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Polyadenylate-binding protein 3 (PABP-3) (Poly(A)-binding protein 3) (Testis-specific poly(A)-binding protein)

 PABP3_HUMAN             Reviewed;         631 AA.
Q9H361; Q8NHV0; Q9H086;
01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-FEB-2003, sequence version 2.
25-OCT-2017, entry version 146.
RecName: Full=Polyadenylate-binding protein 3;
Short=PABP-3;
Short=Poly(A)-binding protein 3;
AltName: Full=Testis-specific poly(A)-binding protein;
Name=PABPC3; Synonyms=PABP3, PABPL3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=11328870; DOI=10.1093/nar/29.9.1872;
Feral C., Guellaen G., Pawlak A.;
"Human testis expresses a specific poly(A)-binding protein.";
Nucleic Acids Res. 29:1872-1883(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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).
[4]
STRUCTURE BY NMR OF 286-376.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RNA binding domain 4 in polyadenylation binding
protein 3.";
Submitted (JUN-2006) to the PDB data bank.
-!- FUNCTION: Binds the poly(A) tail of mRNA. May be involved in
cytoplasmic regulatory processes of mRNA metabolism. Binds poly(A)
with a slightly lower affinity as compared to PABPC1.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Testis specific.
{ECO:0000269|PubMed:11328870}.
-!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF132026; AAG38953.1; -; mRNA.
EMBL; AL136900; CAB66834.2; -; mRNA.
EMBL; BC027617; AAH27617.1; -; mRNA.
CCDS; CCDS9311.1; -.
RefSeq; NP_112241.2; NM_030979.2.
UniGene; Hs.458280; -.
PDB; 2D9P; NMR; -; A=286-375.
PDB; 4IVE; X-ray; 2.30 A; A/B/C/D=535-631.
PDBsum; 2D9P; -.
PDBsum; 4IVE; -.
ProteinModelPortal; Q9H361; -.
SMR; Q9H361; -.
BioGrid; 111079; 25.
IntAct; Q9H361; 7.
MINT; MINT-3067051; -.
STRING; 9606.ENSP00000281589; -.
iPTMnet; Q9H361; -.
PhosphoSitePlus; Q9H361; -.
SwissPalm; Q9H361; -.
BioMuta; PABPC3; -.
DMDM; 28201852; -.
EPD; Q9H361; -.
MaxQB; Q9H361; -.
PaxDb; Q9H361; -.
PeptideAtlas; Q9H361; -.
PRIDE; Q9H361; -.
DNASU; 5042; -.
Ensembl; ENST00000281589; ENSP00000281589; ENSG00000151846.
GeneID; 5042; -.
KEGG; hsa:5042; -.
UCSC; uc001upy.4; human.
CTD; 5042; -.
EuPathDB; HostDB:ENSG00000151846.8; -.
GeneCards; PABPC3; -.
HGNC; HGNC:8556; PABPC3.
HPA; HPA045423; -.
HPA; HPA067156; -.
MIM; 604680; gene.
neXtProt; NX_Q9H361; -.
OpenTargets; ENSG00000151846; -.
PharmGKB; PA32882; -.
eggNOG; KOG0123; Eukaryota.
eggNOG; ENOG410XR5X; LUCA.
GeneTree; ENSGT00760000118913; -.
HOGENOM; HOG000217922; -.
HOVERGEN; HBG002295; -.
InParanoid; Q9H361; -.
KO; K13126; -.
OrthoDB; EOG091G03ZE; -.
PhylomeDB; Q9H361; -.
TreeFam; TF300458; -.
EvolutionaryTrace; Q9H361; -.
GeneWiki; PABPC3; -.
GenomeRNAi; 5042; -.
PRO; PR:Q9H361; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000151846; -.
CleanEx; HS_PABPC3; -.
ExpressionAtlas; Q9H361; baseline and differential.
Genevisible; Q9H361; HS.
GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
GO; GO:0016071; P:mRNA metabolic process; NAS:UniProtKB.
InterPro; IPR036053; PABP-dom.
InterPro; IPR006515; PABP_1234.
InterPro; IPR002004; PABP_HYD.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR003954; RRM_dom_euk.
Pfam; PF00658; PABP; 1.
Pfam; PF00076; RRM_1; 4.
SMART; SM00517; PolyA; 1.
SMART; SM00360; RRM; 4.
SMART; SM00361; RRM_1; 3.
SUPFAM; SSF54928; SSF54928; 2.
SUPFAM; SSF63570; SSF63570; 1.
TIGRFAMs; TIGR01628; PABP-1234; 1.
PROSITE; PS51309; PABC; 1.
PROSITE; PS50102; RRM; 4.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Reference proteome;
Repeat; RNA-binding.
CHAIN 1 631 Polyadenylate-binding protein 3.
/FTId=PRO_0000081702.
DOMAIN 11 89 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 99 175 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 191 268 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 294 370 RRM 4. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 537 614 PABC. {ECO:0000255|PROSITE-
ProRule:PRU00641}.
CONFLICT 221 222 KV -> EL (in Ref. 2; CAB66834).
{ECO:0000305}.
CONFLICT 492 492 A -> R (in Ref. 1; AAG38953).
{ECO:0000305}.
HELIX 542 546 {ECO:0000244|PDB:4IVE}.
HELIX 550 568 {ECO:0000244|PDB:4IVE}.
TURN 570 572 {ECO:0000244|PDB:4IVE}.
HELIX 573 580 {ECO:0000244|PDB:4IVE}.
HELIX 585 592 {ECO:0000244|PDB:4IVE}.
HELIX 595 609 {ECO:0000244|PDB:4IVE}.
SEQUENCE 631 AA; 70031 MW; 2F8C5BF6F508AAEF CRC64;
MNPSTPSYPT ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RICRDLITSG SSNYAYVNFQ
HTKDAEHALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN IFVKNLDKSI NNKALYDTVS
AFGNILSCNV VCDENGSKGY GFVHFETHEA AERAIKKMNG MLLNGRKVFV GQFKSRKERE
AELGARAKEF PNVYIKNFGE DMDDERLKDL FGKFGPALSV KVMTDESGKS KGFGFVSFER
HEDAQKAVDE MNGKELNGKQ IYVGRAQKKV ERQTELKRTF EQMKQDRITR YQVVNLYVKN
LDDGIDDERL RKAFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT
KPLYVALAQR KEERQAYLTN EYMQRMASVR AVPNQRAPPS GYFMTAVPQT QNHAAYYPPS
QIARLRPSPR WTAQGARPHP FQNKPSAIRP GAPRVPFSTM RPASSQVPRV MSTQRVANTS
TQTVGPRPAA AAAAAATPAV RTVPRYKYAA GVRNPQQHRN AQPQVTMQQL AVHVQGQETL
TASRLASAPP QKQKQMLGER LFPLIQAMHP TLAGKITGML LEIDNSELLY MLESPESLRS
KVDEAVAVLQ AHQAKEATQK AVNSATGVPT V


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