RHBL4_HUMAN
ID RHBL4_HUMAN Reviewed; 315 AA.
AC Q8TEB9; Q495B9; Q53S43; Q5EBM8; Q6P5V8; Q8IV60; Q9H057;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Rhomboid-related protein 4;
DE Short=RRP4;
DE EC=3.4.21.105;
DE AltName: Full=Rhomboid domain-containing protein 1;
DE AltName: Full=Rhomboid-like protein 4;
GN Name=RHBDD1; Synonyms=RHBDL4; ORFNames=HSD-50, HSD50;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Wang Y., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.;
RT "A new spermatogenesis-related gene.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, Lymph, and Pancreas;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 280-315.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION IN CLEAVAGE OF BIK, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP INTERACTION WITH BIK, AND MUTAGENESIS OF GLY-142 AND SER-144.
RX PubMed=18953687; DOI=10.1007/s00018-008-8452-0;
RA Wang Y., Guan X., Fok K.L., Li S., Zhang X., Miao S., Zong S., Koide S.S.,
RA Chan H.C., Wang L.;
RT "A novel member of the Rhomboid family, RHBDD1, regulates BIK-mediated
RT apoptosis.";
RL Cell. Mol. Life Sci. 65:3822-3829(2008).
RN [7]
RP FUNCTION IN CLEAVAGE OF STEAP3, INTERACTION WITH STEAP3, AND MUTAGENESIS OF
RP SER-144.
RX PubMed=22624035; DOI=10.1371/journal.pone.0037452;
RA Wan C., Fu J., Wang Y., Miao S., Song W., Wang L.;
RT "Exosome-related multi-pass transmembrane protein TSAP6 is a target of
RT rhomboid protease RHBDD1-induced proteolysis.";
RL PLoS ONE 7:E37452-E37452(2012).
RN [8]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22795130; DOI=10.1016/j.molcel.2012.06.008;
RA Fleig L., Bergbold N., Sahasrabudhe P., Geiger B., Kaltak L., Lemberg M.K.;
RT "Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of
RT membrane proteins.";
RL Mol. Cell 47:558-569(2012).
CC -!- FUNCTION: Intramembrane-cleaving serine protease that cleaves single
CC transmembrane or multi-pass membrane proteins in the hydrophobic plane
CC of the membrane, luminal loops and juxtamembrane regions. Involved in
CC regulated intramembrane proteolysis and the subsequent release of
CC functional polypeptides from their membrane anchors. Functional
CC component of endoplasmic reticulum-associated degradation (ERAD) for
CC misfolded membrane proteins. Required for the degradation process of
CC some specific misfolded endoplasmic reticulum (ER) luminal proteins.
CC Participates in the transfer of misfolded proteins from the ER to the
CC cytosol, where they are destroyed by the proteasome in a ubiquitin-
CC dependent manner. Functions in BIK, MPZ, PKD1, PTCRA, RHO, STEAP3 and
CC TRAC processing. Involved in the regulation of exosomal secretion;
CC inhibits the TSAP6-mediated secretion pathway. Involved in the
CC regulation of apoptosis; modulates BIK-mediated apoptotic activity.
CC Also plays a role in the regulation of spermatogenesis; inhibits
CC apoptotic activity in spermatogonia. {ECO:0000269|PubMed:18953687,
CC ECO:0000269|PubMed:22624035}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad
CC composed of serine and histidine that are contributed by different
CC transmembrane domains.; EC=3.4.21.105;
CC -!- ACTIVITY REGULATION: Inhibited by aprotinin.
CC {ECO:0000269|PubMed:18953687}.
CC -!- SUBUNIT: Interacts (via C-terminal domain) with VCP. Interacts with
CC ubiquitin and ubiquitinated proteins (By similarity). Interacts with
CC BIK and STEAP3. {ECO:0000250, ECO:0000269|PubMed:18953687,
CC ECO:0000269|PubMed:22624035}.
CC -!- INTERACTION:
CC Q8TEB9; Q99675: CGRRF1; NbExp=3; IntAct=EBI-9916444, EBI-2130213;
CC Q8TEB9; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-9916444, EBI-11522780;
CC Q8TEB9; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-9916444, EBI-6942903;
CC Q8TEB9; P04921: GYPC; NbExp=3; IntAct=EBI-9916444, EBI-7797098;
CC Q8TEB9; Q7L5N7: LPCAT2; NbExp=3; IntAct=EBI-9916444, EBI-4280011;
CC Q8TEB9; Q15738: NSDHL; NbExp=3; IntAct=EBI-9916444, EBI-4280135;
CC Q8TEB9; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-9916444, EBI-373552;
CC Q8TEB9; Q59EV6: PPGB; NbExp=3; IntAct=EBI-9916444, EBI-14210385;
CC Q8TEB9; Q99942: RNF5; NbExp=3; IntAct=EBI-9916444, EBI-348482;
CC Q8TEB9; O75396: SEC22B; NbExp=3; IntAct=EBI-9916444, EBI-1058865;
CC Q8TEB9; Q8N2U9: SLC66A2; NbExp=3; IntAct=EBI-9916444, EBI-3907610;
CC Q8TEB9; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-9916444, EBI-12038591;
CC Q8TEB9; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-9916444, EBI-2548832;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22795130}; Multi-pass membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:18953687};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TEB9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TEB9-2; Sequence=VSP_021203, VSP_021204;
CC -!- TISSUE SPECIFICITY: Expressed strongly in testis.
