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Calcium-binding tyrosine phosphorylation-regulated protein (Calcium-binding protein 86) (Cancer/testis antigen 88) (CT88) (Fibrousheathin II) (Fibrousheathin-2) (FSP-2) (Testis-specific calcium-binding protein CBP86)

 CABYR_HUMAN             Reviewed;         493 AA.
O75952; B2R857; Q8WXW5; Q9HAY3; Q9HAY4; Q9HAY5; Q9HCY9;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 149.
RecName: Full=Calcium-binding tyrosine phosphorylation-regulated protein;
AltName: Full=Calcium-binding protein 86;
AltName: Full=Cancer/testis antigen 88;
Short=CT88;
AltName: Full=Fibrousheathin II;
AltName: Full=Fibrousheathin-2;
Short=FSP-2;
AltName: Full=Testis-specific calcium-binding protein CBP86;
Name=CABYR; Synonyms=CBP86, FSP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), PROTEIN
SEQUENCE OF 8-23; 28-48; 379-388 AND 394-410, VARIANTS ARG-448 AND
ALA-490, CALCIUM-BINDING, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=11820818; DOI=10.1006/dbio.2001.0527;
Naaby-Hansen S., Mandal A., Wolkowicz M.J., Sen B., Westbrook V.A.,
Shetty J., Coonrod S.A., Klotz K.L., Kim Y.-H., Bush L.A.,
Flickinger C.J., Herr J.C.;
"CABYR, a novel calcium-binding tyrosine phosphorylation-regulated
fibrous sheath protein involved in capacitation.";
Dev. Biol. 242:236-254(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Ovary;
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]
ALTERNATIVE SPLICING (ISOFORMS 3 AND 5), SUBUNIT, INTERACTION WITH
GSK3B, PHOSPHORYLATION AT THR-151 AND SER-155, MUTAGENESIS OF THR-146;
THR-151; SER-154; SER-155 AND THR-159, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=15752768; DOI=10.1016/j.bbrc.2005.02.089;
Hsu H.-C., Lee Y.-L., Cheng T.-S., Howng S.-L., Chang L.-K., Lu P.-J.,
Hong Y.-R.;
"Characterization of two non-testis-specific CABYR variants that bind
to GSK3beta with a proline-rich extensin-like domain.";
Biochem. Biophys. Res. Commun. 329:1108-1117(2005).
[7]
CALCIUM-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16139264; DOI=10.1016/j.ydbio.2005.07.005;
Kim Y.-H., Jha K.N., Mandal A., Vanage G., Farris E., Snow P.L.,
Klotz K., Naaby-Hansen S., Flickinger C.J., Herr J.C.;
"Translation and assembly of CABYR coding region B in fibrous sheath
and restriction of calcium binding to coding region A.";
Dev. Biol. 286:46-56(2005).
-!- FUNCTION: May function as a regulator of both motility- and head-
associated functions such as capacitation and the acrosome
reaction. Isoform 1 binds calcium in vitro. Isoform 2 and isoform
6 probably bind calcium. Isoform 3 and isoform 5 do not bind
calcium in vitro. Isoform 4 probably does not bind calcium.
-!- SUBUNIT: Interacts with FSCB (By similarity). Isoform 3 self-
associates. Isoform 3 and isoform 5 interact with GSK3B. Isoform 1
does not interact with GSK3B. {ECO:0000250,
ECO:0000269|PubMed:15752768}.
-!- INTERACTION:
P49841:GSK3B; NbExp=3; IntAct=EBI-10900795, EBI-373586;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
cilium, flagellum. Note=Localized to fibrous sheath including the
surface of the longitudinal columns and ribs of the principal
piece of sperm flagella.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus. Cytoplasm. Cell
projection, cilium, flagellum. Note=According to PubMed:15752768,
isoform 1, isoform 3 and isoform 5 are both nuclear and
cytoplasmic.
-!- SUBCELLULAR LOCATION: Isoform 3: Nucleus. Cytoplasm. Cell
projection, cilium, flagellum. Note=According to PubMed:15752768,
isoform 1, isoform 3 and isoform 5 are both nuclear and
cytoplasmic.
