ID   NIN_HUMAN               Reviewed;        2090 AA.
AC   Q8N4C6; A6NDB8; B7WPA3; C9JSB6; C9JSG2; C9JXL2; Q5BKU3; Q6P0P6; Q9BWU6;
AC   Q9C012; Q9C013; Q9C014; Q9H5I6; Q9HAT7; Q9HBY5; Q9HCK7; Q9UH61;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 4.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Ninein;
DE            Short=hNinein;
DE   AltName: Full=Glycogen synthase kinase 3 beta-interacting protein;
DE            Short=GSK3B-interacting protein;
GN   Name=NIN; Synonyms=KIAA1565;
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] (ISOFORM 5), SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, INTERACTION WITH GSK3B, AND VARIANTS PRO-1125 AND GLU-1320.
RC   TISSUE=Fetal liver;
RX   PubMed=11004522; DOI=10.1016/s0167-4781(00)00127-5;
RA   Hong Y.-R., Chen C.-H., Chang J.-H., Wang S.-K., Sy W.-D., Chou C.-K.,
RA   Howng S.-L.;
RT   "Cloning and characterization of a novel human ninein protein that
RT   interacts with the glycogen synthase kinase 3beta.";
RL   Biochim. Biophys. Acta 1492:513-516(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP   PRO-1125 AND GLU-1320.
RX   PubMed=11162463; DOI=10.1006/bbrc.2000.4050;
RA   Hong Y.-R., Chen C.-H., Chuo M.-H., Liou S.-Y., Howng S.-L.;
RT   "Genomic organization and molecular characterization of the human ninein
RT   gene.";
RL   Biochem. Biophys. Res. Commun. 279:989-995(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), PARTIAL NUCLEOTIDE SEQUENCE
RP   [MRNA] (ISOFORM 3), FUNCTION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION,
RP   AND VARIANTS PRO-1125 AND GLU-1320.
RC   TISSUE=Thymus;
RX   PubMed=15190203;
RA   Stillwell E.E., Zhou J., Joshi H.C.;
RT   "Human ninein is a centrosomal autoantigen recognized by CREST patient sera
RT   and plays a regulatory role in microtubule nucleation.";
RL   Cell Cycle 3:923-930(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC   TISSUE=Brain;
RX   PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA   Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:273-281(2000).
RN   [5]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-434 (ISOFORM 8), AND NUCLEOTIDE SEQUENCE [LARGE
RP   SCALE MRNA] OF 1877-2090 (ISOFORM 4).
RC   TISSUE=Lymph;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 1561-2090 (ISOFORMS 1 AND 7).
RC   TISSUE=Bone marrow;
RA   Choquette M.C., de Medicis E.;
RT   "3' isoforms of human ninein.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1928-2090 (ISOFORM 7).
RC   TISSUE=Hepatoma;
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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11956314; DOI=10.1242/jcs.115.9.1825;
RA   Ou Y.Y., Mack G.J., Zhang M., Rattner J.B.;
RT   "CEP110 and ninein are located in a specific domain of the centrosome
RT   associated with centrosome maturation.";
RL   J. Cell Sci. 115:1825-1835(2002).
RN   [11]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12403812; DOI=10.1083/jcb.200204023;
RA   Dammermann A., Merdes A.;
RT   "Assembly of centrosomal proteins and microtubule organization depends on
RT   PCM-1.";
RL   J. Cell Biol. 159:255-266(2002).
RN   [12]
RP   HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DOMAIN, AND
RP   PHOSPHORYLATION.
RX   PubMed=12927815; DOI=10.1016/s0006-291x(03)01510-9;
RA   Chen C.-H., Howng S.-L., Cheng T.-S., Chou M.-H., Huang C.-Y., Hong Y.-R.;
RT   "Molecular characterization of human ninein protein: two distinct
RT   subdomains required for centrosomal targeting and regulating signals in
RT   cell cycle.";
RL   Biochem. Biophys. Res. Commun. 308:975-983(2003).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [14]
RP   INTERACTION WITH C14ORF166.
RX   PubMed=15147888; DOI=10.1016/j.febslet.2004.04.024;
RA   Howng S.-L., Hsu H.-C., Cheng T.-S., Lee Y.-L., Chang L.-K., Lu P.-J.,
RA   Hong Y.-R.;
RT   "A novel ninein-interaction protein, CGI-99, blocks ninein phosphorylation
RT   by GSK3beta and is highly expressed in brain tumors.";
RL   FEBS Lett. 566:162-168(2004).
