DIK1B_MOUSE
ID DIK1B_MOUSE Reviewed; 431 AA.
AC Q99ML4; Q0VG43; Q80UM6; Q9JMG0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Divergent protein kinase domain 1B {ECO:0000305};
DE AltName: Full=Pancreatitis-induced protein 49;
DE AltName: Full=Protein FAM69B;
GN Name=Dipk1b; Synonyms=Fam69b, Pip49;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA Inoue S., Sano H., Ohta M.;
RT "Growth suppression of Escherichia coli by induction of expression of
RT mammalian genes with transmembrane or ATPase domains.";
RL Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11281735; DOI=10.1006/mcbr.2000.0277;
RA Samir A.A., Ropolo A., Grasso D., Tomasini R., Dagorn J.-C., Dusetti N.,
RA Iovanna J.L., Vaccaro M.I.;
RT "Cloning and expression of the mouse PIP49 (pancreatitis induced protein
RT 49) mRNA which encodes a new putative transmembrane protein activated in
RT the pancreas with acute pancreatitis.";
RL Mol. Cell Biol. Res. Commun. 4:188-193(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-431.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION, DISULFIDE BONDS, AND TISSUE SPECIFICITY.
RX PubMed=21334309; DOI=10.1016/j.bbrc.2011.02.076;
RA Tennant-Eyles A.J., Moffitt H., Whitehouse C.A., Roberts R.G.;
RT "Characterisation of the FAM69 family of cysteine-rich endoplasmic
RT reticulum proteins.";
RL Biochem. Biophys. Res. Commun. 406:471-477(2011).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21334309}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:21334309}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, testis, lung, heart, stomach,
CC intestine, pancreas, liver and salivary gland. Strongly expressed in
CC acute pancreatitis, brain, and in peripheral endothelial cells.
CC {ECO:0000269|PubMed:11281735, ECO:0000269|PubMed:21334309}.
CC -!- PTM: Among the many cysteines in the lumenal domain, most are probably
CC involved in disulfide bonds.
CC -!- SIMILARITY: Belongs to the DIPK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH51954.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH60081.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI16752.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA92750.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB030186; BAA92750.1; ALT_FRAME; mRNA.
DR EMBL; AF332189; AAK17190.1; -; mRNA.
DR EMBL; AK045880; BAC32519.1; -; mRNA.
DR EMBL; AL732311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051954; AAH51954.2; ALT_INIT; mRNA.
DR EMBL; BC060081; AAH60081.2; ALT_INIT; mRNA.
DR EMBL; BC116751; AAI16752.1; ALT_INIT; mRNA.
DR CCDS; CCDS50542.1; -.
DR RefSeq; NP_062807.2; NM_019833.3.
DR AlphaFoldDB; Q99ML4; -.
DR SMR; Q99ML4; -.
DR STRING; 10090.ENSMUSP00000073860; -.
DR PhosphoSitePlus; Q99ML4; -.
DR SwissPalm; Q99ML4; -.
DR MaxQB; Q99ML4; -.
DR PaxDb; Q99ML4; -.
DR PRIDE; Q99ML4; -.
DR ProteomicsDB; 266827; -.
DR Antibodypedia; 53284; 47 antibodies from 13 providers.
DR DNASU; 56279; -.
DR Ensembl; ENSMUST00000074240; ENSMUSP00000073860; ENSMUSG00000036186.
DR GeneID; 56279; -.
DR KEGG; mmu:56279; -.
DR UCSC; uc008ivx.2; mouse.
DR CTD; 138311; -.
DR MGI; MGI:1927576; Dipk1b.
DR VEuPathDB; HostDB:ENSMUSG00000036186; -.
DR eggNOG; ENOG502QU5P; Eukaryota.
DR GeneTree; ENSGT00390000006452; -.
DR HOGENOM; CLU_039177_0_0_1; -.
DR InParanoid; Q99ML4; -.
DR OMA; WALLHIN; -.
DR OrthoDB; 661899at2759; -.
DR PhylomeDB; Q99ML4; -.
DR TreeFam; TF313319; -.
DR BioGRID-ORCS; 56279; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q99ML4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99ML4; protein.
DR Bgee; ENSMUSG00000036186; Expressed in facial nucleus and 200 other tissues.
DR Genevisible; Q99ML4; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR022049; FAM69_kinase_dom.
DR InterPro; IPR029244; FAM69_N.
DR Pfam; PF12260; PIP49_C; 1.
DR Pfam; PF14875; PIP49_N; 1.
DR SMART; SM01299; PIP49_N; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..431
FT /note="Divergent protein kinase domain 1B"
FT /id="PRO_0000287232"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..431
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 5..6
FT /note="May mediate ER retention"
FT DISULFID 57..94
FT /evidence="ECO:0000305|PubMed:21334309"
FT DISULFID 62..117
FT /evidence="ECO:0000305|PubMed:21334309"
FT CONFLICT 399
FT /note="L -> K (in Ref. 1; BAA92750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 48792 MW; A4F84CD9CDC33202 CRC64;
MRRLRRLVHL VLLCPFSKGL QGRLPGLRVK YVLLVWLGIF VGSWMVYVHY SSYSELCRGH
VCQVVICDQY RKGIISGSVC QDLCELQKVE WRTCLSSAPG QQVYSGLWQD KEVTIKCGIE
EALNSKAWPD AAPRRELVLF DKPTRGTSIK EFREMTLSFL KANLGDLPSL PALVDQILLM
ADFNKDSRVS LAEAKSVWAL LQRNEFLLLL SLQEKEHASR LLGYCGDLYL TEGIPHGSWH
GAVLLPALRP LLPSVLHRAL QQWFGPAWPW RAKIAIGLLE FVEELFHGSY GTFYMCETTL
ANVGYTATYD FKMADLQQVA PEATVRRFLQ GRHCEQSSDC IYGRDCRAPC DRLMRQCKGD
LIQPNLAKVC ELLRDYLLPG APAGLYEELG KQLRTCTTLS GLASQIEAHH SLVLSHLKTL
LWREISNTNY S
