CEP55_HUMAN
ID CEP55_HUMAN Reviewed; 464 AA.
AC Q53EZ4; B2RDG8; D3DR37; Q32WF5; Q3MV20; Q5VY28; Q6N034; Q96H32; Q9NVS7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Centrosomal protein of 55 kDa {ECO:0000312|HGNC:HGNC:1161};
DE Short=Cep55;
DE AltName: Full=Up-regulated in colon cancer 6;
GN Name=CEP55 {ECO:0000312|HGNC:HGNC:1161};
GN Synonyms=C10orf3 {ECO:0000312|HGNC:HGNC:1161}, URCC6;
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), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, HOMODIMERIZATION, AND VARIANTS GLN-57 AND ALA-99.
RX PubMed=16406728; DOI=10.1016/j.ygeno.2005.11.006;
RA Martinez-Garay I., Rustom A., Gerdes H.-H., Kutsche K.;
RT "The novel centrosomal associated protein CEP55 is present in the spindle
RT midzone and the midbody.";
RL Genomics 87:243-253(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-99.
RA Shimokawa T., Furukawa Y., Sakai M., Nakamura Y.;
RT "Cloning and characterization of URCC6, a novel gene up-regulated in colon
RT cancer.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 33-464 (ISOFORM 2), AND VARIANTS GLN-57; ALA-99 AND
RP LEU-378.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-99 AND
RP LEU-378.
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-99.
RC TISSUE=Esophageal carcinoma;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ALA-99 AND
RP LEU-378.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-99 AND
RP LEU-378.
RC TISSUE=Muscle;
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PLK1;
RP AKAP9 AND PCNT, PHOSPHORYLATION AT SER-425; SER-428 AND SER-436,
RP MUTAGENESIS OF SER-396; SER-425; SER-428 AND SER-436, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=16198290; DOI=10.1016/j.devcel.2005.09.003;
RA Fabbro M., Zhou B.-B., Takahashi M., Sarcevic B., Lal P., Graham M.E.,
RA Gabrielli B.G., Robinson P.J., Nigg E.A., Ono Y., Khanna K.K.;
RT "Cdk1/Erk2- and Plk1-dependent phosphorylation of a centrosome protein,
RT Cep55, is required for its recruitment to midbody and cytokinesis.";
RL Dev. Cell 9:477-488(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY
RP 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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, SELF-ASSOCIATION, AND INTERACTION WITH
RP PDCD6IP; TSG101; MVB12A; VPS37B; VPS37C AND VPS28.
RX PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
RA Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K.,
RA Sundquist W.I.;
RT "Human ESCRT and ALIX proteins interact with proteins of the midbody and
RT function in cytokinesis.";
RL EMBO J. 26:4215-4227(2007).
RN [12]
RP SELF-ASSOCIATION, INTERACTION WITH PDCD6IP AND TSG101, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17556548; DOI=10.1126/science.1143422;
RA Carlton J.G., Martin-Serrano J.;
RT "Parallels between cytokinesis and retroviral budding: a role for the ESCRT
RT machinery.";
RL Science 316:1908-1912(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP INTERACTION WITH PDCD6IP, AND SUBCELLULAR LOCATION.
RX PubMed=18641129; DOI=10.1073/pnas.0802008105;
RA Carlton J.G., Agromayor M., Martin-Serrano J.;
RT "Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1
RT release.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10541-10546(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-428; THR-430 AND
RP SER-436, 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 [16]
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP SUBCELLULAR LOCATION.
RX PubMed=21310966; DOI=10.1126/science.1201847;
RA Guizetti J., Schermelleh L., Maentler J., Maar S., Poser I., Leonhardt H.,
RA Mueller-Reichert T., Gerlich D.W.;
RT "Cortical constriction during abscission involves helices of ESCRT-III-
RT dependent filaments.";
RL Science 331:1616-1620(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND SER-436, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 160-217 IN COMPLEX WITH PDCD6IP,
RP INTERACTION WITH TSG101, AND MUTAGENESIS OF TRP-184; TYR-187; ASP-188;
RP ARG-191 AND GLU-192.
RX PubMed=18948538; DOI=10.1126/science.1162042;
RA Lee H.H., Elia N., Ghirlando R., Lippincott-Schwartz J., Hurley J.H.;
RT "Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in
RT CEP55.";
RL Science 322:576-580(2008).
