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Centrosomal protein of 164 kDa (Cep164)

 CE164_HUMAN             Reviewed;        1460 AA.
Q9UPV0; Q6PKH9; Q7Z2X9; Q9NVS0; Q9UFJ6;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 3.
28-FEB-2018, entry version 134.
RecName: Full=Centrosomal protein of 164 kDa;
Short=Cep164;
Name=CEP164; Synonyms=KIAA1052, NPHP15;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=17954613; DOI=10.1083/jcb.200707181;
Graser S., Stierhof Y.-D., Lavoie S.B., Gassner O.S., Lamla S.,
Le Clech M., Nigg E.A.;
"Cep164, a novel centriole appendage protein required for primary
cilium formation.";
J. Cell Biol. 179:321-330(2007).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
ATM; ATR; ATRIP AND MDC1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
SER-186, AND MUTAGENESIS OF SER-186.
PubMed=18283122; DOI=10.1101/gad.1627708;
Sivasubramaniam S., Sun X., Pan Y.R., Wang S., Lee E.Y.;
"Cep164 is a mediator protein required for the maintenance of genomic
stability through modulation of MDC1, RPA, and CHK1.";
Genes Dev. 22:587-600(2008).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-116 (ISOFORMS 1/2).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 868-1460 (ISOFORM 1), AND
VARIANTS SER-988 AND ARG-1119.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1038-1460 (ISOFORM 1), AND
VARIANT ARG-1119.
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[9]
INTERACTION WITH XPA, AND SUBCELLULAR LOCATION.
PubMed=19197159; DOI=10.4161/cc.8.4.7844;
Pan Y.R., Lee E.Y.;
"UV-dependent interaction between Cep164 and XPA mediates localization
of Cep164 at sites of DNA damage and UV sensitivity.";
Cell Cycle 8:655-664(2009).
[10]
SUBCELLULAR LOCATION.
PubMed=21976302; DOI=10.1002/cm.20536;
Sillibourne J.E., Specht C.G., Izeddin I., Hurbain I., Tran P.,
Triller A., Darzacq X., Dahan M., Bornens M.;
"Assessing the localization of centrosomal proteins by PALM/STORM
nanoscopy.";
Cytoskeleton 68:619-627(2011).
[11]
SUBCELLULAR LOCATION, INTERACTION WITH CCDC92; TTBK2; NPHP3; NPHP4 AND
DVL3, AND VARIANTS NPHP15 PRO-11 AND TRP-93.
PubMed=22863007; DOI=10.1016/j.cell.2012.06.028;
Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G.,
Wang H., Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G.,
Hong C.J., Hamilton B.A., Cervenka I., Ganji R.S., Bryja V.,
Arts H.H., van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R.,
Husson H., Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L.,
Sayer J.A., Schermer B., Liebau M.C., Benzing T., Le Corre S.,
Drummond I., Janssen S., Allen S.J., Natarajan S., O'Toole J.F.,
Attanasio M., Saunier S., Antignac C., Koenekoop R.K., Ren H.,
Lopez I., Nayir A., Stoetzel C., Dollfus H., Massoudi R.,
Gleeson J.G., Andreoli S.P., Doherty D.G., Lindstrad A., Golzio C.,
Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A., Lewis R.A.,
Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R.,
Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J.,
Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A.,
Hildebrandt F.;
"Exome capture reveals ZNF423 and CEP164 mutations, linking renal
ciliopathies to DNA damage response signaling.";
Cell 150:533-548(2012).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23348840; DOI=10.1101/gad.207043.112;
Tanos B.E., Yang H.J., Soni R., Wang W.J., Macaluso F.P., Asara J.M.,
Tsou M.F.;
"Centriole distal appendages promote membrane docking, leading to
cilia initiation.";
Genes Dev. 27:163-168(2013).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201; SER-566; SER-1386;
SER-1388 AND SER-1443, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
INTERACTION WITH CEP83, AND SUBCELLULAR LOCATION.
PubMed=23530209; DOI=10.1073/pnas.1220927110;
Joo K., Kim C.G., Lee M.S., Moon H.Y., Lee S.H., Kim M.J., Kweon H.S.,
Park W.Y., Kim C.H., Gleeson J.G., Kim J.;
"CCDC41 is required for ciliary vesicle docking to the mother
centriole.";
Proc. Natl. Acad. Sci. U.S.A. 110:5987-5992(2013).
