KI21A_HUMAN
ID KI21A_HUMAN Reviewed; 1674 AA.
AC Q7Z4S6; A8MX28; B0I1R9; B9EGE4; F5H0C3; F5H219; Q2UVF1; Q6UKL9; Q7Z668;
AC Q86WZ5; Q8IVZ8; Q9C0F5; Q9NXU4; Q9Y590;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Kinesin-like protein KIF21A;
DE AltName: Full=Kinesin-like protein KIF2;
DE AltName: Full=Renal carcinoma antigen NY-REN-62;
GN Name=KIF21A; Synonyms=KIAA1708, KIF2;
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 1), AND VARIANTS CFEOM1 THR-356;
RP ARG-947; VAL-947; GLN-954; TRP-954 AND THR-1010.
RX PubMed=14595441; DOI=10.1038/ng1261;
RA Yamada K., Andrews C., Chan W.M., McKeown C.A., Magli A., De Berardinis T.,
RA Loewenstein A., Lazar M., O'Keefe M., Letson R., London A., Ruttum M.,
RA Matsumoto N., Saito N., Morris L., Monte M.D., Johnson R.H., Uyama E.,
RA Houtman W.A., De Vries B., Carlow T.J., Hart B.L., Krawiecki N.,
RA Shoffner J., Vogel M.C., Katowitz J., Goldstein S.M., Levin A.V.,
RA Sener E.C., Ozturk B.T., Akarsu A.N., Brodsky M.C., Hanisch F., Cruse R.P.,
RA Zubcov A.A., Robb R.M., Roggenkaemper P., Gottlob I., Kowal L., Battu R.,
RA Traboulsi E.I., Franceschini P., Newlin A., Demer J.L., Engle E.C.;
RT "Heterozygous mutations of the kinesin KIF21A in congenital fibrosis of the
RT extraocular muscles type 1 (CFEOM1).";
RL Nat. Genet. 35:318-321(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RC TISSUE=Brain cortex;
RA Pantelidou M., Lederer C.W., Zographos S.E., Pfaffl M.W., Cavallaro S.,
RA Santama N.;
RT "Differential expression analysis of molecular motors in ALS motor neuron
RT disease.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Zan Q., Guo J.H., Yu L.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Yamakawa H., Kikuno R.F., Nagase T., Ohara O.;
RT "Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free
RT recombination: preparation of full-length cDNA clones encoding motor
RT proteins.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-543 (ISOFORMS 1/2), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1243-1674 (ISOFORM 4).
RC TISSUE=Adrenal cortex, Brain, and Testis;
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 1-597 (ISOFORM 2), AND IDENTIFICATION AS A
RP RENAL CANCER ANTIGEN.
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-586 (ISOFORM 2).
RC TISSUE=Colon;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1674 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 654-1674 (ISOFORM 3).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1212; SER-1239 AND SER-1673,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
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 [15]
RP IDENTIFICATION BY 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524; SER-1212; SER-1239;
RP SER-1662; THR-1664 AND SER-1673, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1212 AND SER-1239, AND
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524; SER-1212; SER-1225;
RP SER-1229 AND SER-1239, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1212, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23] {ECO:0007744|PDB:5D3A}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 938-1017.
RA Bianchi S., Kraatz S., Steinmetz M.O., Kammerer A.R.;
RT "Structure of KIF21A regulatory coiled coil.";
RL Submitted (AUG-2015) to the PDB data bank.
RN [24] {ECO:0007744|PDB:5NFD}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 938-1017 OF MUTANT CYS-947.
RX PubMed=30135143; DOI=10.1042/bsr20181073;
RA Kraatz S.H.W., Bianchi S., Steinmetz M.O.;
RT "Combinatorial use of disulfide bridges and native sulfur-SAD phasing for
RT rapid structure determination of coiled-coils.";
RL Biosci. Rep. 38:0-0(2018).
