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         489
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUU9"
FT   MOD_RES         490
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUU9"
FT   MOD_RES         508
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUU9"
FT   MOD_RES         538
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         557
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..1259
FT                   /note="Missing (in isoform MCM3AP)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_053438"
FT   VARIANT         102
FT                   /note="S -> L (in dbSNP:rs9975588)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT                   /id="VAR_019240"
FT   VARIANT         288
FT                   /note="M -> V (in dbSNP:rs17182545)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_019241"
FT   VARIANT         333
FT                   /note="R -> L (in dbSNP:rs17182552)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_019242"
FT   VARIANT         409
FT                   /note="L -> V (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs773228537)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035472"
FT   VARIANT         413
FT                   /note="P -> L (in dbSNP:rs17182566)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_019243"
FT   VARIANT         762
FT                   /note="M -> T (in PNRIID; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:28633435"
FT                   /id="VAR_081543"
FT   VARIANT         867
FT                   /note="A -> D (in PNRIID; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:28633435"
FT                   /id="VAR_081544"
FT   VARIANT         870
FT                   /note="L -> S (in PNRIID; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:29982295"
FT                   /id="VAR_081545"
FT   VARIANT         878
FT                   /note="R -> H (in PNRIID; uncertain significance;
FT                   dbSNP:rs373674344)"
FT                   /evidence="ECO:0000269|PubMed:28969388"
FT                   /id="VAR_081546"
FT   VARIANT         889..1980
FT                   /note="Missing (in PNRIID)"
FT                   /evidence="ECO:0000269|PubMed:28633435"
FT                   /id="VAR_081547"
FT   VARIANT         915
FT                   /note="E -> K (in PNRIID; uncertain significance;
FT                   dbSNP:rs483352869)"
FT                   /evidence="ECO:0000269|PubMed:24123876"
FT                   /id="VAR_070560"
FT   VARIANT         951
FT                   /note="S -> P (in PNRIID; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:28969388"
FT                   /id="VAR_081548"
FT   VARIANT         1051
FT                   /note="P -> L (in dbSNP:rs17182850)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_019244"
FT   VARIANT         1062
FT                   /note="V -> M (in dbSNP:rs17182857)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_019245"
FT   VARIANT         1272
FT                   /note="V -> M (in PNRIID; uncertain significance;
FT                   dbSNP:rs779248881)"
FT                   /evidence="ECO:0000269|PubMed:28633435"
FT                   /id="VAR_081549"
FT   VARIANT         1314
FT                   /note="R -> W (in dbSNP:rs17176709)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_019246"
FT   VARIANT         1449
FT                   /note="D -> E (in dbSNP:rs17183220)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_019247"
FT   VARIANT         1478..1980
FT                   /note="Missing (in PNRIID; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:28633435"
FT                   /id="VAR_081550"
FT   VARIANT         1576
FT                   /note="V -> I (in dbSNP:rs17183248)"
FT                   /evidence="ECO:0000269|PubMed:16959974, ECO:0000269|Ref.2"
FT                   /id="VAR_019248"
FT   VARIANT         1577
FT                   /note="E -> K (in PNRIID; uncertain significance;
FT                   dbSNP:rs779630101)"
FT                   /evidence="ECO:0000269|PubMed:28633435"
FT                   /id="VAR_081551"
FT   VARIANT         1795
FT                   /note="A -> T (in dbSNP:rs17183290)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_019249"
FT   VARIANT         1804..1980
FT                   /note="Missing (in PNRIID; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:28969388"
FT                   /id="VAR_081552"
FT   VARIANT         1831
FT                   /note="R -> C (in dbSNP:rs2298697)"
FT                   /id="VAR_053973"
FT   VARIANT         1870
FT                   /note="L -> R (in dbSNP:rs17176933)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_019250"
FT   VARIANT         1941
FT                   /note="A -> V (in dbSNP:rs17183403)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_019251"
FT   MUTAGEN         1496..1501
FT                   /note="LPLVVL->APLAAA: Loss of i nteraction with MCM3, loss
FT                   of nuclear localization, loss of chromatin-binding."
FT                   /evidence="ECO:0000269|PubMed:12226073"
FT   MUTAGEN         1730..1733
FT                   /note="HGAG->AAAA: Severely decreased acetylase activity,
FT                   loss of DNA replication inhibition. Does not affect
FT                   chromatin-binding."