[15]
SUBCELLULAR LOCATION.
PubMed=26337392; DOI=10.1091/mbc.E15-04-0235;
Van de Mark D., Kong D., Loncarek J., Stearns T.;
"MDM1 is a microtubule-binding protein that negatively regulates
centriole duplication.";
Mol. Biol. Cell 26:3788-3802(2015).
-!- FUNCTION: Plays a role in microtubule organization and/or
maintenance for the formation of primary cilia (PC), a
microtubule-based structure that protrudes from the surface of
epithelial cells. Plays a critical role in G2/M checkpoint and
nuclear divisions. A key player in the DNA damage-activated
ATR/ATM signaling cascade since it is required for the proper
phosphorylation of H2AX, RPA, CHEK2 and CHEK1. Plays a critical
role in chromosome segregation, acting as a mediator required for
the maintenance of genomic stability through modulation of MDC1,
RPA and CHEK1. {ECO:0000269|PubMed:17954613,
ECO:0000269|PubMed:18283122, ECO:0000269|PubMed:23348840}.
-!- SUBUNIT: Interacts (via N-terminus) with ATRIP. Interacts with
ATM, ATR and MDC1. Interacts with XPA (via N-terminus) upon UV
irradiation. Interacts with CEP83, CCDC92, TTBK2, DVL3, NPHP3 and
weakly with NPHP4. {ECO:0000269|PubMed:18283122,
ECO:0000269|PubMed:19197159, ECO:0000269|PubMed:22863007,
ECO:0000269|PubMed:23530209}.
-!- INTERACTION:
Q53HC0:CCDC92; NbExp=5; IntAct=EBI-3937015, EBI-719994;
Q92997:DVL3; NbExp=5; IntAct=EBI-3937015, EBI-739789;
Q7Z494:NPHP3; NbExp=2; IntAct=EBI-3937015, EBI-2804263;
Q6IQ55:TTBK2; NbExp=4; IntAct=EBI-3937015, EBI-1050303;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriole
{ECO:0000269|PubMed:26337392}. Nucleus. Note=Localizes
specifically to very distally located appendage structures on the
mature centriole from which initiate PC formation
(PubMed:26337392). Persisted at centrioles throughout mitosis.
Expressed in chromatin-enriched nuclear fraction of HeLa cells. In
response to DNA damage, it translocates to nuclear foci that
contain the DNA damage response proteins KAT5/TIP60 and CHEK1.
{ECO:0000269|PubMed:26337392}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UPV0-1; Sequence=Displayed;
Name=2;
IsoId=Q9UPV0-2; Sequence=VSP_029843, VSP_029844;
-!- TISSUE SPECIFICITY: Expressed in several cell lines.
{ECO:0000269|PubMed:17954613}.
-!- PTM: Phosphorylation at Ser-186 is induced upon DNA-damage caused
by treatment with IR irradiation, UV irradiation, hydroxyurea or
amphidicolin. Also MDC1-mediated chromatin remodeling is critical
for DNA damage-induced phosphorylation.
{ECO:0000269|PubMed:18283122}.
-!- DISEASE: Nephronophthisis 15 (NPHP15) [MIM:614845]: An autosomal
recessive disorder characterized by the association of
nephronophthisis with Leber congenital amaurosis and retinal
degeneration, often resulting in blindness during childhood.
Additional features include seizures, cerebellar vermis
hypoplasia, facial dysmorphism, bronchiectasis and liver failure.
Nephronophthisis is a chronic tubulo-interstitial nephritis that
progresses to end-stage renal failure.
{ECO:0000269|PubMed:22863007}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAH00602.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH54015.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA83004.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA91677.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAB56023.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AB028975; BAA83004.2; ALT_INIT; mRNA.
EMBL; AP000892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000602; AAH00602.1; ALT_SEQ; mRNA.
EMBL; BC054015; AAH54015.1; ALT_SEQ; mRNA.
EMBL; AL117632; CAB56023.1; ALT_INIT; mRNA.
EMBL; AK001412; BAA91677.1; ALT_INIT; mRNA.
CCDS; CCDS31683.1; -. [Q9UPV0-1]
PIR; T17333; T17333.
