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Receptor-interacting serine/threonine-protein kinase 4 (EC 2.7.11.1) (Ankyrin repeat domain-containing protein 3) (PKC-associated protein kinase) (PKC-regulated protein kinase)

 RIPK4_MOUSE             Reviewed;         786 AA.
Q9ERK0; Q3UM04;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 2.
12-SEP-2018, entry version 134.
RecName: Full=Receptor-interacting serine/threonine-protein kinase 4;
EC=2.7.11.1;
AltName: Full=Ankyrin repeat domain-containing protein 3;
AltName: Full=PKC-associated protein kinase;
AltName: Full=PKC-regulated protein kinase;
Name=Ripk4; Synonyms=Ankrd3, Pkk;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PRKCB, PHOSPHORYLATION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=BALB/cJ;
PubMed=11278382; DOI=10.1074/jbc.M008069200;
Chen L., Haider K., Ponda M., Cariappa A., Rowitch D., Pillai S.;
"Protein kinase C-associated kinase (PKK), a novel membrane-
associated, ankyrin repeat-containing protein kinase.";
J. Biol. Chem. 276:21737-21744(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI; TISSUE=Mammary tumor;
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]
PROTEOLYTIC CLEAVAGE AT ASP-342 AND ASP-380, INTERACTION WITH TRAF1;
TRAF2; TRAF3 AND TRAF5, AND FUNCTION.
PubMed=12446564; DOI=10.1093/embo-reports/kvf236;
Meylan E., Martinon F., Thome M., Gschwendt M., Tschopp J.;
"RIP4 (DIK/PKK), a novel member of the RIP kinase family, activates
NF-kappa B and is processed during apoptosis.";
EMBO Rep. 3:1201-1208(2002).
[5]
PHOSPHORYLATION.
PubMed=12676934; DOI=10.1074/jbc.M301575200;
Moran S.T., Haider K., Ow Y., Milton P., Chen L., Pillai S.;
"Protein kinase C-associated kinase can activate NFkappaB in both a
kinase-dependent and a kinase-independent manner.";
J. Biol. Chem. 278:21526-21533(2003).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22197488; DOI=10.1016/j.ajhg.2011.11.013;
Mitchell K., O'Sullivan J., Missero C., Blair E., Richardson R.,
Anderson B., Antonini D., Murray J.C., Shanske A.L., Schutte B.C.,
Romano R.A., Sinha S., Bhaskar S.S., Black G.C., Dixon J., Dixon M.J.;
"Exome sequence identifies RIPK4 as the Bartsocas-Papas syndrome
locus.";
Am. J. Hum. Genet. 90:69-75(2012).
-!- FUNCTION: Involved in stratified epithelial development (By
similarity). It is a direct transcriptional target of TP63. Plays
a role in NF-kappa-B activation. {ECO:0000250,
ECO:0000269|PubMed:12446564, ECO:0000269|PubMed:22197488}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with PRKCB. Interacts with TRAF1, TRAF2, TRAF3
and TRAF5. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and
XIAP/BIRC4. {ECO:0000269|PubMed:11278382,
ECO:0000269|PubMed:12446564}.
-!- INTERACTION:
Q6Q0C0:TRAF7 (xeno); NbExp=2; IntAct=EBI-6116422, EBI-307556;
-!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
protein. Note=At steady state, a minor portion of this protein is
membrane-associated. The major portion is cytoplasmic.
-!- TISSUE SPECIFICITY: Ubiquitously expressed, with an abundant
expression in the thymus, bone marrow, pro-B, pre-B and immature B
cells and a weak expression in the spleen.
{ECO:0000269|PubMed:11278382}.
-!- DEVELOPMENTAL STAGE: Expressed at 10.5 dpc at diverse locations
including the embryonic forebrain, otic vesicle, branchial arches,
primitive gut, and genitourinary system. Transient expression in
the ventral neural tube at 12.5 dpc. By 14.5 dpc, strong
expression throughout the gastrointestinal tract was observed in
the luminal tissues of the esophagus, stomach, duodenum, and
intestines, as well as transient expression in the skin. Not
expressed in kidney. {ECO:0000269|PubMed:11278382}.