FT                   /evidence="ECO:0000269|PubMed:11258703,
FT                   ECO:0000269|PubMed:12226073"
FT   HELIX           1168..1232
FT                   /evidence="ECO:0007829|PDB:4DHX"
SQ   SEQUENCE   1980 AA;  218405 MW;  503D192686FC38A8 CRC64;
     MNPTNPFSGQ QPSAFSASSS NVGTLPSKPP FRFGQPSLFG QNSTLSGKSS GFSQVSSFPA
     SSGVSHSSSV QTLGFTQTSS VGPFSGLEHT STFVATSGPS SSSVLGNTGF SFKSPTSVGA
     FPSTSAFGQE AGEIVNSGFG KTEFSFKPLE NAVFKPILGA ESEPEKTQSQ IASGFFTFSH
     PISSAPGGLA PFSFPQVTSS SATTSNFTFS KPVSSNNSLS AFTPALSNQN VEEEKRGPKS
     IFGSSNNSFS SFPVSSAVLG EPFQASKAGV RQGCEEAVSQ VEPLPSLMKG LKRKEDQDRS
     PRRHGHEPAE DSDPLSRGDH PPDKRPVRLN RPRGGTLFGR TIQDVFKSNK EVGRLGNKEA
     KKETGFVESA ESDHMAIPGG NQSVLAPSRI PGVNKEEETE SREKKEDSLR GTPARQSNRS
     ESTDSLGGLS PSEVTAIQCK NIPDYLNDRT ILENHFGKIA KVQRIFTRRS KKLAVVHFFD
     HASAALARKK GKSLHKDMAI FWHRKKISPN KKPFSLKEKK PGDGEVSPST EDAPFQHSPL
     GKAAGRTGAS SLLNKSSPVK KPSLLKAHQF EGDSFDSASE GSEGLGPCVL SLSTLIGTVA
     ETSKEKYRLL DQRDRIMRQA RVKRTDLDKA RTFVGTCLDM CPEKERYMRE TRSQLSVFEV
     VPGTDQVDHA AAVKEYSRSS ADQEEPLPHE LRPLPVLSRT MDYLVTQIMD QKEGSLRDWY
     DFVWNRTRGI RKDITQQHLC DPLTVSLIEK CTRFHIHCAH FMCEEPMSSF DAKINNENMT
     KCLQSLKEMY QDLRNKGVFC ASEAEFQGYN VLLSLNKGDI LREVQQFHPA VRNSSEVKFA
     VQAFAALNSN NFVRFFKLVQ SASYLNACLL HCYFSQIRKD ALRALNFAYT VSTQRSTIFP
     LDGVVRMLLF RDCEEATDFL TCHGLTVSDG CVELNRSAFL EPEGLSKTRK SVFITRKLTV
     SVGEIVNGGP LPPVPRHTPV CSFNSQNKYI GESLAAELPV STQRPGSDTV GGGRGEECGV
     EPDAPLSSLP QSLPAPAPSP VPLPPVLALT PSVAPSLFQL SVQPEPPPPE PVPMYSDEDL
     AQVVDELIQE ALQRDCEEVG SAGAAYAAAA LGVSNAAMED LLTAATTGIL RHIAAEEVSK
     ERERREQERQ RAEEERLKQE RELVLSELSQ GLAVELMERV MMEFVRETCS QELKNAVETD
     QRVRVARCCE DVCAHLVDLF LVEEIFQTAK ETLQELQCFC KYLQRWREAV TARKKLRRQM
     RAFPAAPCCV DVSDRLRALA PSAECPIAEE NLARGLLDLG HAGRLGISCT RLRRLRNKTA
     HQMKVQHFYQ QLLSDVAWAS LDLPSLVAEH LPGRQEHVFW KLVLVLPDVE EQSPESCGRI
     LANWLKVKFM GDEGSVDDTS SDAGGIQTLS LFNSLSSKGD QMISVNVCIK VAHGALSDGA
     IDAVETQKDL LGASGLMLLL PPKMKSEDMA EEDVYWLSAL LQLKQLLQAK PFQPALPLVV
     LVPSPGGDAV EKEVEDGLML QDLVSAKLIS DYTVTEIPDT INDLQGSTKV LQAVQWLVSH
     CPHSLDLCCQ TLIQYVEDGI GHEFSGRFFH DRRERRLGGL ASQEPGAIIE LFNSVLQFLA
     SVVSSEQLCD LSWPVTEFAE AGGSRLLPHL HWNAPEHLAW LKQAVLGFQL PQMDLPPLGA
     PWLPVCSMVV QYASQIPSSR QTQPVLQSQV ENLLHRTYCR WKSKSPSPVH GAGPSVMEIP
     WDDLIALCIN HKLRDWTPPR LPVTSEALSE DGQICVYFFK NDLKKYDVPL SWEQARLQTQ
     KELQLREGRL AIKPFHPSAN NFPIPLLHMH RNWKRSTECA QEGRIPSTED LMRGASAEEL
     LAQCLSSSLL LEKEENKRFE DQLQQWLSED SGAFTDLTSL PLYLPQTLVS LSHTIEPVMK
     TSVTTSPQSD MMREQLQLSE ATGTCLGERL KHLERLIRSS REEEVASELH LSALLDMVDI
//