RN [22]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-99, AND IDENTIFICATION BY MASS
RP 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 [23]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-99, AND IDENTIFICATION BY MASS
RP 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 [24]
RP VARIANT MARCH 86-ARG--LYS-464 DEL, TISSUE SPECIFICITY, AND INVOLVEMENT IN
RP MARCH.
RX PubMed=28295209; DOI=10.1111/cge.13012;
RA Bondeson M.L., Ericson K., Gudmundsson S., Ameur A., Ponten F.,
RA Wesstroem J., Frykholm C., Wilbe M.;
RT "A nonsense mutation in CEP55 defines a new locus for a Meckel-like
RT syndrome, an autosomal recessive lethal fetal ciliopathy.";
RL Clin. Genet. 92:510-516(2017).
RN [25]
RP VARIANT MARCH 425-SER--LYS-464 DEL, CHARACTERIZATION OF VARIANT MARCH
RP 425-SER--LYS-464 DEL, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND CHARACTERIZATION OF VARIANTS GLN-57 AND LEU-378.
RX PubMed=28264986; DOI=10.1136/jmedgenet-2016-104296;
RG FORGE Canada Consortium;
RG Canadian Rare Diseases: Models & Mechanisms Network,;
RA Frosk P., Arts H.H., Philippe J., Gunn C.S., Brown E.L., Chodirker B.,
RA Simard L., Majewski J., Fahiminiya S., Russell C., Liu Y.P., Hegele R.,
RA Katsanis N., Goerz C., Del Bigio M.R., Davis E.E.;
RT "A truncating mutation in CEP55 is the likely cause of MARCH, a novel
RT syndrome affecting neuronal mitosis.";
RL J. Med. Genet. 54:490-501(2017).
CC -!- FUNCTION: Plays a role in mitotic exit and cytokinesis
CC (PubMed:16198290, PubMed:17853893). Recruits PDCD6IP and TSG101 to
CC midbody during cytokinesis. Required for successful completion of
CC cytokinesis (PubMed:17853893). Not required for microtubule nucleation
CC (PubMed:16198290). Plays a role in the development of the brain and
CC kidney (PubMed:28264986). {ECO:0000269|PubMed:16198290,
CC ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:28264986}.
CC -!- SUBUNIT: Homodimer (PubMed:16406728). Interacts (phosphorylated on Ser-
CC 425 and Ser-428) with PLK1 (PubMed:16198290). Interacts with AKAP9/CG-
CC NAP; the interaction occurs in interphase and is lost upon mitotic
CC entry (PubMed:16198290). Interacts with PCNT/Kendrin; the interaction
CC occurs in interphase and is lost upon mitotic entry (PubMed:16198290).
CC Directly interacts with PDCD6IP; this interaction is required for
CC PDCD6IP targeting to the midbody; CEP55 binds PDCD6IP in a 2:1
CC stoichiometry; PDCD6IP competes with TSG101 for the same binding site
CC (PubMed:17853893, PubMed:17556548, PubMed:18641129, PubMed:18948538).
CC Interacts with TSG101; TSG101 competes with PDCD6IP for the same
CC binding site; interaction is required for cytokinesis but not for viral
CC budding (PubMed:17853893, PubMed:17556548, PubMed:18948538). Interacts
CC with MVB12A, VPS37B, VPS37C and VPS28 (PubMed:17853893).
CC {ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:16406728,
CC ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893,
CC ECO:0000269|PubMed:18641129, ECO:0000269|PubMed:18948538}.
