NIN_HUMAN
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 03-AUG-2022, entry version 176.
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="http://atlasgeneticsoncology.org/Genes/NINID176.html";
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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 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. [Q8N4C6-5]
DR AlphaFoldDB; Q8N4C6; -.
DR SMR; Q8N4C6; -.
DR BioGRID; 119372; 379.
DR IntAct; Q8N4C6; 125.
DR MINT; Q8N4C6; -.
DR STRING; 9606.ENSP00000371472; -.
DR BindingDB; Q8N4C6; -.
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; Q8N4C6; -.
DR PeptideAtlas; Q8N4C6; -.
DR PRIDE; 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 Antibodypedia; 23688; 151 antibodies from 24 providers.
DR DNASU; 51199; -.
DR Ensembl; ENST00000324330.13; ENSP00000324210.10; ENSG00000100503.26. [Q8N4C6-11]
DR Ensembl; ENST00000382041.7; ENSP00000371472.3; ENSG00000100503.26. [Q8N4C6-1]
DR Ensembl; ENST00000382043.8; ENSP00000371474.4; ENSG00000100503.26. [Q8N4C6-11]
DR Ensembl; ENST00000530997.7; ENSP00000436092.2; ENSG00000100503.26. [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 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; QKVELLX; -.
DR OrthoDB; 95801at2759; -.
DR PhylomeDB; Q8N4C6; -.
DR TreeFam; TF325139; -.
DR PathwayCommons; Q8N4C6; -.
DR SignaLink; Q8N4C6; -.
DR SIGNOR; Q8N4C6; -.
DR BioGRID-ORCS; 51199; 15 hits in 1083 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 186 other tissues.
DR ExpressionAtlas; Q8N4C6; baseline and differential.
DR Genevisible; Q8N4C6; HS.
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:UniProtKB.
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 InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR029664; NIN.
DR PANTHER; PTHR18905:SF11; PTHR18905:SF11; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 5.
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