RN   [15]
RP   AUTOANTIBODY.
RX   PubMed=9506584;
RX   DOI=10.1002/1529-0131(199803)41:3<551::aid-art22>3.0.co;2-x;
RA   Mack G.J., Rees J., Sandblom O., Balczon R., Fritzler M.J., Rattner J.B.;
RT   "Autoantibodies to a group of centrosomal proteins in human autoimmune sera
RT   reactive with the centrosome.";
RL   Arthritis Rheum. 41:551-558(1998).
RN   [16]
RP   AUTOANTIBODY.
RX   PubMed=14503922; DOI=10.1186/1471-2431-3-11;
RA   Fritzler M.J., Zhang M., Stinton L.M., Rattner J.B.;
RT   "Spectrum of centrosome autoantibodies in childhood varicella and post-
RT   varicella acute cerebellar ataxia.";
RL   BMC Pediatr. 3:11-11(2003).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1550, AND IDENTIFICATION BY
RP   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   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1550, 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   [19]
RP   INTERACTION WITH AUNIP.
RX   PubMed=20596670; DOI=10.3892/ijo_00000691;
RA   Lieu A.S., Cheng T.S., Chou C.H., Wu C.H., Hsu C.Y., Huang C.Y.,
RA   Chang L.K., Loh J.K., Chang C.S., Hsu C.M., Howng S.L., Hong Y.R.;
RT   "Functional characterization of AIBp, a novel Aurora-A binding protein in
RT   centrosome structure and spindle formation.";
RL   Int. J. Oncol. 37:429-436(2010).
RN   [20]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23386061; DOI=10.1038/emboj.2013.3;
RA   Kodani A., Salome Sirerol-Piquer M., Seol A., Garcia-Verdugo J.M.,
RA   Reiter J.F.;
RT   "Kif3a interacts with Dynactin subunit p150 Glued to organize centriole
RT   subdistal appendages.";
RL   EMBO J. 32:597-607(2013).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-1550, 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   [22]
RP   INTERACTION WITH CCDC120.
RX   PubMed=28422092; DOI=10.1038/ncomms15057;
RA   Huang N., Xia Y., Zhang D., Wang S., Bao Y., He R., Teng J., Chen J.;
RT   "Hierarchical assembly of centriole subdistal appendages via centrosome
RT   binding proteins CCDC120 and CCDC68.";
RL   Nat. Commun. 8:15057-15057(2017).
RN   [23]
RP   VARIANT [LARGE SCALE ANALYSIS] GLU-1320.
RX   PubMed=18987736; DOI=10.1038/nature07485;
RA   Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
RA   Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
RA   Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
RA   Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
RA   Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
RA   Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
RA   Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
RA   Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA   DiPersio J.F., Wilson R.K.;
RT   "DNA sequencing of a cytogenetically normal acute myeloid leukaemia
RT   genome.";
RL   Nature 456:66-72(2008).
RN   [24]
RP   VARIANTS SCKL7 ARG-1222 AND SER-1709.
RX   PubMed=22933543; DOI=10.1210/jc.2012-2150;
RA   Dauber A., Lafranchi S.H., Maliga Z., Lui J.C., Moon J.E., McDeed C.,
RA   Henke K., Zonana J., Kingman G.A., Pers T.H., Baron J., Rosenfeld R.G.,
RA   Hirschhorn J.N., Harris M.P., Hwa V.;
RT   "Novel microcephalic primordial dwarfism disorder associated with variants
RT   in the centrosomal protein ninein.";
RL   J. Clin. Endocrinol. Metab. 97:E2140-E2151(2012).
CC   -!- FUNCTION: Centrosomal protein required in the positioning and anchorage
CC       of the microtubule minus-end in epithelial cells (PubMed:15190203,
CC       PubMed:23386061). May also act as a centrosome maturation factor
CC       (PubMed:11956314). May play a role in microtubule nucleation, by
CC       recruiting the gamma-tubulin ring complex to the centrosome
CC       (PubMed:15190203). Overexpression does not perturb nucleation or
CC       elongation of microtubules but suppresses release of microtubules
CC       (PubMed:15190203). Required for centriole organization and microtubule
CC       anchoring at the mother centriole (PubMed:23386061).
