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Rhomboid-related protein 4 (RRP4) (EC 3.4.21.105) (Rhomboid domain-containing protein 1) (Rhomboid-like protein 4)

 RHBL4_HUMAN             Reviewed;         315 AA.
Q8TEB9; Q495B9; Q53S43; Q5EBM8; Q6P5V8; Q8IV60; Q9H057;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
28-MAR-2018, entry version 111.
RecName: Full=Rhomboid-related protein 4;
Short=RRP4;
EC=3.4.21.105;
AltName: Full=Rhomboid domain-containing protein 1;
AltName: Full=Rhomboid-like protein 4;
Name=RHBDD1; Synonyms=RHBDL4; ORFNames=HSD-50, HSD50;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
Wang Y., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.;
"A new spermatogenesis-related gene.";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Eye, Lymph, and Pancreas;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 280-315.
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
FUNCTION IN CLEAVAGE OF BIK, ENZYME REGULATION, SUBCELLULAR LOCATION,
INTERACTION WITH BIK, AND MUTAGENESIS OF GLY-142 AND SER-144.
PubMed=18953687; DOI=10.1007/s00018-008-8452-0;
Wang Y., Guan X., Fok K.L., Li S., Zhang X., Miao S., Zong S.,
Koide S.S., Chan H.C., Wang L.;
"A novel member of the Rhomboid family, RHBDD1, regulates BIK-mediated
apoptosis.";
Cell. Mol. Life Sci. 65:3822-3829(2008).
[7]
FUNCTION IN CLEAVAGE OF STEAP3, INTERACTION WITH STEAP3, AND
MUTAGENESIS OF SER-144.
PubMed=22624035; DOI=10.1371/journal.pone.0037452;
Wan C., Fu J., Wang Y., Miao S., Song W., Wang L.;
"Exosome-related multi-pass transmembrane protein TSAP6 is a target of
rhomboid protease RHBDD1-induced proteolysis.";
PLoS ONE 7:E37452-E37452(2012).
[8]
INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=22795130; DOI=10.1016/j.molcel.2012.06.008;
Fleig L., Bergbold N., Sahasrabudhe P., Geiger B., Kaltak L.,
Lemberg M.K.;
"Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of
membrane proteins.";
Mol. Cell 47:558-569(2012).
-!- FUNCTION: Intramembrane-cleaving serine protease that cleaves
single transmembrane or multi-pass membrane proteins in the
hydrophobic plane of the membrane, luminal loops and juxtamembrane
regions. Involved in regulated intramembrane proteolysis and the
subsequent release of functional polypeptides from their membrane
anchors. Functional component of endoplasmic reticulum-associated
degradation (ERAD) for misfolded membrane proteins. Required for
the degradation process of some specific misfolded endoplasmic
reticulum (ER) luminal proteins. Participates in the transfer of
misfolded proteins from the ER to the cytosol, where they are
destroyed by the proteasome in a ubiquitin-dependent manner.
Functions in BIK, MPZ, PKD1, PTCRA, RHO, STEAP3 and TRAC
processing. Involved in the regulation of exosomal secretion;
inhibits the TSAP6-mediated secretion pathway. Involved in the
regulation of apoptosis; modulates BIK-mediated apoptotic
activity. Also plays a role in the regulation of spermatogenesis;
inhibits apoptotic activity in spermatogonia.
{ECO:0000269|PubMed:18953687, ECO:0000269|PubMed:22624035}.
-!- CATALYTIC ACTIVITY: Cleaves type-1 transmembrane domains using a
catalytic dyad composed of serine and histidine that are
contributed by different transmembrane domains.
-!- ENZYME REGULATION: Inhibited by aprotinin.
{ECO:0000269|PubMed:18953687}.
-!- SUBUNIT: Interacts (via C-terminal domain) with VCP. Interacts
with ubiquitin and ubiquitinated proteins (By similarity).
Interacts with BIK and STEAP3. {ECO:0000250,
ECO:0000269|PubMed:18953687, ECO:0000269|PubMed:22624035}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}. Endoplasmic reticulum membrane; Multi-pass
membrane protein. Mitochondrion {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8TEB9-1; Sequence=Displayed;
Name=2;
IsoId=Q8TEB9-2; Sequence=VSP_021203, VSP_021204;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed strongly in testis.