CC -!- INTERACTION:
CC Q53EZ4; P50995: ANXA11; NbExp=8; IntAct=EBI-747776, EBI-715243;
CC Q53EZ4; Q5T0G8: ANXA11; NbExp=3; IntAct=EBI-747776, EBI-10245225;
CC Q53EZ4; D3DTR7: ARHGEF15; NbExp=3; IntAct=EBI-747776, EBI-10176602;
CC Q53EZ4; O94989: ARHGEF15; NbExp=6; IntAct=EBI-747776, EBI-740691;
CC Q53EZ4; Q9NX04: C1orf109; NbExp=6; IntAct=EBI-747776, EBI-8643161;
CC Q53EZ4; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-747776, EBI-747505;
CC Q53EZ4; Q8N187: CARF; NbExp=3; IntAct=EBI-747776, EBI-745541;
CC Q53EZ4; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-747776, EBI-11524851;
CC Q53EZ4; Q6UXH8: CCBE1; NbExp=3; IntAct=EBI-747776, EBI-3923278;
CC Q53EZ4; Q6UXH8-3: CCBE1; NbExp=3; IntAct=EBI-747776, EBI-12013534;
CC Q53EZ4; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-747776, EBI-744556;
CC Q53EZ4; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-747776, EBI-10175300;
CC Q53EZ4; Q16543: CDC37; NbExp=3; IntAct=EBI-747776, EBI-295634;
CC Q53EZ4; O75419: CDC45; NbExp=7; IntAct=EBI-747776, EBI-374969;
CC Q53EZ4; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-747776, EBI-747776;
CC Q53EZ4; Q8IYX8: CEP57L1; NbExp=4; IntAct=EBI-747776, EBI-1104570;
CC Q53EZ4; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-747776, EBI-10181988;
CC Q53EZ4; P27658: COL8A1; NbExp=3; IntAct=EBI-747776, EBI-747133;
CC Q53EZ4; P50570-2: DNM2; NbExp=3; IntAct=EBI-747776, EBI-10968534;
CC Q53EZ4; O60941: DTNB; NbExp=3; IntAct=EBI-747776, EBI-740402;
CC Q53EZ4; O60941-5: DTNB; NbExp=3; IntAct=EBI-747776, EBI-11984733;
CC Q53EZ4; Q8N9N8: EIF1AD; NbExp=5; IntAct=EBI-747776, EBI-750700;
CC Q53EZ4; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-747776, EBI-744099;
CC Q53EZ4; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-747776, EBI-7225287;
CC Q53EZ4; Q86YD7: FAM90A1; NbExp=6; IntAct=EBI-747776, EBI-6658203;
CC Q53EZ4; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-747776, EBI-10244131;
CC Q53EZ4; P51116: FXR2; NbExp=3; IntAct=EBI-747776, EBI-740459;
CC Q53EZ4; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-747776, EBI-11110431;
CC Q53EZ4; Q0D2H9: GOLGA8DP; NbExp=3; IntAct=EBI-747776, EBI-10181276;
CC Q53EZ4; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-747776, EBI-2514791;
CC Q53EZ4; O14964: HGS; NbExp=5; IntAct=EBI-747776, EBI-740220;
CC Q53EZ4; O75031: HSF2BP; NbExp=3; IntAct=EBI-747776, EBI-7116203;
CC Q53EZ4; P42858: HTT; NbExp=9; IntAct=EBI-747776, EBI-466029;
CC Q53EZ4; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-747776, EBI-2556193;
CC Q53EZ4; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-747776, EBI-2125614;
CC Q53EZ4; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-747776, EBI-14069005;
CC Q53EZ4; O14901: KLF11; NbExp=3; IntAct=EBI-747776, EBI-948266;
CC Q53EZ4; P56470: LGALS4; NbExp=3; IntAct=EBI-747776, EBI-720805;
CC Q53EZ4; Q53EV4: LRRC23; NbExp=3; IntAct=EBI-747776, EBI-13435308;
CC Q53EZ4; Q8NDC0: MAPK1IP1L; NbExp=3; IntAct=EBI-747776, EBI-741424;
CC Q53EZ4; P55081: MFAP1; NbExp=6; IntAct=EBI-747776, EBI-1048159;
CC Q53EZ4; Q5JRA6-2: MIA3; NbExp=4; IntAct=EBI-747776, EBI-10244342;
CC Q53EZ4; Q15014: MORF4L2; NbExp=6; IntAct=EBI-747776, EBI-399257;
CC Q53EZ4; Q96HA8: NTAQ1; NbExp=5; IntAct=EBI-747776, EBI-741158;
CC Q53EZ4; Q8WUM4: PDCD6IP; NbExp=16; IntAct=EBI-747776, EBI-310624;
CC Q53EZ4; Q9UBV8: PEF1; NbExp=6; IntAct=EBI-747776, EBI-724639;