CC       {ECO:0000269|PubMed:11956314, ECO:0000269|PubMed:15190203,
CC       ECO:0000269|PubMed:23386061}.
CC   -!- SUBUNIT: Homooligomer. Interacts with GSK3B/GSK3-beta via its C-
CC       terminal domain (PubMed:11004522). Interacts with C14ORF166, such
CC       interaction may prevent its phosphorylation by GSK3B (PubMed:15147888).
CC       Interacts with AUNIP (via N-terminus) (PubMed:20596670). Identified in
CC       a complex with AUNIP and AURKA (PubMed:20596670). Interacts with
CC       CCDC120 (PubMed:28422092). Interacts (via C-terminus) with CEP250 (By
CC       similarity). Interacts with CEP170 (By similarity). Interacts with the
CC       gamma-tubulin ring complex component TUBGCP3 (By similarity). Interacts
CC       with gamma-tubulin (By similarity). Isoform 6 does not interact with
CC       CEP170 or CEP250 (By similarity). {ECO:0000250|UniProtKB:Q61043,
CC       ECO:0000269|PubMed:11004522, ECO:0000269|PubMed:15147888,
CC       ECO:0000269|PubMed:20596670, ECO:0000269|PubMed:28422092}.
CC   -!- INTERACTION:
CC       Q8N4C6; Q96HB5: CCDC120; NbExp=11; IntAct=EBI-1164022, EBI-744556;
CC       Q8N4C6; P49841: GSK3B; NbExp=3; IntAct=EBI-1164022, EBI-373586;
CC       Q8N4C6; Q9Y224: RTRAF; NbExp=4; IntAct=EBI-1164022, EBI-1104547;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000269|PubMed:11004522,
CC       ECO:0000269|PubMed:11956314, ECO:0000269|PubMed:12403812,
CC       ECO:0000269|PubMed:12927815, ECO:0000269|PubMed:14654843,
CC       ECO:0000269|PubMed:15190203}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriole {ECO:0000269|PubMed:23386061}.
CC       Note=Component of the core centrosome. Arranged in a tubular
CC       conformation with an open and a closed end within the centrosome. In
CC       the mother centrosome, it localizes at both ends of the centrosome
CC       tube, including the site of centrosome duplication, while in the
CC       daughter centrosome it is present only at the closed end. Requires PCM1
CC       for centrosome localization. Localizes to the subdistal appendage
CC       region of the centriole in a DCTN1-dependent manner.
CC       {ECO:0000269|PubMed:11956314, ECO:0000269|PubMed:12403812,
CC       ECO:0000269|PubMed:23386061}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm
CC       {ECO:0000250|UniProtKB:Q61043}. Note=Seems to have a dominant-negative
CC       effect on localization of other isoforms, promoting their dissociation
CC       from the centrosome. {ECO:0000250|UniProtKB:Q61043}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=9;
CC       Name=1; Synonyms=Lm;
CC         IsoId=Q8N4C6-1; Sequence=Displayed;
CC       Name=2; Synonyms=Isotype 3;
CC         IsoId=Q8N4C6-2; Sequence=VSP_010952;
CC       Name=3; Synonyms=Isotype 2;
CC         IsoId=Q8N4C6-10; Sequence=VSP_010952, VSP_010960;
CC       Name=4; Synonyms=Isotype 1;
CC         IsoId=Q8N4C6-4; Sequence=VSP_010952, VSP_010957, VSP_010958;
CC       Name=5;
CC         IsoId=Q8N4C6-5; Sequence=VSP_010950;
CC       Name=6;
CC         IsoId=Q8N4C6-6; Sequence=VSP_010953, VSP_010954, VSP_010955,
CC                                  VSP_010956;
CC       Name=7; Synonyms=B;
CC         IsoId=Q8N4C6-7; Sequence=VSP_010960;
CC       Name=8;
CC         IsoId=Q8N4C6-9; Sequence=VSP_040039;
CC       Name=9;
CC         IsoId=Q8N4C6-11; Sequence=VSP_010953;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart and skeletal
CC       muscle. Isoform 1 is more expressed than isoform 5.
