P21128 (ENDOU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Poly(U)-specific endoribonuclease
EC=3.1.-.-

Alternative name(s):
Placental protein 11
Short name=PP11
Protein endoU
Uridylate-specific endoribonuclease

Gene names

Name:

ENDOU

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Endoribonuclease that cleaves single-stranded RNAs at uridylates and releases products that have 2'-3'-cyclic phosphate termini. Ref.7
Cofactor	Manganese. Ref.7
Subunit structure	Monomer By similarity.
Subcellular location	Secreted Potential.
Tissue specificity	Placental-specific, but also associated with various malignant neoplasms.
Post-translational modification	It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.
Sequence similarities	Belongs to the ENDOU family. Contains 2 SMB (somatomedin-B) domains.
Caution	Was originally (Ref.1) thought to be a serine protease. However, Ref.7 showed it is not the case.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal
Ligand	Manganese Metal-binding RNA-binding
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	female pregnancy Inferred from expression pattern Ref.1. Source: UniProtKB immune response Inferred from electronic annotation. Source: InterPro proteolysis Inferred from direct assay Ref.1. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB extracellular space Traceable author statement. Source: ProtInc plasma membrane Traceable author statement Ref.6. Source: UniProtKB
Molecular function	RNA binding Inferred from direct assay Ref.7. Source: UniProtKB endoribonuclease activity Inferred from direct assay Ref.7. Source: UniProtKB growth factor activity Non-traceable author statement Ref.6. Source: UniProtKB manganese ion binding Traceable author statement Ref.7. Source: UniProtKB polysaccharide binding Inferred from electronic annotation. Source: InterPro scavenger receptor activity Inferred from electronic annotation. Source: InterPro serine-type peptidase activity Inferred from direct assay Ref.1Ref.7. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P21128-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P21128-2)

The sequence of this isoform differs from the canonical sequence as follows:
     19-59: Missing.

Isoform 3 (identifier: P21128-3)

The sequence of this isoform differs from the canonical sequence as follows:
     19-82: GKIESCASRCNEKFNRDAACQCDRRCLWHGNCCEDYEHLCTEDHKESEPLPQLEEETEEALASN → D