CC Q53EZ4; Q13526: PIN1; NbExp=3; IntAct=EBI-747776, EBI-714158;
CC Q53EZ4; Q3KR16: PLEKHG6; NbExp=8; IntAct=EBI-747776, EBI-10240979;
CC Q53EZ4; Q6PIY2: POLM; NbExp=6; IntAct=EBI-747776, EBI-10253863;
CC Q53EZ4; Q96T49: PPP1R16B; NbExp=5; IntAct=EBI-747776, EBI-10293968;
CC Q53EZ4; Q9H3S7: PTPN23; NbExp=3; IntAct=EBI-747776, EBI-724478;
CC Q53EZ4; Q2TAK8-2: PWWP3A; NbExp=3; IntAct=EBI-747776, EBI-10239402;
CC Q53EZ4; Q96I25: RBM17; NbExp=8; IntAct=EBI-747776, EBI-740272;
CC Q53EZ4; Q9NW64: RBM22; NbExp=6; IntAct=EBI-747776, EBI-2602260;
CC Q53EZ4; Q9P2K3: RCOR3; NbExp=3; IntAct=EBI-747776, EBI-743428;
CC Q53EZ4; O00560: SDCBP; NbExp=6; IntAct=EBI-747776, EBI-727004;
CC Q53EZ4; P14678-2: SNRPB; NbExp=3; IntAct=EBI-747776, EBI-372475;
CC Q53EZ4; Q13573: SNW1; NbExp=3; IntAct=EBI-747776, EBI-632715;
CC Q53EZ4; O75177-5: SS18L1; NbExp=3; IntAct=EBI-747776, EBI-12035119;
CC Q53EZ4; Q9Y2D8: SSX2IP; NbExp=5; IntAct=EBI-747776, EBI-2212028;
CC Q53EZ4; P56279: TCL1A; NbExp=6; IntAct=EBI-747776, EBI-749995;
CC Q53EZ4; D3DUQ6: TEAD4; NbExp=3; IntAct=EBI-747776, EBI-10176734;
CC Q53EZ4; Q15561: TEAD4; NbExp=5; IntAct=EBI-747776, EBI-747736;
CC Q53EZ4; Q8IWB6: TEX14; NbExp=5; IntAct=EBI-747776, EBI-6674697;
CC Q53EZ4; Q92734: TFG; NbExp=6; IntAct=EBI-747776, EBI-357061;
CC Q53EZ4; O14656-2: TOR1A; NbExp=3; IntAct=EBI-747776, EBI-25847109;
CC Q53EZ4; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-747776, EBI-11952721;
CC Q53EZ4; O14773: TPP1; NbExp=3; IntAct=EBI-747776, EBI-2800203;
CC Q53EZ4; Q99816: TSG101; NbExp=24; IntAct=EBI-747776, EBI-346882;
CC Q53EZ4; A5D8V6: VPS37C; NbExp=8; IntAct=EBI-747776, EBI-2559305;
CC Q53EZ4; Q9Y3C0: WASHC3; NbExp=7; IntAct=EBI-747776, EBI-712969;
CC Q53EZ4; Q96MX3: ZNF48; NbExp=3; IntAct=EBI-747776, EBI-12006434;
CC Q53EZ4; A8K9C1; NbExp=3; IntAct=EBI-747776, EBI-10174800;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28264986}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000269|PubMed:16198290}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:16198290}. Cleavage furrow
CC {ECO:0000269|PubMed:16198290}. Midbody, Midbody ring
CC {ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:17853893,
CC ECO:0000269|PubMed:18641129, ECO:0000269|PubMed:21310966,
CC ECO:0000269|PubMed:28264986}. Note=Present at the centrosomes at
CC interphase. A small portion is associated preferentially with the
CC mother centriole, whereas the majority localizes to the pericentriolar
CC material. During mitosis, loses affinity for the centrosome at the
CC onset of prophase and diffuses throughout the cell. This dissociation
CC from the centrosome is phosphorylation-dependent. May remain localized
CC at the centrosome during mitosis in certain cell types. Appears at the
CC cleavage furrow in late anaphase and in the midbody in cytokinesis.
CC {ECO:0000269|PubMed:16198290}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q53EZ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53EZ4-2; Sequence=VSP_014750, VSP_014751;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic brain (PubMed:28264986).
CC Expressed in fetal brain ganglionic eminence, kidney tubules and
CC multinucleate neurons in the temporal cortex (PubMed:28264986).
CC Expressed in adult brain, cerebellum, kidney tubules, intestine and
CC muscles (at protein level) (PubMed:28295209, PubMed:28264986). Widely
CC expressed, mostly in proliferative tissues. Highly expressed in testis.