-!- SUBCELLULAR LOCATION: Isoform 5: Nucleus. Cytoplasm. Cell
projection, cilium, flagellum. Note=According to PubMed:15752768,
isoform 1, isoform 3 and isoform 5 are both nuclear and
cytoplasmic.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=O75952-1; Sequence=Displayed;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=2; Synonyms=CBP86-VII;
IsoId=O75952-2; Sequence=VSP_016247;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=3; Synonyms=CBP86-II;
IsoId=O75952-3; Sequence=VSP_016248, VSP_016251;
Name=4; Synonyms=CBP86-IV;
IsoId=O75952-4; Sequence=VSP_016249, VSP_016250;
Name=5; Synonyms=CBP86-III;
IsoId=O75952-5; Sequence=VSP_016246, VSP_016248, VSP_016251;
Name=6; Synonyms=CBP86-VI;
IsoId=O75952-6; Sequence=VSP_016245;
-!- TISSUE SPECIFICITY: Expressed in elongating spermatids and
spermatozoa (at protein level). Isoform 1 is expressed in testis.
Isoform 3 and isoform 5 are also expressed in brain, pancreas and
numerous brain tumors. {ECO:0000269|PubMed:11820818,
ECO:0000269|PubMed:15752768, ECO:0000269|PubMed:16139264}.
-!- PTM: Isoform 1 is phosphorylated on tyrosine residues during in
vitro capacitation. Isoform 3 and isoform 5 are phosphorylated by
GSK3B in vitro. Dephosphorylation affects its ability to bind
calcium. {ECO:0000269|PubMed:11820818,
ECO:0000269|PubMed:15752768}.
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EMBL; AF088868; AAC35373.1; -; mRNA.
EMBL; AF295037; AAG17889.1; -; mRNA.
EMBL; AF295038; AAG17890.1; -; mRNA.
EMBL; AF295039; AAG17891.1; -; mRNA.
EMBL; AF329634; AAL56051.1; -; mRNA.
EMBL; AY007205; AAG01891.1; -; mRNA.
EMBL; AK313243; BAG36054.1; -; mRNA.
EMBL; AC090772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471088; EAX01177.1; -; Genomic_DNA.
EMBL; BC011996; AAH11996.1; -; mRNA.
CCDS; CCDS11881.1; -. [O75952-1]
CCDS; CCDS11882.1; -. [O75952-2]
CCDS; CCDS11883.1; -. [O75952-5]
CCDS; CCDS42420.1; -. [O75952-3]
CCDS; CCDS45840.1; -. [O75952-4]
RefSeq; NP_036321.2; NM_012189.3. [O75952-1]
RefSeq; NP_619584.1; NM_138643.2. [O75952-5]
RefSeq; NP_619585.1; NM_138644.2. [O75952-3]
RefSeq; NP_722452.1; NM_153768.2. [O75952-2]
RefSeq; NP_722453.1; NM_153769.2. [O75952-3]
RefSeq; NP_722454.1; NM_153770.2. [O75952-4]
RefSeq; XP_016881195.1; XM_017025706.1. [O75952-1]
UniGene; Hs.511983; -.
ProteinModelPortal; O75952; -.
SMR; O75952; -.
BioGrid; 117642; 2.
IntAct; O75952; 1.
STRING; 9606.ENSP00000432870; -.
iPTMnet; O75952; -.
PhosphoSitePlus; O75952; -.
BioMuta; CABYR; -.
EPD; O75952; -.
MaxQB; O75952; -.
PaxDb; O75952; -.
PeptideAtlas; O75952; -.
PRIDE; O75952; -.
DNASU; 26256; -.
Ensembl; ENST00000327201; ENSP00000317095; ENSG00000154040. [O75952-5]
Ensembl; ENST00000399481; ENSP00000382404; ENSG00000154040. [O75952-2]
Ensembl; ENST00000399496; ENSP00000382419; ENSG00000154040. [O75952-3]
Ensembl; ENST00000399499; ENSP00000382421; ENSG00000154040. [O75952-3]
Ensembl; ENST00000415309; ENSP00000399973; ENSG00000154040. [O75952-4]
Ensembl; ENST00000463087; ENSP00000432870; ENSG00000154040. [O75952-1]
Ensembl; ENST00000486759; ENSP00000431142; ENSG00000154040. [O75952-1]
Ensembl; ENST00000621648; ENSP00000483621; ENSG00000154040. [O75952-1]
GeneID; 26256; -.