CC       {ECO:0000269|PubMed:11004522, ECO:0000269|PubMed:11162463}.
CC   -!- DEVELOPMENTAL STAGE: In interphase cells, it is localized in the
CC       centrosome. Decreases in metaphase and anaphase and reappears in
CC       telophase. {ECO:0000269|PubMed:12927815}.
CC   -!- DOMAIN: There is conflicting information regarding the regions required
CC       for centrosomal localization. One study shows that the region 1601-1682
CC       is necessary and sufficient for targeting to the centrosome
CC       (PubMed:12927815). Another study shows that a separate region, 1291-
CC       1575, is important for centrosomal localization (PubMed:15190203).
CC       However, a third study shows that the coiled-coil region (373-1885) is
CC       not sufficient for centrosomal localization and instead localizes to
CC       cytoplasmic speckles (By similarity). The observed differences might be
CC       due to oligomerization of the longer coiled-coil domain-containing
CC       sequence, which would mask the shorter centrosomal targeting sequences
CC       (By similarity). {ECO:0000250|UniProtKB:Q61043,
CC       ECO:0000269|PubMed:12927815, ECO:0000269|PubMed:15190203}.
CC   -!- DOMAIN: The N-terminal domain is important for targeting to the mother
CC       centriole, although it is not sufficient by itself for centrosomal
CC       localization. {ECO:0000250|UniProtKB:Q61043}.
CC   -!- PTM: Phosphorylated by AURKA/Aurora kinase A and PKA kinases but not
CC       CK2 or AURKB/ Aurora kinase B. {ECO:0000269|PubMed:12927815}.
CC   -!- DISEASE: Seckel syndrome 7 (SCKL7) [MIM:614851]: A rare autosomal
CC       recessive disorder characterized by proportionate dwarfism of prenatal
CC       onset associated with low birth weight, growth retardation, severe
CC       microcephaly with a bird-headed like appearance, and intellectual
CC       disability. {ECO:0000269|PubMed:22933543}. Note=The disease is caused
CC       by variants affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: Antibodies against NIN are present in sera from patients
CC       with autoimmune diseases that developed autoantibodies against
CC       centrosomal proteins.
CC   -!- MISCELLANEOUS: [Isoform 2]: Dubious isoform produced through aberrant
CC       splice sites. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 3]: Dubious isoform produced through aberrant
CC       splice sites. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 4]: Dubious isoform produced through aberrant
CC       splice sites. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH65521.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH65521.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=AAK00628.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
CC       Sequence=AAK00629.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors and frameshifts.; Evidence={ECO:0000305};
CC       Sequence=AAK00630.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
CC       Sequence=BAB13391.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB15640.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/176/NIN";
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DR   EMBL; AF212162; AAF23015.2; -; mRNA.
DR   EMBL; AF302773; AAG33512.2; -; mRNA.
DR   EMBL; AF223937; AAK00628.1; ALT_SEQ; mRNA.
DR   EMBL; AF223938; AAK00629.1; ALT_SEQ; mRNA.
DR   EMBL; AF223939; AAK00630.1; ALT_SEQ; mRNA.
DR   EMBL; AB046785; BAB13391.2; ALT_INIT; mRNA.
DR   EMBL; AL133485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL606834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC034708; AAH34708.2; -; mRNA.
DR   EMBL; BC065521; AAH65521.1; ALT_SEQ; mRNA.
DR   EMBL; BC090932; AAH90932.1; -; mRNA.
DR   EMBL; AY027794; AAK27375.1; -; mRNA.
DR   EMBL; AY027795; AAK27376.1; -; mRNA.
DR   EMBL; AY027796; AAK27377.1; -; mRNA.
DR   EMBL; AF186776; AAG17027.1; -; mRNA.
DR   EMBL; AK027054; BAB15640.1; ALT_INIT; mRNA.
DR   CCDS; CCDS32078.2; -. [Q8N4C6-11]
DR   CCDS; CCDS32079.1; -. [Q8N4C6-1]
DR   CCDS; CCDS91876.1; -. [Q8N4C6-7]
DR   RefSeq; NP_057434.4; NM_016350.4. [Q8N4C6-11]
DR   RefSeq; NP_065972.3; NM_020921.3. [Q8N4C6-7]
DR   RefSeq; NP_891989.2; NM_182944.2.