-!- PTM: May be phosphorylated by MAP3K2 and MAP3K3.
{ECO:0000269|PubMed:11278382, ECO:0000269|PubMed:12676934}.
-!- PTM: Proteolytically cleaved by during Fas-induced apoptosis.
Cleavage at Asp-342 and Asp-380. {ECO:0000269|PubMed:12446564}.
-!- PTM: Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by
BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-
B. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF302127; AAG30871.2; -; mRNA.
EMBL; AK145203; BAE26294.1; -; mRNA.
EMBL; BC057871; AAH57871.1; -; mRNA.
CCDS; CCDS28360.1; -.
RefSeq; NP_076152.2; NM_023663.6.
UniGene; Mm.35290; -.
PDB; 5WNI; X-ray; 2.65 A; A=1-342.
PDB; 5WNJ; X-ray; 2.55 A; A=1-342.
PDB; 5WNK; X-ray; 3.11 A; A=1-342.
PDB; 5WNL; X-ray; 2.50 A; A=1-342.
PDB; 5WNM; X-ray; 2.60 A; A=1-342.
PDBsum; 5WNI; -.
PDBsum; 5WNJ; -.
PDBsum; 5WNK; -.
PDBsum; 5WNL; -.
PDBsum; 5WNM; -.
ProteinModelPortal; Q9ERK0; -.
SMR; Q9ERK0; -.
IntAct; Q9ERK0; 2.
MINT; Q9ERK0; -.
STRING; 10090.ENSMUSP00000019386; -.
iPTMnet; Q9ERK0; -.
PhosphoSitePlus; Q9ERK0; -.
PaxDb; Q9ERK0; -.
PRIDE; Q9ERK0; -.
Ensembl; ENSMUST00000019386; ENSMUSP00000019386; ENSMUSG00000005251.
GeneID; 72388; -.
KEGG; mmu:72388; -.
UCSC; uc008adn.1; mouse.
CTD; 54101; -.
MGI; MGI:1919638; Ripk4.
eggNOG; KOG0192; Eukaryota.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0515; LUCA.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00550000074536; -.
HOGENOM; HOG000294086; -.
HOVERGEN; HBG061582; -.
InParanoid; Q9ERK0; -.
KO; K08848; -.
OMA; ACQHGQE; -.
OrthoDB; EOG091G0505; -.
PhylomeDB; Q9ERK0; -.
TreeFam; TF106506; -.
PRO; PR:Q9ERK0; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000005251; Expressed in 222 organ(s), highest expression level in urinary bladder.
CleanEx; MM_RIPK4; -.
ExpressionAtlas; Q9ERK0; baseline and differential.
Genevisible; Q9ERK0; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0002009; P:morphogenesis of an epithelium; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
CDD; cd00204; ANK; 3.
Gene3D; 1.25.40.20; -; 4.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF12796; Ank_2; 3.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 10.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 9.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ANK repeat; ATP-binding; Complete proteome; Cytoplasm;
Isopeptide bond; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase; Ubl conjugation.
CHAIN 1 786 Receptor-interacting serine/threonine-
protein kinase 4.
/FTId=PRO_0000273726.
DOMAIN 22 286 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REPEAT 439 468 ANK 1.
REPEAT 472 501 ANK 2.
REPEAT 505 534 ANK 3.
REPEAT 538 567 ANK 4.
REPEAT 571 601 ANK 5.
REPEAT 605 634 ANK 6.
REPEAT 638 667 ANK 7.
REPEAT 671 700 ANK 8.
REPEAT 704 734 ANK 9.
REPEAT 736 765 ANK 10.
NP_BIND 28 36 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 305 392 Ser-rich.
ACT_SITE 143 143 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 51 51 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 342 343 Cleavage. {ECO:0000269|PubMed:12446564}.
SITE 380 381 Cleavage. {ECO:0000269|PubMed:12446564}.
CROSSLNK 51 51 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P57078}.
CROSSLNK 145 145 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P57078}.
CONFLICT 718 718 S -> T (in Ref. 2; BAE26294).
{ECO:0000305}.