KEGG; hsa:26256; -.
UCSC; uc002kux.5; human. [O75952-1]
CTD; 26256; -.
DisGeNET; 26256; -.
EuPathDB; HostDB:ENSG00000154040.20; -.
GeneCards; CABYR; -.
HGNC; HGNC:15569; CABYR.
HPA; HPA040703; -.
HPA; HPA047801; -.
MIM; 612135; gene.
neXtProt; NX_O75952; -.
OpenTargets; ENSG00000154040; -.
PharmGKB; PA26005; -.
eggNOG; ENOG410IFPT; Eukaryota.
eggNOG; ENOG410ZQAQ; LUCA.
GeneTree; ENSGT00390000000444; -.
HOVERGEN; HBG080982; -.
InParanoid; O75952; -.
OMA; EQIVIPF; -.
OrthoDB; EOG091G18VB; -.
PhylomeDB; O75952; -.
TreeFam; TF332959; -.
SIGNOR; O75952; -.
ChiTaRS; CABYR; human.
GeneWiki; CABYR; -.
GenomeRNAi; 26256; -.
PRO; PR:O75952; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000154040; -.
CleanEx; HS_CABYR; -.
ExpressionAtlas; O75952; baseline and differential.
Genevisible; O75952; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031514; C:motile cilium; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0097229; C:sperm end piece; IEA:Ensembl.
GO; GO:0035686; C:sperm fibrous sheath; IDA:BHF-UCL.
GO; GO:0097228; C:sperm principal piece; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; ISS:BHF-UCL.
GO; GO:0017124; F:SH3 domain binding; NAS:BHF-UCL.
GO; GO:0003351; P:epithelial cilium movement; NAS:BHF-UCL.
GO; GO:0048240; P:sperm capacitation; NAS:BHF-UCL.
InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
Pfam; PF02197; RIIa; 1.
SMART; SM00394; RIIa; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell projection; Cilium;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Flagellum; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 493 Calcium-binding tyrosine phosphorylation-
regulated protein.
/FTId=PRO_0000089268.
DOMAIN 12 49 RIIa.
MOD_RES 151 151 Phosphothreonine.
{ECO:0000305|PubMed:15752768}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000305|PubMed:15752768}.
VAR_SEQ 1 201 Missing (in isoform 6).
{ECO:0000303|PubMed:11820818}.
/FTId=VSP_016245.
VAR_SEQ 1 98 Missing (in isoform 5).
{ECO:0000303|PubMed:11820818}.
/FTId=VSP_016246.
VAR_SEQ 49 66 Missing (in isoform 2).
{ECO:0000303|PubMed:11820818,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_016247.
VAR_SEQ 181 379 GKVSSIHSDQSDVLMVDVATSMPVVIKEVPSSEAAEDVMVA
APLVCSGKVLEVQVVNQTSVHVDLGSQPKENEAEPSTASSV
PLQDEQEPPAYDQAPEVTLQADIEVMSTVHISSVYNDVPVT
EGVVYIEQLPEQIVIPFTDQVACLKENEQSKENEQSPRVSP
KSVVEKTTSGMSKKSVESVKLAQLEENAKYSSVYM -> AM
ATSERGQPPPCSNMWTLYCLTDKNQQGHPSPPPAPGPFPQA
TLYLPNPKDPQFQQHPPKVTFPTYVMGDTKKTSAPPFILVG
SNVQEAQGWKPLPGHAVVSQSDVLRYVAMQVPIAVPADEKY
QKHTLSPQNANPPSGQDVPRPKSPVFLSVAFPVEDVAKKSS
GSGDKCAPFGSYGIAGEVTVTTAHKRRKAETEN (in
isoform 3 and isoform 5).
{ECO:0000303|PubMed:11820818,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_016248.
VAR_SEQ 181 221 GKVSSIHSDQSDVLMVDVATSMPVVIKEVPSSEAAEDVMVA
-> EDVAKKSSGSGDKCAPFGSYGIAGEVTVTTAHKRRKAE
TEN (in isoform 4).
