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Leucine-rich repeat protein 1 (4-1BB-mediated-signaling molecule) (4-1BBlrr) (LRR-repeat protein 1) (LRR-1) (Peptidylprolyl isomerase-like 5)

 LLR1_HUMAN              Reviewed;         414 AA.
Q96L50; A5D6X3; B4DDE0; Q52M24; Q86SZ1; Q8N6H9;
26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
26-SEP-2003, sequence version 2.
27-SEP-2017, entry version 135.
RecName: Full=Leucine-rich repeat protein 1;
AltName: Full=4-1BB-mediated-signaling molecule;
AltName: Full=4-1BBlrr;
AltName: Full=LRR-repeat protein 1;
Short=LRR-1;
AltName: Full=Peptidylprolyl isomerase-like 5;
Name=LRR1; Synonyms=PPIL5;
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 AND 2), AND CHARACTERIZATION.
TISSUE=T-cell lymphoma;
PubMed=11804328;
Jang I.-K., Lee Z.-H., Kim H.-H., Hill J.M., Kim J.-D., Kwon B.S.;
"A novel leucine-rich repeat protein (LRR-1): potential involvement in
4-1BB-mediated signal transduction.";
Mol. Cells 12:304-312(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix carcinoma;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Neuroblastoma;
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).
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=B-cell, Heart, and Lung;
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]
FUNCTION IN AN E3 UBIQUITIN LIGASE COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, INTERACTION WITH CUL2; RBX1; ELOB AND ELOC, AND
MUTAGENESIS OF 341-HIS--PRO-344.
PubMed=15601820; DOI=10.1101/gad.1252404;
Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D.,
Conaway R.C., Conaway J.W., Nakayama K.I.;
"VHL-box and SOCS-box domains determine binding specificity for Cul2-
Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases.";
Genes Dev. 18:3055-3065(2004).
-!- FUNCTION: May negatively regulate the 4-1BB-mediated signaling
cascades which result in the activation of NK-kappaB and JNK1.
Probable substrate recognition subunit of an ECS (Elongin BC-
CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which
mediates the ubiquitination and subsequent proteasomal degradation
of target proteins. {ECO:0000269|PubMed:15601820}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with the cytoplasmic domain of TNFRSF9.
Component of the probable ECS(LRR1) E3 ubiquitin-protein ligase
complex which contains CUL2, RBX1, Elongin BC complex and LRR1.
Interacts with CUL2, RBX1, ELOB and ELOC.
{ECO:0000269|PubMed:15601820}.
-!- INTERACTION:
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-2510106, EBI-742948;
Q9UL42:PNMA2; NbExp=3; IntAct=EBI-2510106, EBI-302355;
Q15645:TRIP13; NbExp=3; IntAct=EBI-2510106, EBI-358993;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=LRR-1a;
IsoId=Q96L50-1; Sequence=Displayed;
Name=2; Synonyms=LRR-1b;
IsoId=Q96L50-2; Sequence=VSP_008363, VSP_008364;
-!- TISSUE SPECIFICITY: Ubiquitous. Maximal expression was seen in the
heart and skeletal muscle and minimal expression seen in the
kidney.
-!- SEQUENCE CAUTION:
Sequence=CAD62625.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY052405; AAL11430.1; -; mRNA.
EMBL; BX248298; CAD62625.1; ALT_INIT; mRNA.
EMBL; AK293156; BAG56701.1; -; mRNA.
EMBL; CH471078; EAW65761.1; -; Genomic_DNA.
EMBL; BC030142; AAH30142.1; -; mRNA.
EMBL; BC093697; AAH93697.1; -; mRNA.
EMBL; BC112241; AAI12242.1; -; mRNA.
EMBL; BC139921; AAI39922.1; -; mRNA.
CCDS; CCDS9686.1; -. [Q96L50-1]
CCDS; CCDS9687.1; -. [Q96L50-2]
RefSeq; NP_689542.2; NM_152329.3. [Q96L50-1]
RefSeq; NP_982292.1; NM_203467.1. [Q96L50-2]
UniGene; Hs.451090; -.
ProteinModelPortal; Q96L50; -.
BioGrid; 125793; 26.
IntAct; Q96L50; 16.
STRING; 9606.ENSP00000298288; -.
iPTMnet; Q96L50; -.
PhosphoSitePlus; Q96L50; -.
BioMuta; LRR1; -.
DMDM; 37079896; -.
EPD; Q96L50; -.
MaxQB; Q96L50; -.
PaxDb; Q96L50; -.
PeptideAtlas; Q96L50; -.