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18
	Chain	19 – 410	392	Poly(U)-specific endoribonuclease		PRO_0000036405
Regions
	Domain	20 – 62	43	SMB 1
	Domain	86 – 130	45	SMB 2
Amino acid modifications
	Disulfide bond	24 ↔ 40		Alternate By similarity
	Disulfide bond	24 ↔ 28		Alternate By similarity
	Disulfide bond	28 ↔ 58		Alternate By similarity
	Disulfide bond	38 ↔ 51		Alternate By similarity
	Disulfide bond	38 ↔ 40		Alternate By similarity
	Disulfide bond	44 ↔ 50		By similarity
	Disulfide bond	51 ↔ 58		Alternate By similarity
	Disulfide bond	90 ↔ 106		Alternate By similarity
	Disulfide bond	90 ↔ 94		Alternate By similarity
	Disulfide bond	94 ↔ 124		Alternate By similarity
	Disulfide bond	104 ↔ 117		Alternate By similarity
	Disulfide bond	104 ↔ 106		Alternate By similarity
	Disulfide bond	110 ↔ 116		By similarity
	Disulfide bond	117 ↔ 124		Alternate By similarity
Natural variations
	Alternative sequence	19 – 82	64	GKIES…ALASN → D in isoform 3.		VSP_039215
	Alternative sequence	19 – 59	41	Missing in isoform 2.		VSP_039216
	Natural variant	72	1	E → Q. Corresponds to variant rs6504 [ dbSNP | Ensembl ].		VAR_014793
	Natural variant	72	1	E → V. Corresponds to variant rs6505 [ dbSNP | Ensembl ].		VAR_014794
Experimental info
	Mutagenesis	284	1	E → Q: Abolishes endoribonuclease activity and increases RNA-binding activity. Ref.7
	Mutagenesis	285	1	H → A: Abolishes endoribonuclease activity without affecting RNA-binding activity. Ref.7
	Mutagenesis	290	1	E → Q: Abolishes endoribonuclease activity without affecting RNA-binding activity. Ref.7
	Mutagenesis	300	1	H → A: Abolishes endoribonuclease activity without affecting RNA-binding activity. Ref.7
	Mutagenesis	343	1	K → A: Strongly impairs endoribonuclease activity without affecting RNA-binding activity. Ref.7
	Sequence conflict	123	1	L → P in BAG37240. Ref.2
	Sequence conflict	387	1	Y → H in BAG37240. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: CC19484F40355129	FASTA	410	46,872
	10 20 30 40 50 60 MRACISLVLA VLCGLAWAGK IESCASRCNE KFNRDAACQC DRRCLWHGNC CEDYEHLCTE 70 80 90 100 110 120 DHKESEPLPQ LEEETEEALA SNLYSAPTSC QGRCYEAFDK HHQCHCNARC QEFGNCCKDF 130 140 150 160 170 180 ESLCSDHEVS HSSDAITKEE IQSISEKIYR ADTNKAQKED IVLNSQNCIS PSETRNQVDR 190 200 210 220 230 240 CPKPLFTYVN EKLFSKPTYA AFINLLNNYQ RATGHGEHFS AQELAEQDAF LREIMKTAVM 250 260 270 280 290 300 KELYSFLHHQ NRYGSEQEFV DDLKNMWFGL YSRGNEEGDS SGFEHVFSGE VKKGKVTGFH 310 320 330 340 350 360 NWIRFYLEEK EGLVDYYSHI YDGPWDSYPD VLAMQFNWDG YYKEVGSAFI GSSPEFEFAL 370 380 390 400 410 YSLCFIARPG KVCQLSLGGY PLAVRTYTWD KSTYGNGKKY IATAYIVSST
	Isoform 2 [UniParc]. Checksum: F5935AE12D7E924C	FASTA	369	42,121
	10 20 30 40 50 60 MRACISLVLA VLCGLAWAED HKESEPLPQL EEETEEALAS NLYSAPTSCQ GRCYEAFDKH 70 80 90 100 110 120 HQCHCNARCQ EFGNCCKDFE SLCSDHEVSH SSDAITKEEI QSISEKIYRA DTNKAQKEDI 130 140 150 160 170 180 VLNSQNCISP SETRNQVDRC PKPLFTYVNE KLFSKPTYAA FINLLNNYQR ATGHGEHFSA 190 200 210 220 230 240 QELAEQDAFL REIMKTAVMK ELYSFLHHQN RYGSEQEFVD DLKNMWFGLY SRGNEEGDSS 250 260 270 280 290 300 GFEHVFSGEV KKGKVTGFHN WIRFYLEEKE GLVDYYSHIY DGPWDSYPDV LAMQFNWDGY 310 320 330 340 350 360 YKEVGSAFIG SSPEFEFALY SLCFIARPGK VCQLSLGGYP LAVRTYTWDK STYGNGKKYI ATAYIVSST
	Isoform 3 [UniParc]. Checksum: D7F5B74604503201	FASTA	347	39,629