-!- INDUCTION: Up-regulated by endoplasmic reticulum stress agents
that induce the unfolded protein response (UPR).
{ECO:0000269|PubMed:22795130}.
-!- MISCELLANEOUS: According to PubMed:22795130; it is not localized
in the mitochondrion.
-!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY640233; AAU14246.1; -; mRNA.
EMBL; AK074258; BAB85031.1; -; mRNA.
EMBL; AC010735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073149; AAY24060.1; -; Genomic_DNA.
EMBL; BC027900; AAH27900.1; -; mRNA.
EMBL; BC062636; AAH62636.1; -; mRNA.
EMBL; BC089404; AAH89404.1; -; mRNA.
EMBL; BC101262; AAI01263.1; -; mRNA.
EMBL; BC101263; AAI01264.1; -; mRNA.
EMBL; BC101264; AAI01265.1; -; mRNA.
EMBL; BC101265; AAI01266.1; -; mRNA.
EMBL; BC111056; AAI11057.1; -; mRNA.
EMBL; AL512717; CAC21658.2; -; mRNA.
CCDS; CCDS2464.1; -. [Q8TEB9-1]
RefSeq; NP_001161080.1; NM_001167608.1. [Q8TEB9-1]
RefSeq; NP_115652.2; NM_032276.3. [Q8TEB9-1]
RefSeq; XP_016860572.1; XM_017005083.1. [Q8TEB9-1]
RefSeq; XP_016860573.1; XM_017005084.1. [Q8TEB9-1]
RefSeq; XP_016860574.1; XM_017005085.1. [Q8TEB9-1]
RefSeq; XP_016860575.1; XM_017005086.1. [Q8TEB9-1]
RefSeq; XP_016860576.1; XM_017005087.1. [Q8TEB9-1]
RefSeq; XP_016860577.1; XM_017005088.1. [Q8TEB9-1]
RefSeq; XP_016860578.1; XM_017005089.1. [Q8TEB9-1]
RefSeq; XP_016860579.1; XM_017005090.1. [Q8TEB9-1]
RefSeq; XP_016860580.1; XM_017005091.1. [Q8TEB9-1]
RefSeq; XP_016860581.1; XM_017005092.1. [Q8TEB9-1]
UniGene; Hs.471514; -.
UniGene; Hs.548040; -.
UniGene; Hs.664759; -.
PDB; 5EPP; X-ray; 1.88 A; B=300-314.
PDBsum; 5EPP; -.
ProteinModelPortal; Q8TEB9; -.
SMR; Q8TEB9; -.
BioGrid; 123968; 39.
IntAct; Q8TEB9; 7.
STRING; 9606.ENSP00000344779; -.
MEROPS; S54.008; -.
TCDB; 9.B.104.4.1; the rhomboid protease (rhomboid) family.
iPTMnet; Q8TEB9; -.
PhosphoSitePlus; Q8TEB9; -.
BioMuta; RHBDD1; -.
DMDM; 74723955; -.
EPD; Q8TEB9; -.
MaxQB; Q8TEB9; -.
PaxDb; Q8TEB9; -.
PeptideAtlas; Q8TEB9; -.
PRIDE; Q8TEB9; -.
Ensembl; ENST00000341329; ENSP00000344779; ENSG00000144468. [Q8TEB9-1]
Ensembl; ENST00000392062; ENSP00000375914; ENSG00000144468. [Q8TEB9-1]
GeneID; 84236; -.
KEGG; hsa:84236; -.
UCSC; uc002voi.4; human. [Q8TEB9-1]
CTD; 84236; -.
DisGeNET; 84236; -.
EuPathDB; HostDB:ENSG00000144468.16; -.
GeneCards; RHBDD1; -.
HGNC; HGNC:23081; RHBDD1.
HPA; HPA013972; -.
HPA; HPA057125; -.
MIM; 617515; gene.
neXtProt; NX_Q8TEB9; -.
OpenTargets; ENSG00000144468; -.
PharmGKB; PA143485593; -.
eggNOG; KOG2632; Eukaryota.
eggNOG; ENOG41100KJ; LUCA.
GeneTree; ENSGT00390000010744; -.