RN [25] {ECO:0007744|PDB:5YBU, ECO:0007744|PDB:5YBV}
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 1146-1167 IN COMPLEX WITH KANK1
RP AND KANK2 ANKYRIN REPEAT REGIONS, INTERACTION WITH KANK1 AND KANK2, AND
RP MUTAGENESIS OF ARG-1154 AND LEU-1164.
RX PubMed=29183992; DOI=10.1074/jbc.m117.817494;
RA Guo Q., Liao S., Zhu Z., Li Y., Li F., Xu C.;
RT "Structural basis for the recognition of kinesin family member 21A (KIF21A)
RT by the ankyrin domains of KANK1 and KANK2 proteins.";
RL J. Biol. Chem. 293:557-566(2018).
RN [26] {ECO:0007744|PDB:7KLJ}
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 1337-1653.
RA Zeng H., Dong A., Loppnau P., Hutchinson A., Seitova A., Edwards A.M.,
RA Arrowsmith C.H., Halabelian L.;
RT "Crystal structure of the WD-repeat domain of human KIF21A.";
RL Submitted (OCT-2020) to the PDB data bank.
RN [27]
RP VARIANT CFEOM1 THR-947.
RX PubMed=16157808; DOI=10.1001/archopht.123.9.1254;
RA Yamada K., Hunter D.G., Andrews C., Engle E.C.;
RT "A novel KIF21A mutation in a patient with congenital fibrosis of the
RT extraocular muscles and Marcus Gunn jaw-winking phenomenon.";
RL Arch. Ophthalmol. 123:1254-1259(2005).
RN [28]
RP VARIANTS CFEOM1 THR-356; GLN-944; GLN-954; LEU-954; TRP-954 AND PRO-1008.
RX PubMed=17511870; DOI=10.1186/1471-2156-8-26;
RA Chan W.M., Andrews C., Dragan L., Fredrick D., Armstrong L., Lyons C.,
RA Geraghty M.T., Hunter D.G., Yazdani A., Traboulsi E.I., Pott J.W.,
RA Gutowski N.J., Ellard S., Young E., Hanisch F., Koc F., Schnall B.,
RA Engle E.C.;
RT "Three novel mutations in KIF21A highlight the importance of the third
RT coiled-coil stalk domain in the etiology of CFEOM1.";
RL BMC Genet. 8:26-26(2007).
RN [29]
RP VARIANT CFEOM1 GLU-352.
RX PubMed=24715754;
RA Ali Z., Xing C., Anwar D., Itani K., Weakley D., Gong X., Pascual J.M.,
RA Mootha V.V.;
RT "A novel de novo KIF21A mutation in a patient with congenital fibrosis of
RT the extraocular muscles and Moebius syndrome.";
RL Mol. Vis. 20:368-375(2014).
CC -!- FUNCTION: Microtubule-binding motor protein probably involved in
CC neuronal axonal transport. In vitro, has a plus-end directed motor
CC activity. {ECO:0000250|UniProtKB:Q9QXL2}.
CC -!- SUBUNIT: Interacts (via residues 1146-1167) with KANK1 (via ankyrin
CC repeats 1-5) and KANK2 (via ankyrin repeats 1-5).
CC {ECO:0000269|PubMed:29183992}.