DR   RefSeq; NP_891991.1; NM_182946.1. [Q8N4C6-1]
DR   RefSeq; XP_011535125.1; XM_011536823.2.
DR   AlphaFoldDB; Q8N4C6; -.
DR   SMR; Q8N4C6; -.
DR   BioGRID; 119372; 389.
DR   IntAct; Q8N4C6; 130.
DR   MINT; Q8N4C6; -.
DR   STRING; 9606.ENSP00000371472; -.
DR   BindingDB; Q8N4C6; -.
DR   GlyGen; Q8N4C6; 6 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; Q8N4C6; -.
DR   PhosphoSitePlus; Q8N4C6; -.
DR   BioMuta; NIN; -.
DR   DMDM; 311033487; -.
DR   EPD; Q8N4C6; -.
DR   jPOST; Q8N4C6; -.
DR   MassIVE; Q8N4C6; -.
DR   MaxQB; Q8N4C6; -.
DR   PaxDb; 9606-ENSP00000371472; -.
DR   PeptideAtlas; Q8N4C6; -.
DR   ProteomicsDB; 71907; -. [Q8N4C6-1]
DR   ProteomicsDB; 71908; -. [Q8N4C6-10]
DR   ProteomicsDB; 71909; -. [Q8N4C6-11]
DR   ProteomicsDB; 71910; -. [Q8N4C6-2]
DR   ProteomicsDB; 71911; -. [Q8N4C6-4]
DR   ProteomicsDB; 71912; -. [Q8N4C6-5]
DR   ProteomicsDB; 71913; -. [Q8N4C6-6]
DR   ProteomicsDB; 71914; -. [Q8N4C6-7]
DR   ProteomicsDB; 71915; -. [Q8N4C6-9]
DR   Pumba; Q8N4C6; -.
DR   Antibodypedia; 23688; 177 antibodies from 24 providers.
DR   DNASU; 51199; -.
DR   Ensembl; ENST00000324330.13; ENSP00000324210.10; ENSG00000100503.27. [Q8N4C6-11]
DR   Ensembl; ENST00000382041.7; ENSP00000371472.3; ENSG00000100503.27. [Q8N4C6-1]
DR   Ensembl; ENST00000382043.8; ENSP00000371474.4; ENSG00000100503.27. [Q8N4C6-11]
DR   Ensembl; ENST00000530997.7; ENSP00000436092.2; ENSG00000100503.27. [Q8N4C6-7]
DR   GeneID; 51199; -.
DR   KEGG; hsa:51199; -.
DR   MANE-Select; ENST00000530997.7; ENSP00000436092.2; NM_020921.4; NP_065972.4. [Q8N4C6-7]
DR   UCSC; uc001wyi.3; human. [Q8N4C6-1]
DR   AGR; HGNC:14906; -.
DR   CTD; 51199; -.
DR   DisGeNET; 51199; -.
DR   GeneCards; NIN; -.
DR   HGNC; HGNC:14906; NIN.
DR   HPA; ENSG00000100503; Tissue enhanced (bone).
DR   MalaCards; NIN; -.
DR   MIM; 608684; gene.
DR   MIM; 614851; phenotype.
DR   neXtProt; NX_Q8N4C6; -.
DR   OpenTargets; ENSG00000100503; -.
DR   Orphanet; 319675; Microcephalic primordial dwarfism, Dauber type.
DR   PharmGKB; PA31630; -.
DR   VEuPathDB; HostDB:ENSG00000100503; -.
DR   eggNOG; ENOG502QZCC; Eukaryota.
DR   GeneTree; ENSGT00660000095541; -.
DR   HOGENOM; CLU_001462_1_1_1; -.
DR   InParanoid; Q8N4C6; -.
DR   OMA; QDHYEER; -.
DR   OrthoDB; 2880167at2759; -.
DR   PhylomeDB; Q8N4C6; -.
DR   TreeFam; TF325139; -.
DR   PathwayCommons; Q8N4C6; -.
DR   SignaLink; Q8N4C6; -.
DR   SIGNOR; Q8N4C6; -.
DR   BioGRID-ORCS; 51199; 15 hits in 1161 CRISPR screens.
DR   ChiTaRS; NIN; human.