HOVERGEN; HBG054446; -.
InParanoid; Q8TEB9; -.
KO; K09651; -.
OMA; LHHADDW; -.
OrthoDB; EOG091G0GYT; -.
PhylomeDB; Q8TEB9; -.
TreeFam; TF328476; -.
ChiTaRS; RHBDD1; human.
GenomeRNAi; 84236; -.
PRO; PR:Q8TEB9; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000144468; -.
CleanEx; HS_RHBDD1; -.
ExpressionAtlas; Q8TEB9; baseline and differential.
Genevisible; Q8TEB9; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0044322; C:endoplasmic reticulum quality control compartment; ISS:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0034620; P:cellular response to unfolded protein; IEP:ParkinsonsUK-UCL.
GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; ISS:UniProtKB.
GO; GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB.
GO; GO:1904211; P:membrane protein proteolysis involved in retrograde protein transport, ER to cytosol; ISS:ParkinsonsUK-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
GO; GO:0010954; P:positive regulation of protein processing; ISS:UniProtKB.
GO; GO:0051047; P:positive regulation of secretion; IMP:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
GO; GO:0048515; P:spermatid differentiation; ISS:UniProtKB.
Gene3D; 1.20.1540.10; -; 1.
InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
InterPro; IPR035952; Rhomboid-like_sf.
Pfam; PF01694; Rhomboid; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Differentiation; Endoplasmic reticulum; Hydrolase; Membrane;
Mitochondrion; Polymorphism; Protease; Reference proteome;
Serine protease; Spermatogenesis; Transmembrane; Transmembrane helix.
CHAIN 1 315 Rhomboid-related protein 4.
/FTId=PRO_0000254189.
TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TOPO_DOM 43 106 Extracellular. {ECO:0000255}.
TRANSMEM 107 127 Helical. {ECO:0000255}.
TOPO_DOM 128 145 Cytoplasmic. {ECO:0000255}.
TRANSMEM 146 166 Helical. {ECO:0000255}.
TOPO_DOM 167 180 Extracellular. {ECO:0000255}.
TRANSMEM 181 201 Helical. {ECO:0000255}.
TOPO_DOM 202 315 Cytoplasmic. {ECO:0000255}.
REGION 269 284 Ubiquitin-binding domain (UBD).
{ECO:0000250}.
REGION 301 315 VCP/p97-interacting motif (VIM).
{ECO:0000250}.
ACT_SITE 144 144 Nucleophile. {ECO:0000250}.
ACT_SITE 195 195 {ECO:0000250}.
VAR_SEQ 1 209 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021203.
VAR_SEQ 210 218 LKKIMEACA -> MPVFLFKPK (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021204.
VARIANT 110 110 A -> T (in dbSNP:rs35731955).
/FTId=VAR_034454.
MUTAGEN 142 142 G->A: Enzyme inactivation. Reduces the
cleavage of BIK.
{ECO:0000269|PubMed:18953687}.
MUTAGEN 144 144 S->A: Enzyme inactivation. Reduces the
cleavage of BIK and TSAP6. Increases
TSAP6-mediated exosome secretion.
{ECO:0000269|PubMed:18953687,
ECO:0000269|PubMed:22624035}.
CONFLICT 263 263 T -> M (in Ref. 4; AAI01263).
{ECO:0000305}.
HELIX 301 313 {ECO:0000244|PDB:5EPP}.
SEQUENCE 315 AA; 35823 MW; AF81BA8D907BDC63 CRC64;
MQRRSRGINT GLILLLSQIF HVGINNIPPV TLATLALNIW FFLNPQKPLY SSCLSVEKCY
QQKDWQRLLL SPLHHADDWH LYFNMASMLW KGINLERRLG SRWFAYVITA FSVLTGVVYL
LLQFAVAEFM DEPDFKRSCA VGFSGVLFAL KVLNNHYCPG GFVNILGFPV PNRFACWVEL
VAIHLFSPGT SFAGHLAGIL VGLMYTQGPL KKIMEACAGG FSSSVGYPGR QYYFNSSGSS
GYQDYYPHGR PDHYEEAPRN YDTYTAGLSE EEQLERALQA SLWDRGNTRN SPPPYGFHLS
PEEMRRQRLH RFDSQ


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