HELIX 10 13 {ECO:0000244|PDB:5WNI}.
STRAND 15 17 {ECO:0000244|PDB:5WNL}.
HELIX 19 21 {ECO:0000244|PDB:5WNL}.
STRAND 22 29 {ECO:0000244|PDB:5WNL}.
STRAND 31 33 {ECO:0000244|PDB:5WNL}.
STRAND 36 41 {ECO:0000244|PDB:5WNL}.
TURN 42 45 {ECO:0000244|PDB:5WNL}.
STRAND 46 52 {ECO:0000244|PDB:5WNL}.
STRAND 54 57 {ECO:0000244|PDB:5WNJ}.
HELIX 60 75 {ECO:0000244|PDB:5WNL}.
STRAND 84 88 {ECO:0000244|PDB:5WNL}.
TURN 89 92 {ECO:0000244|PDB:5WNL}.
STRAND 93 97 {ECO:0000244|PDB:5WNL}.
STRAND 100 103 {ECO:0000244|PDB:5WNM}.
HELIX 104 110 {ECO:0000244|PDB:5WNL}.
HELIX 115 134 {ECO:0000244|PDB:5WNL}.
STRAND 135 137 {ECO:0000244|PDB:5WNL}.
TURN 146 148 {ECO:0000244|PDB:5WNL}.
STRAND 149 151 {ECO:0000244|PDB:5WNL}.
STRAND 157 159 {ECO:0000244|PDB:5WNL}.
TURN 184 187 {ECO:0000244|PDB:5WNL}.
HELIX 190 194 {ECO:0000244|PDB:5WNL}.
STRAND 195 197 {ECO:0000244|PDB:5WNL}.
HELIX 202 218 {ECO:0000244|PDB:5WNL}.
HELIX 229 237 {ECO:0000244|PDB:5WNL}.
STRAND 249 251 {ECO:0000244|PDB:5WNL}.
HELIX 252 265 {ECO:0000244|PDB:5WNL}.
HELIX 270 272 {ECO:0000244|PDB:5WNL}.
HELIX 276 286 {ECO:0000244|PDB:5WNL}.
SEQUENCE 786 AA; 86613 MW; 66CE2C25EE96A40C CRC64;
MEGEGRGRWA LGLLRTFDAG EFAGWEKVGS GGFGQVYKVR HVHWKTWLAI KCSPSLHVDD
RERMELLEEA KKMEMAKFRY ILPVYGICQE PVGLVMEYME TGSLEKLLAS EPLPWDLRFR
IVHETAVGMN FLHCMSPPLL HLDLKPANIL LDAHYHVKIS DFGLAKCNGM SHSHDLSMDG
LFGTIAYLPP ERIREKSRLF DTKHDVYSFA IVIWGVLTQK KPFADEKNIL HIMMKVVKGH
RPELPPICRP RPRACASLIG LMQRCWHADP QVRPTFQEIT SETEDLCEKP DEEVKDLAHE
PGEKSSLESK SEARPESSRL KRASAPPFDN DCSLSELLSQ LDSGISQTLE GPEELSRSSS
ECKLPSSSSG KRLSGVSSVD SAFSSRGSLS LSFEREASTG DLGPTDIQKK KLVDAIISGD
TSRLMKILQP QDVDLVLDSS ASLLHLAVEA GQEECVKWLL LNNANPNLTN RKGSTPLHMA
VERKGRGIVE LLLARKTSVN AKDEDQWTAL HFAAQNGDEA STRLLLEKNA SVNEVDFEGR
TPMHVACQHG QENIVRTLLR RGVDVGLQGK DAWLPLHYAA WQGHLPIVKL LAKQPGVSVN
AQTLDGRTPL HLAAQRGHYR VARILIDLCS DVNICSLQAQ TPLHVAAETG HTSTARLLLH
RGAGKEALTS EGYTALHLAA QNGHLATVKL LIEEKADVMA RGPLNQTALH LAAARGHSEV
VEELVSADLI DLSDEQGLSA LHLAAQGRHS QTVETLLKHG AHINLQSLKF QGGQSSAATL
LRRSKT


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