CC -!- INTERACTION:
CC Q7Z4S6; Q9Y6D6: ARFGEF1; NbExp=7; IntAct=EBI-2691397, EBI-1044254;
CC Q7Z4S6; Q14678: KANK1; NbExp=5; IntAct=EBI-2691397, EBI-2556221;
CC Q7Z4S6; Q14678-2: KANK1; NbExp=3; IntAct=EBI-2691397, EBI-6173812;
CC Q7Z4S6-2; Q9Y6D6: ARFGEF1; NbExp=4; IntAct=EBI-6251716, EBI-1044254;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9QXL2}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9QXL2}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9QXL2}. Note=In neurons, localized to axons and
CC dendrites. {ECO:0000250|UniProtKB:Q9QXL2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q7Z4S6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z4S6-2; Sequence=VSP_010870;
CC Name=3;
CC IsoId=Q7Z4S6-3; Sequence=VSP_010871;
CC Name=4;
CC IsoId=Q7Z4S6-4; Sequence=VSP_010872;
CC Name=5;
CC IsoId=Q7Z4S6-5; Sequence=VSP_010870, VSP_046791, VSP_046792;
CC Name=6;
CC IsoId=Q7Z4S6-6; Sequence=VSP_010870, VSP_046790, VSP_046792;
CC -!- DISEASE: Fibrosis of extraocular muscles, congenital, 1 (CFEOM1)
CC [MIM:135700]: A congenital ocular motility disorder marked by
CC restrictive ophthalmoplegia affecting extraocular muscles innervated by
CC the oculomotor and/or trochlear nerves. It is clinically characterized
CC by anchoring of the eyes in downward gaze, ptosis, and backward tilt of
CC the head. Patients affected by congenital fibrosis of extraocular
CC muscles type 1 show an absence of the superior division of the
CC oculomotor nerve (cranial nerve III) and corresponding oculomotor
CC subnuclei. {ECO:0000269|PubMed:14595441, ECO:0000269|PubMed:16157808,
CC ECO:0000269|PubMed:17511870, ECO:0000269|PubMed:24715754}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD42883.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH41430.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAP97680.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA90916.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AY368076; AAR04774.1; -; mRNA.
DR EMBL; AM177179; CAJ45483.1; -; mRNA.
DR EMBL; AF450487; AAP97680.1; ALT_FRAME; mRNA.
DR EMBL; AB290166; BAG06720.1; -; mRNA.
DR EMBL; AC084373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF155117; AAD42883.1; ALT_SEQ; mRNA.
DR EMBL; AK000059; BAA90916.1; ALT_SEQ; mRNA.
DR EMBL; CH471111; EAW57803.1; -; Genomic_DNA.
DR EMBL; BC041430; AAH41430.1; ALT_SEQ; mRNA.
DR EMBL; BC047572; AAH47572.1; -; mRNA.
DR EMBL; BC136414; AAI36415.1; -; mRNA.
DR EMBL; AB051495; BAB21799.2; -; mRNA.
DR EMBL; BX537855; CAD97863.1; -; mRNA.
DR CCDS; CCDS31773.1; -. [Q7Z4S6-2]
DR CCDS; CCDS53774.1; -. [Q7Z4S6-6]
DR CCDS; CCDS53775.1; -. [Q7Z4S6-5]
DR CCDS; CCDS53776.1; -. [Q7Z4S6-1]
DR RefSeq; NP_001166934.1; NM_001173463.1. [Q7Z4S6-5]
DR RefSeq; NP_001166935.1; NM_001173464.1. [Q7Z4S6-1]
DR RefSeq; NP_001166936.1; NM_001173465.1. [Q7Z4S6-6]
DR RefSeq; NP_060111.2; NM_017641.3. [Q7Z4S6-2]
DR RefSeq; XP_005269064.1; XM_005269007.2.
DR RefSeq; XP_005269070.1; XM_005269013.2. [Q7Z4S6-3]
DR PDB; 5D3A; X-ray; 2.50 A; A/B=938-1017.
DR PDB; 5NFD; X-ray; 2.18 A; A/B=938-1017.
DR PDB; 5YBU; X-ray; 1.89 A; B=1146-1167.
DR PDB; 5YBV; X-ray; 2.12 A; C/D=1146-1167.
DR PDB; 7KLJ; X-ray; 1.52 A; A/B=1337-1653.
DR PDBsum; 5D3A; -.
DR PDBsum; 5NFD; -.
DR PDBsum; 5YBU; -.
DR PDBsum; 5YBV; -.
DR PDBsum; 7KLJ; -.
DR AlphaFoldDB; Q7Z4S6; -.
DR SMR; Q7Z4S6; -.
DR BioGRID; 120746; 69.
DR DIP; DIP-56253N; -.
DR IntAct; Q7Z4S6; 51.
DR MINT; Q7Z4S6; -.