CC Intermediate levels in adult and fetal thymus, as well as in various
CC cancer cell lines. Low levels in different parts of the digestive
CC tract, bone marrow, lymph nodes, placenta, fetal heart and fetal
CC spleen. Hardly detected in brain. {ECO:0000269|PubMed:16198290,
CC ECO:0000269|PubMed:16406728, ECO:0000269|PubMed:28264986,
CC ECO:0000269|PubMed:28295209}.
CC -!- PTM: There is a hierachy of phosphorylation, where both Ser-425 and
CC Ser-428 are phosphorylated at the onset of mitosis, prior to Ser-436.
CC Phosphorylation at Ser-425 and Ser-428 is required for dissociation
CC from the centrosome at the G2/M boundary. Phosphorylation at the 3
CC sites, Ser-425, Ser-428 and Ser-436, is required for protein function
CC at the final stages of cell division to complete cytokinesis
CC successfully. {ECO:0000269|PubMed:16198290}.
CC -!- DISEASE: Multinucleated neurons, anhydramnios, renal dysplasia,
CC cerebellar hypoplasia and hydranencephaly (MARCH) [MIM:236500]: An
CC autosomal recessive, congenital disease characterized by severe
CC hydranencephaly with multinucleated neurons, renal aplasia or
CC dysplasia, and hypoplastic kidneys. Hydranencephaly is an anomaly
CC leading to replacement of the cerebral hemispheres with a fluid-filled
CC cyst. MARCH results in death in utero or in the perinatal period.
CC {ECO:0000269|PubMed:28264986, ECO:0000269|PubMed:28295209}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91670.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY788918; AAX14687.1; -; mRNA.
DR EMBL; AB091343; BAE45243.1; -; mRNA.
DR EMBL; AK001402; BAA91670.1; ALT_INIT; mRNA.
DR EMBL; AK315536; BAG37915.1; -; mRNA.
DR EMBL; AK223495; BAD97215.1; -; mRNA.
DR EMBL; BX640718; CAE45837.1; -; mRNA.
DR EMBL; AL356214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW50071.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW50072.1; -; Genomic_DNA.
DR EMBL; BC008947; AAH08947.1; -; mRNA.
DR CCDS; CCDS7428.1; -. [Q53EZ4-1]
DR RefSeq; NP_001120654.1; NM_001127182.1. [Q53EZ4-1]
DR RefSeq; NP_060601.3; NM_018131.4. [Q53EZ4-1]
DR PDB; 3E1R; X-ray; 2.00 A; A/B=160-217.
DR PDB; 3WUT; X-ray; 2.30 A; A/B/D/E/G/H/J/K=160-217.
DR PDB; 3WUU; X-ray; 2.90 A; A/B/D/E/G/H/J/K=160-217.
DR PDB; 3WUV; X-ray; 2.79 A; A/B/D/E/G/H/J/K/M/N/P/Q=160-217.
DR PDBsum; 3E1R; -.
DR PDBsum; 3WUT; -.
DR PDBsum; 3WUU; -.
DR PDBsum; 3WUV; -.
DR AlphaFoldDB; Q53EZ4; -.
DR SMR; Q53EZ4; -.
DR BioGRID; 120465; 245.
DR CORUM; Q53EZ4; -.
DR DIP; DIP-44581N; -.
DR ELM; Q53EZ4; -.
DR IntAct; Q53EZ4; 144.
DR MINT; Q53EZ4; -.
DR STRING; 9606.ENSP00000360540; -.
DR iPTMnet; Q53EZ4; -.
DR PhosphoSitePlus; Q53EZ4; -.
DR BioMuta; CEP55; -.
DR DMDM; 296439403; -.
DR EPD; Q53EZ4; -.
DR jPOST; Q53EZ4; -.
DR MassIVE; Q53EZ4; -.
DR MaxQB; Q53EZ4; -.
DR PaxDb; Q53EZ4; -.
DR PeptideAtlas; Q53EZ4; -.
DR PRIDE; Q53EZ4; -.
DR ProteomicsDB; 62452; -. [Q53EZ4-1]
DR ProteomicsDB; 62453; -. [Q53EZ4-2]
DR Antibodypedia; 30468; 327 antibodies from 32 providers.
DR DNASU; 55165; -.
DR Ensembl; ENST00000371485.8; ENSP00000360540.3; ENSG00000138180.16. [Q53EZ4-1]
DR GeneID; 55165; -.