	10 20 30 40 50 60 MRACISLVLA VLCGLAWADL YSAPTSCQGR CYEAFDKHHQ CHCNARCQEF GNCCKDFESL 70 80 90 100 110 120 CSDHEVSHSS DAITKEEIQS ISEKIYRADT NKAQKEDIVL NSQNCISPSE TRNQVDRCPK 130 140 150 160 170 180 PLFTYVNEKL FSKPTYAAFI NLLNNYQRAT GHGEHFSAQE LAEQDAFLRE IMKTAVMKEL 190 200 210 220 230 240 YSFLHHQNRY GSEQEFVDDL KNMWFGLYSR GNEEGDSSGF EHVFSGEVKK GKVTGFHNWI 250 260 270 280 290 300 RFYLEEKEGL VDYYSHIYDG PWDSYPDVLA MQFNWDGYYK EVGSAFIGSS PEFEFALYSL 310 320 330 340 CFIARPGKVC QLSLGGYPLA VRTYTWDKST YGNGKKYIAT AYIVSST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of a cDNA encoding human placental protein 11, a putative serine protease with diagnostic significance as a tumor marker." Grundmann U., Roemisch J., Siebold B., Bohn H., Amann E. DNA Cell Biol. 9:243-250(1990) [PubMed: 2350438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF N-TERMINUS. Tissue: Placenta.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Tissue: Placenta.
[3]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[6]	"Homology of placental protein 11 and pea seed albumin 2 with vitronectin." Jenne D.E. Biochem. Biophys. Res. Commun. 176:1000-1006(1991) [PubMed: 1710108] [Abstract] Cited for: DOMAIN SOMATOMEDIN-B.
[7]	"The tumor marker human placental protein 11 is an endoribonuclease." Laneve P., Gioia U., Ragno R., Altieri F., Di Franco C., Santini T., Arceci M., Bozzoni I., Caffarelli E. J. Biol. Chem. 283:34712-34719(2008) [PubMed: 18936097] [Abstract] Cited for: FUNCTION, RNA-BINDING, COFACTOR, MUTAGENESIS OF GLU-284; HIS-285; GLU-290; HIS-300 AND LYS-343.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M32402 mRNA. Translation: AAA36464.1. M36109 mRNA. Translation: AAA36465.1. AK075446 mRNA. Translation: BAG52139.1. AK300169 mRNA. Translation: BAH13227.1. AK314688 mRNA. Translation: BAG37240.1. AC004241 Genomic DNA. No translation available. CH471111 Genomic DNA. Translation: EAW57940.1. BC069715 mRNA. Translation: AAH69715.1. BC074763 mRNA. Translation: AAH74763.1. BC111782 mRNA. Translation: AAI11783.1.
IPI	IPI00006995. IPI00795429. IPI00956135.
PIR	A34614.
RefSeq	NP_001165910.1. NM_001172439.1. NP_001165911.1. NM_001172440.1. NP_006016.1. NM_006025.3.
UniGene	Hs.997.
3D structure databases
ProteinModelPortal	P21128.
SMR	P21128. Positions 17-408.
ModBase	Search...
Protein-protein interaction databases
STRING	P21128.
Polymorphism databases
DMDM	296434493.
Proteomic databases
PRIDE	P21128.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000229003; ENSP00000229003; ENSG00000111405. ENST00000422538; ENSP00000397679; ENSG00000111405.
GeneID	8909.
KEGG	hsa:8909.
UCSC	uc001rpt.1. human.
Organism-specific databases
CTD	8909.
GeneCards	GC12M048103.
H-InvDB	HIX0036755.
HGNC	HGNC:14369. ENDOU.
HPA	HPA012388.
MIM	606720. gene.
neXtProt	NX_P21128.
PharmGKB	PA165512645.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05621.
GeneTree	ENSGT00530000063825.
HOVERGEN	HBG008236.
InParanoid	P21128.
OMA	RCQEFGN.
OrthoDB	EOG4V6ZH0.
PhylomeDB	P21128.
Gene expression databases
ArrayExpress	P21128.
Bgee	P21128.
Genevestigator	P21128.
GermOnline	ENSG00000111405. Homo sapiens.
Family and domain databases
InterPro	IPR018998. Endoribonuclease_XendoU. IPR020436. Somatomedin_B_chordata. IPR001212. Somatomedin_B_dom. [Graphical view]
KO	K14648.
Pfam	PF01033. Somatomedin_B. 2 hits. PF09412. XendoU. 1 hit. [Graphical view]
PRINTS	PR00022. SOMATOMEDINB.
SMART	SM00201. SO. 2 hits. [Graphical view]
PROSITE	PS00524. SMB_1. 2 hits. PS50958. SMB_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	33477.
SOURCE	Search...

Entry information

Entry name

ENDOU_HUMAN

Accession

Primary (citable) accession number: P21128
Secondary accession number(s): B2RBJ3 , B3KQS7, B7Z6E1, Q2NKJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	May 18, 2010
Last modified:	January 25, 2012
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.