DR STRING; 9606.ENSP00000354878; -.
DR iPTMnet; Q7Z4S6; -.
DR PhosphoSitePlus; Q7Z4S6; -.
DR BioMuta; KIF21A; -.
DR DMDM; 50400977; -.
DR EPD; Q7Z4S6; -.
DR jPOST; Q7Z4S6; -.
DR MassIVE; Q7Z4S6; -.
DR MaxQB; Q7Z4S6; -.
DR PaxDb; Q7Z4S6; -.
DR PeptideAtlas; Q7Z4S6; -.
DR PRIDE; Q7Z4S6; -.
DR ProteomicsDB; 25297; -.
DR ProteomicsDB; 25828; -.
DR ProteomicsDB; 69226; -. [Q7Z4S6-1]
DR ProteomicsDB; 69227; -. [Q7Z4S6-2]
DR ProteomicsDB; 69228; -. [Q7Z4S6-3]
DR ProteomicsDB; 69229; -. [Q7Z4S6-4]
DR Antibodypedia; 13055; 58 antibodies from 20 providers.
DR DNASU; 55605; -.
DR Ensembl; ENST00000361418.10; ENSP00000354878.5; ENSG00000139116.19. [Q7Z4S6-1]
DR Ensembl; ENST00000361961.7; ENSP00000354851.3; ENSG00000139116.19. [Q7Z4S6-2]
DR Ensembl; ENST00000541463.6; ENSP00000438075.2; ENSG00000139116.19. [Q7Z4S6-6]
DR Ensembl; ENST00000544797.6; ENSP00000445606.2; ENSG00000139116.19. [Q7Z4S6-5]
DR GeneID; 55605; -.
DR KEGG; hsa:55605; -.
DR MANE-Select; ENST00000361418.10; ENSP00000354878.5; NM_001173464.2; NP_001166935.1.
DR UCSC; uc001rlx.4; human. [Q7Z4S6-1]
DR CTD; 55605; -.
DR DisGeNET; 55605; -.
DR GeneCards; KIF21A; -.
DR GeneReviews; KIF21A; -.
DR HGNC; HGNC:19349; KIF21A.
DR HPA; ENSG00000139116; Tissue enhanced (brain, retina).
DR MalaCards; KIF21A; -.
DR MIM; 135700; phenotype.
DR MIM; 608283; gene.
DR neXtProt; NX_Q7Z4S6; -.
DR OpenTargets; ENSG00000139116; -.
DR Orphanet; 45358; Congenital fibrosis of extraocular muscles.
DR PharmGKB; PA134882934; -.
DR VEuPathDB; HostDB:ENSG00000139116; -.
DR eggNOG; KOG0244; Eukaryota.
DR GeneTree; ENSGT00940000155323; -.
DR HOGENOM; CLU_001485_4_5_1; -.
DR InParanoid; Q7Z4S6; -.
DR OMA; GECTPIG; -.
DR OrthoDB; 390391at2759; -.
DR PhylomeDB; Q7Z4S6; -.
DR TreeFam; TF105224; -.
DR PathwayCommons; Q7Z4S6; -.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q7Z4S6; -.
DR BioGRID-ORCS; 55605; 11 hits in 1075 CRISPR screens.
DR ChiTaRS; KIF21A; human.
DR GeneWiki; KIF21A; -.
DR GenomeRNAi; 55605; -.
DR Pharos; Q7Z4S6; Tbio.
DR PRO; PR:Q7Z4S6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q7Z4S6; protein.
DR Bgee; ENSG00000139116; Expressed in dorsal root ganglion and 193 other tissues.
DR ExpressionAtlas; Q7Z4S6; baseline and differential.
