RHBD2_MOUSE
ID RHBD2_MOUSE Reviewed; 361 AA.
AC Q8VEK2; Q3TT71; Q4G0C4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Rhomboid domain-containing protein 2;
DE AltName: Full=Rhomboid-like protein 7;
GN Name=Rhbdd2; Synonyms=Rhbdl7;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Lung, Pituitary, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF SER-185; GLY-189; GLY-193 AND GLY-197.
RX PubMed=23386608; DOI=10.1074/jbc.m112.419960;
RA Ahmedli N.B., Gribanova Y., Njoku C.C., Naidu A., Young A., Mendoza E.,
RA Yamashita C.K., Ozgul R.K., Johnson J.E., Fox D.A., Farber D.B.;
RT "Dynamics of the rhomboid-like protein RHBDD2 expression in mouse retina
RT and involvement of its human ortholog in retinitis pigmentosa.";
RL J. Biol. Chem. 288:9742-9754(2013).
CC -!- SUBUNIT: Might form homotrimers; these trimers are only formed in
CC retina. {ECO:0000269|PubMed:23386608}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:23386608}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23386608}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VEK2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VEK2-2; Sequence=VSP_021249;
CC -!- TISSUE SPECIFICITY: Widely expressed, including in retina and brain (at
CC protein level), as well as in kidney, testis and ovary. Expressed in
CC all layers of the retina, including inner segments of photoreceptor
CC cells and ganglion cells (at protein level).
CC {ECO:0000269|PubMed:23386608}.
CC -!- DEVELOPMENTAL STAGE: In the developing eye, already detected at 10.5
CC dpc. Expression increases from 12.5 though 18.5 dpc in all retinal
CC cells (at protein level). At P1, expressed in a small number of cells
CC at the level of the ganglion cell layer and in the inner edge of the
CC ventricular zone of the retina. The number of expressing cells
CC increases and, by P8 to P11, entirely occupies the ganglion cell layer
CC and inner nuclear layer. At that stage, not detected in the
CC photoreceptor cell bodies of the outer nuclear layer. At P21, expressed
CC in all nuclear layers of the retina, including cones (at protein
CC level). {ECO:0000269|PubMed:23386608}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC -!- CAUTION: Although strongly related to the peptidase S54 family, it
CC lacks the conserved active sites, suggesting that it has no peptidase
CC activity. {ECO:0000305}.
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DR EMBL; AK041845; BAC31081.1; -; mRNA.
DR EMBL; AK161545; BAE36454.1; -; mRNA.
DR EMBL; AK165926; BAE38463.1; -; mRNA.
DR EMBL; BC018360; AAH18360.1; -; mRNA.
DR EMBL; BC098493; AAH98493.1; -; mRNA.
DR CCDS; CCDS19743.1; -. [Q8VEK2-1]
DR RefSeq; NP_666114.1; NM_146002.2. [Q8VEK2-1]
DR AlphaFoldDB; Q8VEK2; -.
DR BioGRID; 229600; 2.
DR STRING; 10090.ENSMUSP00000049060; -.
DR MEROPS; S54.955; -.
DR PhosphoSitePlus; Q8VEK2; -.
DR SwissPalm; Q8VEK2; -.
DR MaxQB; Q8VEK2; -.
DR PaxDb; Q8VEK2; -.
DR PRIDE; Q8VEK2; -.
DR ProteomicsDB; 255325; -. [Q8VEK2-1]
DR ProteomicsDB; 255326; -. [Q8VEK2-2]
DR Antibodypedia; 48862; 47 antibodies from 19 providers.
DR DNASU; 215160; -.
DR Ensembl; ENSMUST00000043707; ENSMUSP00000049060; ENSMUSG00000039917. [Q8VEK2-1]
DR GeneID; 215160; -.
DR KEGG; mmu:215160; -.
DR UCSC; uc008zyr.1; mouse. [Q8VEK2-1]
DR CTD; 57414; -.
DR MGI; MGI:1915612; Rhbdd2.
DR VEuPathDB; HostDB:ENSMUSG00000039917; -.
DR eggNOG; KOG2632; Eukaryota.
DR GeneTree; ENSGT00390000000699; -.
DR HOGENOM; CLU_064872_1_0_1; -.
DR InParanoid; Q8VEK2; -.
DR OMA; HCFFTLI; -.
DR OrthoDB; 895980at2759; -.
DR PhylomeDB; Q8VEK2; -.
DR TreeFam; TF335461; -.
DR BioGRID-ORCS; 215160; 7 hits in 72 CRISPR screens.
DR PRO; PR:Q8VEK2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8VEK2; protein.
DR Bgee; ENSMUSG00000039917; Expressed in superior frontal gyrus and 200 other tissues.
DR ExpressionAtlas; Q8VEK2; baseline and differential.
DR Genevisible; Q8VEK2; MM.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR Pfam; PF01694; Rhomboid; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Golgi apparatus; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..361
FT /note="Rhomboid domain-containing protein 2"
FT /id="PRO_0000254597"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 265..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..222
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021249"
FT MUTAGEN 185
FT /note="S->L: No effect on cis-Golgi localization."
FT /evidence="ECO:0000269|PubMed:23386608"
FT MUTAGEN 189
FT /note="G->L: Loss of cis-Golgi localization."
FT /evidence="ECO:0000269|PubMed:23386608"
FT MUTAGEN 193
FT /note="G->L: Loss of cis-Golgi localization."
FT /evidence="ECO:0000269|PubMed:23386608"
FT MUTAGEN 197
FT /note="G->L: No effect on cis-Golgi localization."
FT /evidence="ECO:0000269|PubMed:23386608"
FT CONFLICT 238
FT /note="E -> K (in Ref. 2; AAH98493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 39108 MW; 27AB709BF3E232B8 CRC64;
MAAPGPASRF WCSCPEVPSA TFFTALLSLL VSGPRLFLLQ PPLAPSGLSL RSEALRNWQV
YRLVTYIFVY ENPVSLLCGA IIIWRFAGNF ERTVGTVRHC FFTLIFTVFS AIIYLSFESV
SSLSKLGEVE DARGFTPVAF AMLGVTSVRS RMRRALVFGV VVPSVLVPWL LLCASWLIPQ
TSFLSNVSGL LIGLSYGLTY CYSLDLSERV ALKLDQKFPF SLMRRIPLFK YISGSSAERR
AAQSRRLNPA PGSYPTQSCH PHLTPSYPVT QMQHASGQKL ASWPPGHMPS LPPYQPASGL
CYVQNHFGPN PNASSVYPAS AGTSQGVQPP SPISCPGTVY SGALGTPGAT GSKESSKVAM
P