DR   GeneWiki; NIN_(gene); -.
DR   GenomeRNAi; 51199; -.
DR   Pharos; Q8N4C6; Tbio.
DR   PRO; PR:Q8N4C6; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q8N4C6; Protein.
DR   Bgee; ENSG00000100503; Expressed in oviduct epithelium and 188 other cell types or tissues.
DR   ExpressionAtlas; Q8N4C6; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR   GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
DR   GO; GO:0120103; C:centriolar subdistal appendage; IDA:GO_Central.
DR   GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IDA:HPA.
DR   GO; GO:0097539; C:ciliary transition fiber; IBA:GO_Central.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR   GO; GO:0097431; C:mitotic spindle pole; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0000242; C:pericentriolar material; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0000922; C:spindle pole; IMP:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR   GO; GO:0051011; F:microtubule minus-end binding; IEA:Ensembl.
DR   GO; GO:0010457; P:centriole-centriole cohesion; IMP:GO_Central.
DR   GO; GO:0051642; P:centrosome localization; IBA:GO_Central.
DR   GO; GO:0090222; P:centrosome-templated microtubule nucleation; IBA:GO_Central.
DR   GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
DR   GO; GO:0021540; P:corpus callosum morphogenesis; IEA:Ensembl.
DR   GO; GO:0021957; P:corticospinal tract morphogenesis; IEA:Ensembl.
DR   GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:UniProtKB.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; IEA:Ensembl.
DR   GO; GO:0008104; P:protein localization; IMP:GO_Central.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR18905; NINEIN; 1.
DR   PANTHER; PTHR18905:SF11; NINEIN; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS50222; EF_HAND_2; 5.
DR   Genevisible; Q8N4C6; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Disease variant; Dwarfism; GTP-binding; Intellectual disability;
KW   Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..2090
FT                   /note="Ninein"
FT                   /id="PRO_0000096844"
FT   DOMAIN          8..43
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          42..77
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          182..217
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          219..252
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          317..352
FT                   /note="EF-hand 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          574..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          802..1505
FT                   /note="Important for interaction with CEP170"
FT                   /evidence="ECO:0000250|UniProtKB:Q61043"
FT   REGION          1152..1190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          357..570
FT                   /evidence="ECO:0000255"
FT   COILED          625..1027
FT                   /evidence="ECO:0000255"
FT   COILED          1068..1099
FT                   /evidence="ECO:0000255"
FT   COILED          1181..1341
FT                   /evidence="ECO:0000255"
FT   COILED          1441..1816
FT                   /evidence="ECO:0000255"
FT   COILED          1854..1885
FT                   /evidence="ECO:0000255"
FT   COILED          1922..2067
FT                   /evidence="ECO:0000255"
FT   BINDING         245..252
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         300..304
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         420..423
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         269
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61043"
FT   MOD_RES         1550
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1837
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61043"
FT   VAR_SEQ         1..38
FT                   /note="Missing (in isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040039"
FT   VAR_SEQ         1..35
FT                   /note="MDEVEQDQHEARLKELFDSFDTTGTGSLGQEELTD -> MAEVTVPRVYVVF
