GenomeNet

Database: UniProt
Entry: H0UYQ5_CAVPO
LinkDB: H0UYQ5_CAVPO
Original site: H0UYQ5_CAVPO 
ID   H0UYQ5_CAVPO            Unreviewed;       908 AA.
AC   H0UYQ5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=RNA binding motif protein 27 {ECO:0000313|Ensembl:ENSCPOP00000002276.3};
GN   Name=RBM27 {ECO:0000313|Ensembl:ENSCPOP00000002276.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000002276.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000002276.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000002276.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May be involved in the turnover of nuclear polyadenylated
CC       (pA+) RNA. {ECO:0000256|ARBA:ARBA00043866}.
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DR   EMBL; AAKN02009999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02010000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02010001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0UYQ5; -.
DR   STRING; 10141.ENSCPOP00000002276; -.
DR   Ensembl; ENSCPOT00000002531.3; ENSCPOP00000002276.3; ENSCPOG00000002498.4.
DR   VEuPathDB; HostDB:ENSCPOG00000002498; -.
DR   eggNOG; KOG2135; Eukaryota.
DR   GeneTree; ENSGT00510000046929; -.
DR   HOGENOM; CLU_006190_0_0_1; -.
DR   InParanoid; H0UYQ5; -.
DR   OMA; CPMEHGL; -.
DR   TreeFam; TF319253; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000002498; Expressed in testis and 12 other cell types or tissues.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR002483; PWI_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR045137; RBM26/27.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR14398; RNA RECOGNITION RRM/RNP DOMAIN; 1.
DR   PANTHER; PTHR14398:SF1; RNA-BINDING PROTEIN 27; 1.
DR   Pfam; PF01480; PWI; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00176}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT   DOMAIN          271..299
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          539..613
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   ZN_FING         271..299
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          77..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          863..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          735..809
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        86..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..179
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..354
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..375
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..725
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..900
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   908 AA;  102421 MW;  C285D5FAC869B031 CRC64;
     MLIEDVDALK SWLAKLLECD ADPSALANYV VALVKKDKPE KELKAFCADQ LDVFLQKETS
     GFVDKLFESL YTKNYLPPLE PVKPEPKPLV QEKEEIKEEV FQEPAEEERD GRKKKYPSPQ
     KARSESSERR TREKKREDGK WRDYDRYYER NELYREKYDW RRGRSKSRSK SRGLSRSRSR
     SRGRSKDRDP NRNVEHRERS KFKSERNDLE SSYVPVSAPP PSSSEQYSSG AQSIPSTVTV
     IAPAHHSENT TESWSNYYNN HSSSNSFGRN PPPKRRCRDY DERGFCVLGD LCQFDHGNDP
     LVVDEVALPS MIPFPPPPPG LPPPPPPGML MPPMPGPGPG PGPGPGPGPG PGHSMRLPVP
     QGHGQPPPSV VLPIPRPPIS QSSLINSRDQ PGTSAVPNLT PVGARLPPPL PQNLLYTVSE
     HTYEPDGYNP EAPSITSSGR SQYRQFFSRT QTQRPNLIGL TSGDMDANPR AANIVIQTEP
     PVPVSINSNI TRVVLEPDSR KRAVSGLEGP LTKKPWLGKQ GNNNQSKPGF LRKNQYTNTK
     LEVKKIPQEL NNITKLNEHF SKFGTIVNIQ VAFKGDPEAA LIQYLTNEEA RKAISSTEAV
     LNNRFIRVLW HRENNEQPAL QSPTQLLLQQ QQTLSHLSQQ QHHLPQHLHP QQALVGQAST
     SSVHGGIQKM MSKPQTSVPV KHRLGHASAN QIDTAGEDCQ IFSPPGHPKT TYSSSNLKTS
     SKLCTGSKSH DVQEVLKKKQ EAMKLQQDMR KKRQEVLEKQ IECQKMLISR LEKNKNMKPE
     ERANIMKTLK ELGEKISQLK DELKTSSTVS TPSKVKTKTE VSTLSNIFSN VDVFKLLRIL
     QIKIAANQGS KFKDRRLQIS WHKPKVPSIS TETEEEEVKE EETETSDLFL HDDDDEDEDE
     YESRSWRR
//
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