DR Genevisible; Q7Z4S6; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0071532; F:ankyrin repeat binding; IPI:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 3.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Disease variant;
KW Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1674
FT /note="Kinesin-like protein KIF21A"
FT /id="PRO_0000125462"
FT DOMAIN 9..371
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REPEAT 1345..1382
FT /note="WD 1"
FT REPEAT 1385..1423
FT /note="WD 2"
FT REPEAT 1449..1487
FT /note="WD 3"
FT REPEAT 1490..1532
FT /note="WD 4"
FT REPEAT 1541..1578
FT /note="WD 5"
FT REPEAT 1582..1621
FT /note="WD 6"
FT REPEAT 1624..1661
FT /note="WD 7"
FT REGION 556..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1167
FT /note="Interaction with KANK1 and KANK2"
FT /evidence="ECO:0000269|PubMed:29183992"
FT REGION 1170..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 365..575
FT /evidence="ECO:0000255"
FT COILED 931..1019
FT /evidence="ECO:0000255"
FT COILED 1053..1083
FT /evidence="ECO:0000255"
FT COMPBIAS 558..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..635
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1664
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 558..570
FT /note="Missing (in isoform 2, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10508479,
FT ECO:0000303|PubMed:11214970, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT /id="VSP_010870"
FT VAR_SEQ 807..829
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_046790"
FT VAR_SEQ 1107..1113
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046791"
FT VAR_SEQ 1260..1319
FT /note="HSDSGTSEASLSPPSSPPSRPRNELNVFNRLTVSQGNTSVQQDKSDESDSSL
FT SEVHRSSR -> QSDESDSSLSEVH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_010871"
FT VAR_SEQ 1304..1320
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_046792"
FT VAR_SEQ 1315
FT /note="H -> HS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010872"
FT VARIANT 352
FT /note="D -> E (in CFEOM1; de novo mutation)"
FT /evidence="ECO:0000269|PubMed:24715754"
FT /id="VAR_074031"
FT VARIANT 356
FT /note="M -> T (in CFEOM1; dbSNP:rs121912588)"
FT /evidence="ECO:0000269|PubMed:14595441,
FT ECO:0000269|PubMed:17511870"
FT /id="VAR_019399"
FT VARIANT 944
FT /note="E -> Q (in CFEOM1)"
FT /evidence="ECO:0000269|PubMed:17511870"
FT /id="VAR_074032"
FT VARIANT 947
FT /note="M -> R (in CFEOM1; dbSNP:rs121912590)"
FT /evidence="ECO:0000269|PubMed:14595441"
FT /id="VAR_019400"
FT VARIANT 947
FT /note="M -> T (in CFEOM1)"
FT /evidence="ECO:0000269|PubMed:16157808"
FT /id="VAR_027021"
FT VARIANT 947
FT /note="M -> V (in CFEOM1; dbSNP:rs121912589)"
FT /evidence="ECO:0000269|PubMed:14595441"
FT /id="VAR_019401"
FT VARIANT 954
FT /note="R -> L (in CFEOM1)"
FT /evidence="ECO:0000269|PubMed:17511870"
FT /id="VAR_074033"
FT VARIANT 954
FT /note="R -> Q (in CFEOM1; dbSNP:rs121912586)"
FT /evidence="ECO:0000269|PubMed:14595441,
FT ECO:0000269|PubMed:17511870"
FT /id="VAR_019402"
FT VARIANT 954
FT /note="R -> W (in CFEOM1; dbSNP:rs121912585)"
FT /evidence="ECO:0000269|PubMed:14595441,
FT ECO:0000269|PubMed:17511870"
FT /id="VAR_019403"
FT VARIANT 1008
FT /note="A -> P (in CFEOM1)"
FT /evidence="ECO:0000269|PubMed:17511870"
FT /id="VAR_074034"
FT VARIANT 1010
FT /note="I -> T (in CFEOM1; dbSNP:rs121912587)"
FT /evidence="ECO:0000269|PubMed:14595441"
FT /id="VAR_019404"
FT MUTAGEN 1154
FT /note="R->A: Very weak binding affinity for KANK1 and
FT KANK2."
FT /evidence="ECO:0000269|PubMed:29183992"
FT MUTAGEN 1164
FT /note="L->A: Does not bind to KANK1 or KANK2."