PRIDE; Q96L50; -.
DNASU; 122769; -.
Ensembl; ENST00000298288; ENSP00000298288; ENSG00000165501. [Q96L50-1]
Ensembl; ENST00000318317; ENSP00000315628; ENSG00000165501. [Q96L50-2]
GeneID; 122769; -.
KEGG; hsa:122769; -.
UCSC; uc001wwn.3; human. [Q96L50-1]
CTD; 122769; -.
DisGeNET; 122769; -.
EuPathDB; HostDB:ENSG00000165501.16; -.
GeneCards; LRR1; -.
H-InvDB; HIX0037761; -.
HGNC; HGNC:19742; LRR1.
HPA; HPA065703; -.
HPA; HPA069364; -.
MIM; 609193; gene.
neXtProt; NX_Q96L50; -.
OpenTargets; ENSG00000165501; -.
PharmGKB; PA134915321; -.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00530000063533; -.
HOGENOM; HOG000273865; -.
HOVERGEN; HBG045576; -.
InParanoid; Q96L50; -.
KO; K10348; -.
OMA; LVDNMGG; -.
OrthoDB; EOG091G0F7R; -.
PhylomeDB; Q96L50; -.
TreeFam; TF319257; -.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
GenomeRNAi; 122769; -.
PRO; PR:Q96L50; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000165501; -.
CleanEx; HS_PPIL5; -.
ExpressionAtlas; Q96L50; baseline and differential.
Genevisible; Q96L50; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR025875; Leu-rich_rpt_4.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
Pfam; PF12799; LRR_4; 1.
Pfam; PF13516; LRR_6; 1.
SMART; SM00369; LRR_TYP; 4.
SUPFAM; SSF52058; SSF52058; 1.
PROSITE; PS51450; LRR; 6.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Leucine-rich repeat;
Polymorphism; Reference proteome; Repeat; Ubl conjugation pathway.
CHAIN 1 414 Leucine-rich repeat protein 1.
/FTId=PRO_0000084447.
REPEAT 155 176 LRR 1.
REPEAT 178 199 LRR 2.
REPEAT 201 222 LRR 3.
REPEAT 227 248 LRR 4.
REPEAT 250 271 LRR 5.
REPEAT 273 294 LRR 6.
REPEAT 295 316 LRR 7.
VAR_SEQ 95 146 AISSSLKGFLSAMRLAHRGCNVDTPVSTLTPVKTSEFENFK
TKMVITSKKDY -> DSIWLSYHSIPSLPRFGYRKNLCLWK
ILSELFHSRNYYHESAFCCPHCGLSR (in isoform
2). {ECO:0000303|PubMed:11804328,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_008363.
VAR_SEQ 147 414 Missing (in isoform 2).
{ECO:0000303|PubMed:11804328,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_008364.
VARIANT 96 96 I -> N (in dbSNP:rs17121605).
/FTId=VAR_051095.
VARIANT 229 229 R -> W (in dbSNP:rs7148147).
/FTId=VAR_051096.
MUTAGEN 341 344 HIIP->AAA: Abolishes interaction with
CUL2 and RBX1.
{ECO:0000269|PubMed:15601820}.
CONFLICT 9 9 V -> A (in Ref. 3; BAG56701).
{ECO:0000305}.
CONFLICT 25 25 G -> V (in Ref. 1; AAL11430).
{ECO:0000305}.
CONFLICT 28 28 A -> S (in Ref. 1; AAL11430).
{ECO:0000305}.
SEQUENCE 414 AA; 46723 MW; B19B178D6CB33C4C CRC64;
MKLHCEVEVI SRHLPALGLR NRGKGVRAVL SLCQQTSRSQ PPVRAFLLIS TLKDKRGTRY
ELRENIEQFF TKFVDEGKAT VRLKEPPVDI CLSKAISSSL KGFLSAMRLA HRGCNVDTPV
STLTPVKTSE FENFKTKMVI TSKKDYPLSK NFPYSLEHLQ TSYCGLVRVD MRMLCLKSLR
KLDLSHNHIK KLPATIGDLI HLQELNLNDN HLESFSVALC HSTLQKSLRS LDLSKNKIKA
LPVQFCQLQE LKNLKLDDNE LIQFPCKIGQ LINLRFLSAA RNKLPFLPSE FRNLSLEYLD
LFGNTFEQPK VLPVIKLQAP LTLLESSART ILHNRIPYGS HIIPFHLCQD LDTAKICVCG
RFCLNSFIQG TTTMNLHSVA HTVVLVDNLG GTEAPIISYF CSLGCYVNSS DMLK


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