DR KEGG; hsa:55165; -.
DR MANE-Select; ENST00000371485.8; ENSP00000360540.3; NM_018131.5; NP_060601.4.
DR UCSC; uc001kiq.4; human. [Q53EZ4-1]
DR CTD; 55165; -.
DR DisGeNET; 55165; -.
DR GeneCards; CEP55; -.
DR HGNC; HGNC:1161; CEP55.
DR HPA; ENSG00000138180; Tissue enhanced (lymphoid tissue, testis).
DR MalaCards; CEP55; -.
DR MIM; 236500; phenotype.
DR MIM; 610000; gene.
DR neXtProt; NX_Q53EZ4; -.
DR OpenTargets; ENSG00000138180; -.
DR Orphanet; 500135; Multinucleated neurons-anhydramnios-renal dysplasia-cerebellar hypoplasia-hydranencephaly syndrome.
DR PharmGKB; PA25475; -.
DR VEuPathDB; HostDB:ENSG00000138180; -.
DR eggNOG; ENOG502QTDI; Eukaryota.
DR GeneTree; ENSGT00510000047961; -.
DR HOGENOM; CLU_047132_0_0_1; -.
DR InParanoid; Q53EZ4; -.
DR OMA; KHSSCLD; -.
DR OrthoDB; 850483at2759; -.
DR PhylomeDB; Q53EZ4; -.
DR TreeFam; TF331107; -.
DR PathwayCommons; Q53EZ4; -.
DR SignaLink; Q53EZ4; -.
DR SIGNOR; Q53EZ4; -.
DR BioGRID-ORCS; 55165; 193 hits in 1085 CRISPR screens.
DR ChiTaRS; CEP55; human.
DR EvolutionaryTrace; Q53EZ4; -.
DR GeneWiki; CEP55; -.
DR GenomeRNAi; 55165; -.
DR Pharos; Q53EZ4; Tbio.
DR PRO; PR:Q53EZ4; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q53EZ4; protein.
DR Bgee; ENSG00000138180; Expressed in ventricular zone and 125 other tissues.
DR ExpressionAtlas; Q53EZ4; baseline and differential.
DR Genevisible; Q53EZ4; HS.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:1904888; P:cranial skeletal system development; IMP:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
DR GO; GO:0061952; P:midbody abscission; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IGI:MGI.
DR GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IEA:InterPro.
DR InterPro; IPR038926; CEP55.
DR InterPro; IPR022008; EABR.
DR PANTHER; PTHR31838; PTHR31838; 1.
DR Pfam; PF12180; EABR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Developmental protein; Disease variant; Mitosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..464
FT /note="Centrosomal protein of 55 kDa"
FT /id="PRO_0000089777"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..236
FT /note="Interaction with TSG101"
FT REGION 160..214
FT /note="Interaction with PDCD6IP"
FT REGION 355..464
FT /note="Required for localization to the interphase
FT centrosome and to the midbody during cytokinesis"
FT /evidence="ECO:0000269|PubMed:16198290"
FT COILED 22..186
FT /evidence="ECO:0000255"
FT COILED 238..337
FT /evidence="ECO:0000255"
FT COILED 374..403
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BT07"
FT MOD_RES 425
FT /note="Phosphoserine; by CDK1 and MAPK1"
FT /evidence="ECO:0000269|PubMed:16198290,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976"
FT MOD_RES 428
FT /note="Phosphoserine; by CDK1 and MAPK1"
FT /evidence="ECO:0000269|PubMed:16198290,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 436
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:16198290,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 389..400
FT /note="NQITQLESLKQL -> KNNTVGILETAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014750"
FT VAR_SEQ 401..464
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014751"
FT VARIANT 57
FT /note="H -> Q (no effect on protein localization to midbody
FT ring; dbSNP:rs3740370)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16406728, ECO:0000269|PubMed:28264986"
FT /id="VAR_026559"
FT VARIANT 86..464
FT /note="Missing (in MARCH)"
FT /evidence="ECO:0000269|PubMed:28295209"
FT /id="VAR_079363"
FT VARIANT 99
FT /note="T -> A (in dbSNP:rs7080916)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16406728,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21269460"
FT /id="VAR_022996"
FT VARIANT 236
FT /note="C -> R (in dbSNP:rs7072484)"
FT /id="VAR_056791"
FT VARIANT 378
FT /note="H -> L (no effect on protein localization to midbody
FT ring; rescues craniofacial development when expressed in a
FT zebrafish heterologous system; dbSNP:rs2293277)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:28264986,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.7"
FT /id="VAR_022997"
FT VARIANT 425..464
FT /note="Missing (in MARCH; loss of protein localization to
FT midbody ring; loss of function; fails to rescue
FT craniofacial development when expressed in a zebrafish
FT heterologous system)"
FT /evidence="ECO:0000269|PubMed:28264986"
FT /id="VAR_079364"
FT MUTAGEN 184
FT /note="W->A: Abolishes interaction with PDCD6IP."