RefSeq; NP_001258862.1; NM_001271933.1. [Q9UPV0-2]
RefSeq; NP_055771.4; NM_014956.4. [Q9UPV0-1]
RefSeq; XP_005271513.1; XM_005271456.1. [Q9UPV0-1]
RefSeq; XP_005271514.1; XM_005271457.1. [Q9UPV0-2]
UniGene; Hs.504009; -.
ProteinModelPortal; Q9UPV0; -.
SMR; Q9UPV0; -.
BioGrid; 116561; 89.
CORUM; Q9UPV0; -.
IntAct; Q9UPV0; 73.
STRING; 9606.ENSP00000278935; -.
CarbonylDB; Q9UPV0; -.
iPTMnet; Q9UPV0; -.
PhosphoSitePlus; Q9UPV0; -.
BioMuta; CEP164; -.
DMDM; 162416241; -.
EPD; Q9UPV0; -.
PaxDb; Q9UPV0; -.
PeptideAtlas; Q9UPV0; -.
PRIDE; Q9UPV0; -.
DNASU; 22897; -.
Ensembl; ENST00000278935; ENSP00000278935; ENSG00000110274. [Q9UPV0-1]
GeneID; 22897; -.
KEGG; hsa:22897; -.
UCSC; uc001prc.4; human. [Q9UPV0-1]
CTD; 22897; -.
DisGeNET; 22897; -.
EuPathDB; HostDB:ENSG00000110274.14; -.
GeneCards; CEP164; -.
H-InvDB; HIX0010166; -.
HGNC; HGNC:29182; CEP164.
HPA; HPA037605; -.
HPA; HPA037606; -.
MalaCards; CEP164; -.
MIM; 614845; phenotype.
MIM; 614848; gene.
neXtProt; NX_Q9UPV0; -.
OpenTargets; ENSG00000110274; -.
Orphanet; 3156; Senior-Loken syndrome.
PharmGKB; PA142672127; -.
eggNOG; ENOG410IJHV; Eukaryota.
eggNOG; ENOG4111VEQ; LUCA.
GeneTree; ENSGT00730000111178; -.
HOGENOM; HOG000111523; -.
HOVERGEN; HBG065113; -.
InParanoid; Q9UPV0; -.
KO; K16462; -.
OMA; NRKWLEH; -.
OrthoDB; EOG091G11U7; -.
PhylomeDB; Q9UPV0; -.
TreeFam; TF333034; -.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
ChiTaRS; CEP164; human.
GeneWiki; CEP164; -.
GenomeRNAi; 22897; -.
PRO; PR:Q9UPV0; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110274; -.
CleanEx; HS_CEP164; -.
ExpressionAtlas; Q9UPV0; baseline and differential.
Genevisible; Q9UPV0; HS.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0097539; C:ciliary transition fiber; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
CDD; cd00201; WW; 1.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
SMART; SM00456; WW; 1.
SUPFAM; SSF51045; SSF51045; 1.
PROSITE; PS50020; WW_DOMAIN_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division; Ciliopathy;
Cilium biogenesis/degradation; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Disease mutation; DNA damage; DNA repair;
Mitosis; Nephronophthisis; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 1460 Centrosomal protein of 164 kDa.
/FTId=PRO_0000312494.
DOMAIN 56 89 WW. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
REGION 1 194 Interaction with ATRIP.
{ECO:0000269|PubMed:18283122}.
COILED 1154 1206 {ECO:0000255}.
COMPBIAS 110 122 Lys-rich.
COMPBIAS 468 955 Glu-rich.
MOD_RES 186 186 Phosphoserine; by ATR and ATM.
{ECO:0000269|PubMed:18283122}.
MOD_RES 201 201 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 566 566 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1386 1386 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1388 1388 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1443 1443 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 469 469 E -> ERYH (in isoform 2).
{ECO:0000303|PubMed:10470851,
ECO:0000303|PubMed:18283122}.
/FTId=VSP_029843.
VAR_SEQ 1242 1250 REWWRQQRI -> L (in isoform 2).
{ECO:0000303|PubMed:10470851,
ECO:0000303|PubMed:18283122}.
/FTId=VSP_029844.
VARIANT 11 11 Q -> P (in NPHP15; dbSNP:rs387907309).
{ECO:0000269|PubMed:22863007}.
/FTId=VAR_068503.