FT /evidence="ECO:0000269|PubMed:29183992"
FT CONFLICT 172
FT /note="K -> R (in Ref. 2; CAJ45483)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="R -> G (in Ref. 2; CAJ45483)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="A -> G (in Ref. 2; CAJ45483)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="S -> C (in Ref. 2; CAJ45483)"
FT /evidence="ECO:0000305"
FT CONFLICT 596..597
FT /note="NN -> TQ (in Ref. 3; AAP97680 and 8; AAD42883)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="E -> D (in Ref. 3; AAP97680)"
FT /evidence="ECO:0000305"
FT CONFLICT 801..802
FT /note="DQ -> AP (in Ref. 3; AAP97680)"
FT /evidence="ECO:0000305"
FT CONFLICT 801
FT /note="D -> G (in Ref. 2; CAJ45483)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="E -> G (in Ref. 3; AAP97680)"
FT /evidence="ECO:0000305"
FT CONFLICT 826
FT /note="K -> Q (in Ref. 3; AAP97680)"
FT /evidence="ECO:0000305"
FT CONFLICT 875
FT /note="R -> G (in Ref. 2; CAJ45483)"
FT /evidence="ECO:0000305"
FT CONFLICT 892
FT /note="L -> S (in Ref. 2; CAJ45483)"
FT /evidence="ECO:0000305"
FT CONFLICT 1071
FT /note="Q -> R (in Ref. 2; CAJ45483)"
FT /evidence="ECO:0000305"
FT CONFLICT 1167
FT /note="D -> G (in Ref. 2; CAJ45483)"
FT /evidence="ECO:0000305"
FT CONFLICT 1237
FT /note="E -> D (in Ref. 7; AAI36415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1341
FT /note="H -> N (in Ref. 2; CAJ45483)"
FT /evidence="ECO:0000305"
FT CONFLICT 1378..1379
FT /note="QE -> HR (in Ref. 2; CAJ45483)"
FT /evidence="ECO:0000305"
FT CONFLICT 1429
FT /note="G -> A (in Ref. 2; CAJ45483)"
FT /evidence="ECO:0000305"
FT CONFLICT 1503
FT /note="I -> T (in Ref. 11; CAD97863)"
FT /evidence="ECO:0000305"
FT CONFLICT 1511
FT /note="I -> T (in Ref. 11; CAD97863)"
FT /evidence="ECO:0000305"
FT HELIX 939..973
FT /evidence="ECO:0007829|PDB:5NFD"
FT HELIX 982..1014
FT /evidence="ECO:0007829|PDB:5NFD"
FT HELIX 1153..1155
FT /evidence="ECO:0007829|PDB:5YBU"
FT HELIX 1160..1164
FT /evidence="ECO:0007829|PDB:5YBU"
FT STRAND 1338..1344
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1350..1355
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1357..1364
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1369..1373
FT /evidence="ECO:0007829|PDB:7KLJ"
FT TURN 1374..1376
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1379..1383
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1392..1396
FT /evidence="ECO:0007829|PDB:7KLJ"
FT TURN 1397..1400
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1401..1406
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1409..1414
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1416..1418
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1420..1426
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1431..1434
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1454..1459
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1463..1470
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1473..1478
FT /evidence="ECO:0007829|PDB:7KLJ"
FT TURN 1479..1482
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1483..1488
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1495..1504