FT /evidence="ECO:0000269|PubMed:18948538"
FT MUTAGEN 187
FT /note="Y->A: Abolishes interaction with PDCD6IP."
FT /evidence="ECO:0000269|PubMed:18948538"
FT MUTAGEN 188
FT /note="D->A: Diminishes interaction with PDCD6IP."
FT /evidence="ECO:0000269|PubMed:18948538"
FT MUTAGEN 191
FT /note="R->A: Abolishes interaction with PDCD6IP."
FT /evidence="ECO:0000269|PubMed:18948538"
FT MUTAGEN 192
FT /note="E->A: Abolishes interaction with PDCD6IP."
FT /evidence="ECO:0000269|PubMed:18948538"
FT MUTAGEN 396
FT /note="S->A: No effect on phosphorylation in mitotic
FT cells."
FT /evidence="ECO:0000269|PubMed:16198290"
FT MUTAGEN 425
FT /note="S->A: Partial loss of phosphorylation in mitotic
FT cells. Complete loss of phosphorylation in mitotic cells;
FT when associated with A-428. Remains associated with the
FT centrosome throughout mitosis; when associated with A-428.
FT Arrests mitotic cells at the midbody stage; when associated
FT with A-428 and A-436."
FT /evidence="ECO:0000269|PubMed:16198290"
FT MUTAGEN 428
FT /note="S->A: Partial loss of phosphorylation in mitotic
FT cells. Complete loss of phosphorylation in mitotic cells;
FT when associated with A-425. Remains associated with the
FT centrosome throughout mitosis; when associated with A-425.
FT Arrests mitotic cells at the midbody stage; when associated
FT with A-425 and A-436."
FT /evidence="ECO:0000269|PubMed:16198290"
FT MUTAGEN 436
FT /note="S->A: No effect on phosphorylation in mitotic cells.
FT Arrests mitotic cells at the midbody stage; when associated
FT with A-425 and A-428."
FT /evidence="ECO:0000269|PubMed:16198290"
FT CONFLICT 155
FT /note="V -> A (in Ref. 4; BAD97215)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="E -> G (in Ref. 4; BAD97215)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="R -> G (in Ref. 5; CAE45837)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="F -> S (in Ref. 1; AAX14687 and 3; BAA91670)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="E -> G (in Ref. 1; AAX14687)"
FT /evidence="ECO:0000305"
FT HELIX 166..209
FT /evidence="ECO:0007829|PDB:3E1R"
SQ SEQUENCE 464 AA; 54178 MW; A652F86EBCE46A51 CRC64;
MSSRSTKDLI KSKWGSKPSN SKSETTLEKL KGEIAHLKTS VDEITSGKGK LTDKERHRLL
EKIRVLEAEK EKNAYQLTEK DKEIQRLRDQ LKARYSTTTL LEQLEETTRE GERREQVLKA
LSEEKDVLKQ QLSAATSRIA ELESKTNTLR LSQTVAPNCF NSSINNIHEM EIQLKDALEK
NQQWLVYDQQ REVYVKGLLA KIFELEKKTE TAAHSLPQQT KKPESEGYLQ EEKQKCYNDL
LASAKKDLEV ERQTITQLSF ELSEFRRKYE ETQKEVHNLN QLLYSQRRAD VQHLEDDRHK
TEKIQKLREE NDIARGKLEE EKKRSEELLS QVQFLYTSLL KQQEEQTRVA LLEQQMQACT
LDFENEKLDR QHVQHQLHVI LKELRKARNQ ITQLESLKQL HEFAITEPLV TFQGETENRE
KVAASPKSPT AALNESLVEC PKCNIQYPAT EHRDLLVHVE YCSK