FT                   GIHCIMAKASSDVQVSGFHRKIQHVKNE (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:11004522"
FT                   /id="VSP_010950"
FT   VAR_SEQ         492..508
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15190203,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010952"
FT   VAR_SEQ         800..1512
FT                   /note="Missing (in isoform 6 and isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:10997877,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010953"
FT   VAR_SEQ         1555
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:10997877"
FT                   /id="VSP_010954"
FT   VAR_SEQ         1960..1988
FT                   /note="MQHLRSTATPSPSPHAWDLQLLQQQACPM -> NSVVGSSREGCSSLPEIVC
FT                   EDAAPEVHCDA (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:10997877"
FT                   /id="VSP_010955"
FT   VAR_SEQ         1989..2090
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:10997877"
FT                   /id="VSP_010956"
FT   VAR_SEQ         2027..2046
FT                   /note="GNQEQLVTVMEERMIEVEQK -> ALLPEQRAVHADSYRRIGHL (in
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15190203,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010957"
FT   VAR_SEQ         2047..2090
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15190203,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010958"
FT   VAR_SEQ         2065..2090
FT                   /note="VSLPGHLCSPTSHSSFNSSFTSLYCH -> LCKNTKADAMVKDLYVENAQLL
FT                   KALEVTEQRQKTAEKKNYLLEEKIASLSNIVRNLTPAPLTSTPPLRS (in isoform
FT                   3 and isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.8"
FT                   /id="VSP_010960"
FT   VARIANT         1111
FT                   /note="P -> A (in dbSNP:rs2236316)"
FT                   /id="VAR_019453"
FT   VARIANT         1125
FT                   /note="Q -> P (in dbSNP:rs12882191)"
FT                   /evidence="ECO:0000269|PubMed:11004522,
FT                   ECO:0000269|PubMed:11162463, ECO:0000269|PubMed:15190203"
FT                   /id="VAR_051235"
FT   VARIANT         1222
FT                   /note="Q -> R (in SCKL7; does not disrupt protein
FT                   expression or localization or affect mitotic functions in
FT                   an obvious way; dbSNP:rs187464517)"
FT                   /evidence="ECO:0000269|PubMed:22933543"
FT                   /id="VAR_069083"
FT   VARIANT         1320
FT                   /note="G -> E (in dbSNP:rs2073347)"
FT                   /evidence="ECO:0000269|PubMed:11004522,
FT                   ECO:0000269|PubMed:11162463, ECO:0000269|PubMed:15190203,
FT                   ECO:0000269|PubMed:18987736"
FT                   /id="VAR_019454"
FT   VARIANT         1709
FT                   /note="N -> S (in SCKL7; does not disrupt protein
FT                   expression or localization or affect mitotic functions in
FT                   an obvious way; dbSNP:rs387907308)"
FT                   /evidence="ECO:0000269|PubMed:22933543"
FT                   /id="VAR_069084"
FT   VARIANT         1837
FT                   /note="S -> T (in dbSNP:rs12717411)"
FT                   /id="VAR_019455"
FT   VARIANT         1934
FT                   /note="Q -> E (in dbSNP:rs2295847)"
FT                   /id="VAR_051236"
FT   CONFLICT        137
FT                   /note="H -> Y (in Ref. 1; AAF23015 and 2; AAG33512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="S -> F (in Ref. 1; AAF23015)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        203
FT                   /note="N -> D (in Ref. 2; AAG33512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223
FT                   /note="M -> I (in Ref. 2; AAG33512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="F -> I (in Ref. 2; AAG33512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        369
FT                   /note="I -> V (in Ref. 2; AAG33512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        399
