POF8_SCHPO
ID POF8_SCHPO Reviewed; 402 AA.
AC O13795;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=La-related protein 7 homolog {ECO:0000303|PubMed:29422501};
GN Name=pof8 {ECO:0000303|PubMed:29422503, ECO:0000303|PubMed:29422664,
GN ECO:0000312|PomBase:SPAC17G6.17};
GN Synonyms=lar7 {ECO:0000303|PubMed:29422501};
GN ORFNames=SPAC17G6.17 {ECO:0000312|PomBase:SPAC17G6.17};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Harrison C.L., Toda T.;
RT "Systematic genome-wide analysis of F-box protein-encoding genes in fission
RT yeast.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP INTERACTION WITH SKP1.
RX PubMed=15147268; DOI=10.1111/j.1356-9597.2004.00730.x;
RA Lehmann A., Katayama S., Harrison C., Dhut S., Kitamura K., McDonald N.,
RA Toda T.;
RT "Molecular interactions of fission yeast Skp1 and its role in the DNA
RT damage checkpoint.";
RL Genes Cells 9:367-382(2004).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TRP-103; 197-PHE-VAL-198
RP AND 341-ILE-ILE-342.
RX PubMed=29422501; DOI=10.1038/s41467-017-02296-4;
RA Collopy L.C., Ware T.L., Goncalves T., I Kongsstovu S., Yang Q.,
RA Amelina H., Pinder C., Alenazi A., Moiseeva V., Pearson S.R.,
RA Armstrong C.A., Tomita K.;
RT "LARP7 family proteins have conserved function in telomerase assembly.";
RL Nat. Commun. 9:557-557(2018).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TYR-330 AND ARG-343.
RX PubMed=29422503; DOI=10.1038/s41467-018-02874-0;
RA Mennie A.K., Moser B.A., Nakamura T.M.;
RT "LARP7-like protein Pof8 regulates telomerase assembly and poly(A)+TERRA
RT expression in fission yeast.";
RL Nat. Commun. 9:586-586(2018).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=29422664; DOI=10.1038/s41467-017-02284-8;
RA Paez-Moscoso D.J., Pan L., Sigauke R.F., Schroeder M.R., Tang W.,
RA Baumann P.;
RT "Pof8 is a La-related protein and a constitutive component of telomerase in
RT fission yeast.";
RL Nat. Commun. 9:587-587(2018).
CC -!- FUNCTION: RNA-binding protein required for assembly of the holoenzyme
CC telomerase ribonucleoprotein (RNP) complex (PubMed:29422501,
CC PubMed:29422503, PubMed:29422664). Specifically binds telomerase RNA
CC ter1 and promotes assembly of ter1 with catalytic subunit trt1
CC (PubMed:29422501, PubMed:29422503). Telomerase is a ribonucleoprotein
CC enzyme essential that copies new telomeric repeats onto chromosome ends
CC and functions to maintain cell division (PubMed:29422501,
CC PubMed:29422503, PubMed:29422664). {ECO:0000269|PubMed:29422501,
CC ECO:0000269|PubMed:29422503, ECO:0000269|PubMed:29422664}.
CC -!- SUBUNIT: Component of the telomerase holoenzyme complex composed
CC minimally of trt1 and the telomerase RNA template component
CC (PubMed:29422503, PubMed:29422664). Interacts with skp1
CC (PubMed:15147268). {ECO:0000269|PubMed:15147268,
CC ECO:0000269|PubMed:29422503, ECO:0000269|PubMed:29422664}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000269|PubMed:29422503}. Nucleus {ECO:0000269|PubMed:16823372}.
CC Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Critically short telomeres caused by reduced ter1
CC RNA stability and telomerase holoenzyme complex assembly defects.
CC {ECO:0000269|PubMed:29422501, ECO:0000269|PubMed:29422503,
CC ECO:0000269|PubMed:29422664}.
CC -!- SIMILARITY: Belongs to the LARP7 family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to contain a F-box domain
CC (PubMed:15147268). However, such a domain is not detectable by any
CC prediction tool. {ECO:0000269|PubMed:15147268, ECO:0000305}.
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DR EMBL; AB062777; BAB60688.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16228.1; -; Genomic_DNA.
DR PIR; T37849; T37849.
DR RefSeq; NP_594264.1; NM_001019687.2.
DR PDB; 6TZN; X-ray; 1.35 A; A=282-402.
DR PDB; 6U7V; X-ray; 1.42 A; A=273-402.
DR PDBsum; 6TZN; -.
DR PDBsum; 6U7V; -.
DR AlphaFoldDB; O13795; -.