VARIANT 93 93 R -> W (in NPHP15; dbSNP:rs387907310).
{ECO:0000269|PubMed:22863007}.
/FTId=VAR_068504.
VARIANT 94 94 S -> N (in dbSNP:rs490262).
/FTId=VAR_037511.
VARIANT 988 988 T -> S (in dbSNP:rs2305830).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_037512.
VARIANT 1119 1119 Q -> R (in dbSNP:rs573455).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_037513.
MUTAGEN 186 186 S->A: Prevents phosphorylation.
{ECO:0000269|PubMed:18283122}.
CONFLICT 110 110 K -> N (in Ref. 5; AAH54015).
{ECO:0000305}.
SEQUENCE 1460 AA; 164314 MW; 7A4F91E1CB7D1E43 CRC64;
MAGRPLRIGD QLVLEEDYDE TYIPSEQEIL EFAREIGIDP IKEPELMWLA REGIVAPLPG
EWKPCQDITG DIYYFNFANG QSMWDHPCDE HYRSLVIQER AKLSTSGAIK KKKKKKEKKD
KKDRDPPKSS LALGSSLAPV HVPLGGLAPL RGLVDTPPSA LRGSQSVSLG SSVESGRQLG
ELMLPSQGLK TSAYTKGLLG SIYEDKTALS LLGLGEETNE EDEEESDNQS VHSSSEPLRN
LHLDIGALGG DFEYEESLRT SQPEEKKDVS LDSDAAGPPT PCKPSSPGAD SSLSSAVGKG
RQGSGARPGL PEKEENEKSE PKICRNLVTP KADPTGSEPA KASEKEAPED TVDAGEEGSR
REEAAKEPKK KASALEEGSS DASQELEISE HMKEPQLSDS IASDPKSFHG LDFGFRSRIS
EHLLDVDVLS PVLGGACRQA QQPLGIEDKD DSQSSQDELQ SKQSKGLEER LSPPLPHEER
AQSPPRSLAT EEEPPQGPEG QPEWKEAEEL GEDSAASLSL QLSLQREQAP SPPAACEKGK
EQHSQAEELG PGQEEAEDPE EKVAVSPTPP VSPEVRSTEP VAPPEQLSEA ALKAMEEAVA
QVLEQDQRHL LESKQEKMQQ LREKLCQEEE EEILRLHQQK EQSLSSLRER LQKAIEEEEA
RMREEESQRL SWLRAQVQSS TQADEDQIRA EQEASLQKLR EELESQQKAE RASLEQKNRQ
MLEQLKEEIE ASEKSEQAAL NAAKEKALQQ LREQLEGERK EAVATLEKEH SAELERLCSS
LEAKHREVVS SLQKKIQEAQ QKEEAQLQKC LGQVEHRVHQ KSYHVAGYEH ELSSLLREKR
QEVEGEHERR LDKMKEEHQQ VMAKAREQYE AEERKQRAEL LGHLTGELER LQRAHERELE
TVRQEQHKRL EDLRRRHREQ ERKLQDLELD LETRAKDVKA RLALLEVQEE TARREKQQLL
DVQRQVALKS EEATATHQQL EEAQKEHTHL LQSNQQLREI LDELQARKLK LESQVDLLQA
QSQQLQKHFS SLEAEAQKKQ HLLREVTVEE NNASPHFEPD LHIEDLRKSL GTNQTKEVSS
SLSQSKEDLY LDSLSSHNVW HLLSAEGVAL RSAKEFLVQQ TRSMRRRQTA LKAAQQHWRH
ELASAQEVAK DPPGIKALED MRKNLEKETR HLDEMKSAMR KGHNLLKKKE EKLNQLESSL
WEEASDEGTL GGSPTKKAVT FDLSDMDSLS SESSESFSPP HREWWRQQRI DSTPSLTSRK
IHGLSHSLRQ ISSQLSSVLS ILDSLNPQSP PPLLASMPAQ LPPRDPKSTP TPTYYGSLAR
FSALSSATPT STQWAWDSGQ GPRLPSSVAQ TVDDFLLEKW RKYFPSGIPL LSNSPTPLES
RLGYMSASEQ LRLLQHSHSQ VPEAGSTTFQ GIIEANRRWL ERVKNDPRLP LFSSTPKPKA
TLSLLQLGLD EHNRVKVYRF


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