{ECO:0000303|PubMed:11820818}.
/FTId=VSP_016249.
VAR_SEQ 222 493 Missing (in isoform 4).
{ECO:0000303|PubMed:11820818}.
/FTId=VSP_016250.
VAR_SEQ 380 493 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:11820818,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_016251.
VARIANT 74 74 T -> M (in dbSNP:rs3786417).
/FTId=VAR_030040.
VARIANT 186 186 I -> V (in dbSNP:rs35118855).
/FTId=VAR_050709.
VARIANT 448 448 K -> R (in dbSNP:rs1049682).
{ECO:0000269|PubMed:11820818}.
/FTId=VAR_030041.
VARIANT 490 490 S -> A (in dbSNP:rs1049683).
{ECO:0000269|PubMed:11820818}.
/FTId=VAR_023818.
MUTAGEN 146 146 T->A: Does not affect phosphorylation.
{ECO:0000269|PubMed:15752768}.
MUTAGEN 151 151 T->A: Decreases phosphorylation.
Abolishes phosphorylation; when
associated with A-155.
{ECO:0000269|PubMed:15752768}.
MUTAGEN 154 154 S->A: Does not affect phosphorylation.
Does not affect phosphorylation; when
associated with A-159.
{ECO:0000269|PubMed:15752768}.
MUTAGEN 155 155 S->A: Decreases phosphorylation and
interaction with GSK3B. Abolishes
phosphorylation and decreases interaction
with GSK3B; when associated with A-151.
{ECO:0000269|PubMed:15752768}.
MUTAGEN 159 159 T->A: Does not affect phosphorylation.
Does not affect phosphorylation; when
associated with A-154.
{ECO:0000269|PubMed:15752768}.
CONFLICT 423 423 I -> V (in Ref. 1; AAC35373/AAL56051).
{ECO:0000305}.
SEQUENCE 493 AA; 52774 MW; 42F97605262C8199 CRC64;
MISSKPRLVV PYGLKTLLEG ISRAVLKTNP SNINQFAAAY FQELTMYRGN TTMDIKDLVK
QFHQIKVEKW SEGTTPQKKL ECLKEPGKTS VESKVPTQME KSTDTDEDNV TRTEYSDKTT
QFPSVYAVPG TEQTEAVGGL SSKPATPKTT TPPSSPPPTA VSPEFAYVPA DPAQLAAQML
GKVSSIHSDQ SDVLMVDVAT SMPVVIKEVP SSEAAEDVMV AAPLVCSGKV LEVQVVNQTS
VHVDLGSQPK ENEAEPSTAS SVPLQDEQEP PAYDQAPEVT LQADIEVMST VHISSVYNDV
PVTEGVVYIE QLPEQIVIPF TDQVACLKEN EQSKENEQSP RVSPKSVVEK TTSGMSKKSV
ESVKLAQLEE NAKYSSVYME AEATALLSDT SLKGQPEVPA QLLDAEGAIK IGSEKSLHLE
VEITSIVSDN TGQEESGENS VPQEMEGKPV LSGEAAEAVH SGTSVKSSSG PFPPAPEGLT
APEIEPEGES TAE


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EIAAB36540 Metastasin,Nerve growth factor-induced protein 42A,P9K,Placental calcium-binding protein,Protein S100-A4,Rat,Rattus norvegicus,S100 calcium-binding protein A4,S100a4
EIAAB07237 Calcineurin homologous protein,Calcium-binding protein CHP,Calcium-binding protein p22,Chp,Mouse,Mus musculus,Sid 470,Sid470
EIAAB36537 Capl,Metastasin,Metastatic cell protein,Mouse,Mts1,Mus musculus,PEL98,Placental calcium-binding protein,Protein 18A2,Protein Mts1,Protein S100-A4,S100 calcium-binding protein A4,S100a4
EIAAB36523 CABP,CABP9K,CALB3,Calbindin-D9k,Homo sapiens,Human,Protein S100-G,S100 calcium-binding protein G,S100D,S100G,Vitamin D-dependent calcium-binding protein, intestinal


 

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