FT                   /note="L -> S (in Ref. 2; AAG33512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        568
FT                   /note="L -> F (in Ref. 2; AAG33512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        809
FT                   /note="R -> I (in Ref. 1; AAF23015)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        812
FT                   /note="S -> T (in Ref. 2; AAG33512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        945
FT                   /note="K -> I (in Ref. 2; AAG33512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        977
FT                   /note="D -> A (in Ref. 2; AAG33512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        980
FT                   /note="R -> G (in Ref. 1; AAF23015)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1054
FT                   /note="Q -> H (in Ref. 2; AAG33512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1067
FT                   /note="L -> F (in Ref. 2; AAG33512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1070
FT                   /note="L -> Q (in Ref. 1; AAF23015)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1150
FT                   /note="D -> G (in Ref. 1; AAF23015)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1237
FT                   /note="M -> I (in Ref. 1; AAF23015)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2090 AA;  243249 MW;  51D27CD38A369209 CRC64;
     MDEVEQDQHE ARLKELFDSF DTTGTGSLGQ EELTDLCHML SLEEVAPVLQ QTLLQDNLLG
     RVHFDQFKEA LILILSRTLS NEEHFQEPDC SLEAQPKYVR GGKRYGRRSL PEFQESVEEF
     PEVTVIEPLD EEARPSHIPA GDCSEHWKTQ RSEEYEAEGQ LRFWNPDDLN ASQSGSSPPQ
     DWIEEKLQEV CEDLGITRDG HLNRKKLVSI CEQYGLQNVD GEMLEEVFHN LDPDGTMSVE
     DFFYGLFKNG KSLTPSASTP YRQLKRHLSM QSFDESGRRT TTSSAMTSTI GFRVFSCLDD
     GMGHASVERI LDTWQEEGIE NSQEILKALD FSLDGNINLT ELTLALENEL LVTKNSIHQA
     ALASFKAEIR HLLERVDQVV REKEKLRSDL DKAEKLKSLM ASEVDDHHAA IERRNEYNLR
     KLDEEYKERI AALKNELRKE REQILQQAGK QRLELEQEIE KAKTEENYIR DRLALSLKEN
     SRLENELLEN AEKLAEYENL TNKLQRNLEN VLAEKFGDLD PSSAEFFLQE ERLTQMRNEY
     ERQCRVLQDQ VDELQSELEE YRAQGRVLRL PLKNSPSEEV EANSGGIEPE HGLGSEECNP
     LNMSIEAELV IEQMKEQHHR DICCLRLELE DKVRHYEKQL DETVVSCKKA QENMKQRHEN
     ETHTLEKQIS DLKNEIAELQ GQAAVLKEAH HEATCRHEEE KKQLQVKLEE EKTHLQEKLR
     LQHEMELKAR LTQAQASFER EREGLQSSAW TEEKVRGLTQ ELEQFHQEQL TSLVEKHTLE
     KEELRKELLE KHQRELQEGR EKMETECNRR TSQIEAQFQS DCQKVTERCE SALQSLEGRY
     RQELKDLQEQ QREEKSQWEF EKDELTQECA EAQELLKETL KREKTTSLVL TQEREMLEKT
     YKEHLNSMVV ERQQLLQDLE DLRNVSETQQ SLLSDQILEL KSSHKRELRE REEVLCQAGA
     SEQLASQRLE RLEMEHDQER QEMMSKLLAM ENIHKATCET ADRERAEMST EISRLQSKIK
     EMQQATSPLS MLQSGCQVIG EEEVEGDGAL SLLQQGEQLL EENGDVLLSL QRAHEQAVKE
     NVKMATEISR LQQRLQKLEP GLVMSSCLDE PATEFFGNTA EQTEQFLQQN RTKQVEGVTR
     RHVLSDLEDD EVRDLGSTGT SSVQRQEVKI EESEASVEGF SELENSEETR TESWELKNQI
     SQLQEQLMML CADCDRASEK KQDLLFDVSV LKKKLKMLER IPEASPKYKL LYEDVSREND
     CLQEELRMME TRYDEALENN KELTAEVFRL QDELKKMEEV TETFLSLEKS YDEVKIENEG
     LNVLVLRLQG KIEKLQESVV QRCDCCLWEA SLENLEIEPD GNILQLNQTL EECVPRVRSV
     HHVIEECKQE NQYLEGNTQL LEKVKAHEIA WLHGTIQTHQ ERPRVQNQVI LEENTTLLGF
     QDKHFQHQAT IAELELEKTK LQELTRKLKE RVTILVKQKD VLSHGEKEEE LKAMMHDLQI
     TCSEMQQKVE LLRYESEKLQ QENSILRNEI TTLNEEDSIS NLKLGTLNGS QEEMWQKTET
     VKQENAAVQK MVENLKKQIS ELKIKNQQLD LENTELSQKN SQNQEKLQEL NQRLTEMLCQ
     KEKEPGNSAL EEREQEKFNL KEELERCKVQ SSTLVSSLEA ELSEVKIQTH IVQQENHLLK
     DELEKMKQLH RCPDLSDFQQ KISSVLSYNE KLLKEKEALS EELNSCVDKL AKSSLLEHRI
     ATMKQEQKSW EHQSASLKSQ LVASQEKVQN LEDTVQNVNL QMSRMKSDLR VTQQEKEALK
     QEVMSLHKQL QNAGGKSWAP EIATHPSGLH NQQKRLSWDK LDHLMNEEQQ LLWQENERLQ
     TMVQNTKAEL THSREKVRQL ESNLLPKHQK HLNPSGTMNP TEQEKLSLKR ECDQFQKEQS
     PANRKVSQMN SLEQELETIH LENEGLKKKQ VKLDEQLMEM QHLRSTATPS PSPHAWDLQL
     LQQQACPMVP REQFLQLQRQ LLQAERINQH LQEELENRTS ETNTPQGNQE QLVTVMEERM
     IEVEQKLKLV KRLLQEKVNQ LKEQVSLPGH LCSPTSHSSF NSSFTSLYCH
//