DR SMR; O13795; -.
DR BioGRID; 278669; 15.
DR IntAct; O13795; 1.
DR STRING; 4896.SPAC17G6.17.1; -.
DR iPTMnet; O13795; -.
DR MaxQB; O13795; -.
DR PaxDb; O13795; -.
DR EnsemblFungi; SPAC17G6.17.1; SPAC17G6.17.1:pep; SPAC17G6.17.
DR GeneID; 2542194; -.
DR KEGG; spo:SPAC17G6.17; -.
DR PomBase; SPAC17G6.17; pof8.
DR VEuPathDB; FungiDB:SPAC17G6.17; -.
DR HOGENOM; CLU_689191_0_0_1; -.
DR InParanoid; O13795; -.
DR OMA; CEPMYID; -.
DR PRO; PR:O13795; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IMP:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IPI:PomBase.
DR GO; GO:0070034; F:telomerase RNA binding; IPI:PomBase.
DR GO; GO:0071027; P:nuclear RNA surveillance; IMP:PomBase.
DR GO; GO:1904868; P:telomerase catalytic core complex assembly; IMP:UniProtKB.
DR GO; GO:0090669; P:telomerase RNA stabilization; IMP:PomBase.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR014886; La_xRRM.
DR InterPro; IPR045537; Lar7_xRRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR Pfam; PF19977; xRRM; 1.
DR PROSITE; PS51939; XRRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Cytoplasm; Nucleus; Reference proteome;
KW RNA-binding; Telomere.
FT CHAIN 1..402
FT /note="La-related protein 7 homolog"
FT /id="PRO_0000119975"
FT DOMAIN 288..402
FT /note="xRRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01288"
FT REGION 64..138
FT /note="HTH La-type RNA-binding-like region"
FT /evidence="ECO:0000303|PubMed:29422501"
FT REGION 148..230
FT /note="RRM-like region"
FT /evidence="ECO:0000303|PubMed:29422501"
FT REGION 288..400
FT /note="xRRM-like region"
FT /evidence="ECO:0000303|PubMed:29422501"
FT MUTAGEN 103
FT /note="W->A: Strongly reduced binding to ter1 RNA, leading
FT to short telomeres."
FT /evidence="ECO:0000269|PubMed:29422501"
FT MUTAGEN 197..198
FT /note="FV->EE: Strongly reduced binding to ter1 RNA,
FT leading to short telomeres."
FT /evidence="ECO:0000269|PubMed:29422501"
FT MUTAGEN 330
FT /note="Y->A: Abolishes binding to ter1 RNA without
FT affecting localization to telomeres."
FT /evidence="ECO:0000269|PubMed:29422503"
FT MUTAGEN 341..342
FT /note="II->EE: Strongly reduced binding to ter1 RNA,
FT leading to short telomeres."
FT /evidence="ECO:0000269|PubMed:29422501"
FT MUTAGEN 343
FT /note="R->A: Abolishes binding to ter1 RNA without
FT affecting localization to telomeres."
FT /evidence="ECO:0000269|PubMed:29422503"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:6TZN"
FT HELIX 306..320
FT /evidence="ECO:0007829|PDB:6TZN"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:6TZN"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:6TZN"
FT STRAND 338..346
FT /evidence="ECO:0007829|PDB:6TZN"
FT HELIX 347..359
FT /evidence="ECO:0007829|PDB:6TZN"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:6TZN"
FT HELIX 390..400
FT /evidence="ECO:0007829|PDB:6TZN"
SQ SEQUENCE 402 AA; 46808 MW; 5CE59874476123C5 CRC64;
MFVPRQLNVR KIKAFTGKEN NSIADGNNNK LKDEHYKHNE ASKEPSHSIS GGLMLNQQDR
QLIEPLNPDF LSAVDSILEI YFHRERQKEK VHLAFLIQQD DFWKGIRPNP TQNNLKYALS
YVTNALFHFD NSSHMVIRNE NIVLPLDIPL YDRIIYVEPV PATLSNKSLL LAGKLRKYLK
EFLPYVDAIG TPEGYAFVIL YKKVDQSALS KLPVPPGWVL LTRKEWTNRE EKYFENQLHL
VKASSSDVSN SSNSFPENRY PKLTKVEKQM TKSVSKTSQT DKDEDNLDFT KNLLTRIKNL
HPLTNKSTIH SLLSYVFSRQ TQNIACEPMY IDYRKDETEA IIRWKTPLHA ETCINAFRTQ
ERKQNSHDDI RAHRKKGSSR PFLIAELITG EEEKNYWRML KK