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1507..1514
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1519..1525
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1530..1532
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1535..1537
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1546..1552
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1555..1560
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1565..1569
FT /evidence="ECO:0007829|PDB:7KLJ"
FT TURN 1570..1573
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1574..1579
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1582..1585
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1587..1592
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1596..1603
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1606..1612
FT /evidence="ECO:0007829|PDB:7KLJ"
FT TURN 1613..1615
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1618..1623
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1629..1634
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1639..1643
FT /evidence="ECO:0007829|PDB:7KLJ"
FT STRAND 1646..1652
FT /evidence="ECO:0007829|PDB:7KLJ"
SQ SEQUENCE 1674 AA; 187179 MW; 292AFA5F2C0C6F9A CRC64;
MLGAPDESSV RVAVRIRPQL AKEKIEGCHI CTSVTPGEPQ VFLGKDKAFT FDYVFDIDSQ
QEQIYIQCIE KLIEGCFEGY NATVFAYGQT GAGKTYTMGT GFDVNIVEEE LGIISRAVKH
LFKSIEEKKH IAIKNGLPAP DFKVNAQFLE LYNEEVLDLF DTTRDIDAKS KKSNIRIHED
STGGIYTVGV TTRTVNTESE MMQCLKLGAL SRTTASTQMN VQSSRSHAIF TIHVCQTRVC
PQIDADNATD NKIISESAQM NEFETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG
LLALGNVISA LGDKSKRATH VPYRDSKLTR LLQDSLGGNS QTIMIACVSP SDRDFMETLN
TLKYANRARN IKNKVMVNQD RASQQINALR SEITRLQMEL MEYKTGKRII DEEGVESIND
MFHENAMLQT ENNNLRVRIK AMQETVDALR SRITQLVSDQ ANHVLARAGE GNEEISNMIH
SYIKEIEDLR AKLLESEAVN ENLRKNLTRA TARAPYFSGS STFSPTILSS DKETIEIIDL
AKKDLEKLKR KEKRKKKRLQ KLEESNREER SVAGKEDNTD TDQEKKEEKG VSERENNELE
VEESQEVSDH EDEEEEEEEE EDDIDGGESS DESDSESDEK ANYQADLANI TCEIAIKQKL
IDELENSQKR LQTLKKQYEE KLMMLQHKIR DTQLERDQVL QNLGSVESYS EEKAKKVRSE
YEKKLQAMNK ELQRLQAAQK EHARLLKNQS QYEKQLKKLQ QDVMEMKKTK VRLMKQMKEE
QEKARLTESR RNREIAQLKK DQRKRDHQLR LLEAQKRNQE VVLRRKTEEV TALRRQVRPM
SDKVAGKVTR KLSSSDAPAQ DTGSSAAAVE TDASRTGAQQ KMRIPVARVQ ALPTPATNGN
RKKYQRKGLT GRVFISKTAR MKWQLLERRV TDIIMQKMTI SNMEADMNRL LKQREELTKR
REKLSKRREK IVKENGEGDK NVANINEEME SLTANIDYIN DSISDCQANI MQMEEAKEEG
ETLDVTAVIN ACTLTEARYL LDHFLSMGIN KGLQAAQKEA QIKVLEGRLK QTEITSATQN
QLLFHMLKEK AELNPELDAL LGHALQDLDS VPLENVEDST DEDAPLNSPG SEGSTLSSDL
MKLCGEVKPK NKARRRTTTQ MELLYADSSE LASDTSTGDA SLPGPLTPVA EGQEIGMNTE
TSGTSAREKE LSPPPGLPSK IGSISRQSSL SEKKIPEPSP VTRRKAYEKA EKSKAKEQKH
SDSGTSEASL SPPSSPPSRP RNELNVFNRL TVSQGNTSVQ QDKSDESDSS LSEVHRSSRR
GIINPFPASK GIRAFPLQCI HIAEGHTKAV LCVDSTDDLL FTGSKDRTCK VWNLVTGQEI
MSLGGHPNNV VSVKYCNYTS LVFTVSTSYI KVWDIRDSAK CIRTLTSSGQ VTLGDACSAS
TSRTVAIPSG ENQINQIALN PTGTFLYAAS GNAVRMWDLK RFQSTGKLTG HLGPVMCLTV
DQISSGQDLI ITGSKDHYIK MFDVTEGALG TVSPTHNFEP PHYDGIEALT IQGDNLFSGS
RDNGIKKWDL TQKDLLQQVP NAHKDWVCAL GVVPDHPVLL SGCRGGILKV WNMDTFMPVG
EMKGHDSPIN AICVNSTHIF TAADDRTVRI WKARNLQDGQ ISDTGDLGED IASN