CC -!- INDUCTION: Up-regulated by endoplasmic reticulum stress agents that
CC induce the unfolded protein response (UPR).
CC {ECO:0000269|PubMed:22795130}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC -!- CAUTION: One study reported that the protein is not localized in the
CC mitochondrion. {ECO:0000305|PubMed:22795130}.
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DR EMBL; AY640233; AAU14246.1; -; mRNA.
DR EMBL; AK074258; BAB85031.1; -; mRNA.
DR EMBL; AC010735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073149; AAY24060.1; -; Genomic_DNA.
DR EMBL; BC027900; AAH27900.1; -; mRNA.
DR EMBL; BC062636; AAH62636.1; -; mRNA.
DR EMBL; BC089404; AAH89404.1; -; mRNA.
DR EMBL; BC101262; AAI01263.1; -; mRNA.
DR EMBL; BC101263; AAI01264.1; -; mRNA.
DR EMBL; BC101264; AAI01265.1; -; mRNA.
DR EMBL; BC101265; AAI01266.1; -; mRNA.
DR EMBL; BC111056; AAI11057.1; -; mRNA.
DR EMBL; AL512717; CAC21658.2; -; mRNA.
DR CCDS; CCDS2464.1; -. [Q8TEB9-1]
DR RefSeq; NP_001161080.1; NM_001167608.1. [Q8TEB9-1]
DR RefSeq; NP_115652.2; NM_032276.3. [Q8TEB9-1]
DR RefSeq; XP_016860572.1; XM_017005083.1. [Q8TEB9-1]
DR RefSeq; XP_016860573.1; XM_017005084.1. [Q8TEB9-1]
DR RefSeq; XP_016860574.1; XM_017005085.1. [Q8TEB9-1]
DR RefSeq; XP_016860575.1; XM_017005086.1. [Q8TEB9-1]
DR RefSeq; XP_016860576.1; XM_017005087.1. [Q8TEB9-1]
DR RefSeq; XP_016860577.1; XM_017005088.1. [Q8TEB9-1]
DR RefSeq; XP_016860578.1; XM_017005089.1.
DR RefSeq; XP_016860579.1; XM_017005090.1. [Q8TEB9-1]
DR RefSeq; XP_016860580.1; XM_017005091.1.
DR RefSeq; XP_016860581.1; XM_017005092.1. [Q8TEB9-1]
DR PDB; 5EPP; X-ray; 1.88 A; B=300-314.
DR PDBsum; 5EPP; -.
DR AlphaFoldDB; Q8TEB9; -.
DR SMR; Q8TEB9; -.
DR BioGRID; 123968; 344.
DR IntAct; Q8TEB9; 28.
DR STRING; 9606.ENSP00000375914; -.
DR MEROPS; S54.008; -.
DR TCDB; 9.B.104.4.1; the rhomboid protease (rhomboid) family.
DR iPTMnet; Q8TEB9; -.
DR PhosphoSitePlus; Q8TEB9; -.
DR BioMuta; RHBDD1; -.
DR DMDM; 74723955; -.
DR EPD; Q8TEB9; -.
DR jPOST; Q8TEB9; -.
DR MassIVE; Q8TEB9; -.
DR MaxQB; Q8TEB9; -.
DR PaxDb; Q8TEB9; -.
DR PeptideAtlas; Q8TEB9; -.
DR PRIDE; Q8TEB9; -.
DR ProteomicsDB; 74441; -. [Q8TEB9-1]
DR ProteomicsDB; 74442; -. [Q8TEB9-2]
DR Antibodypedia; 3019; 75 antibodies from 25 providers.
DR DNASU; 84236; -.
DR Ensembl; ENST00000341329.7; ENSP00000344779.3; ENSG00000144468.17. [Q8TEB9-1]
DR Ensembl; ENST00000392062.7; ENSP00000375914.2; ENSG00000144468.17. [Q8TEB9-1]
DR GeneID; 84236; -.
DR KEGG; hsa:84236; -.
DR MANE-Select; ENST00000392062.7; ENSP00000375914.2; NM_001167608.3; NP_001161080.1.
DR UCSC; uc002voi.4; human. [Q8TEB9-1]
DR CTD; 84236; -.
DR DisGeNET; 84236; -.
DR GeneCards; RHBDD1; -.
DR HGNC; HGNC:23081; RHBDD1.
DR HPA; ENSG00000144468; Low tissue specificity.
DR MIM; 617515; gene.
DR neXtProt; NX_Q8TEB9; -.
DR OpenTargets; ENSG00000144468; -.
DR PharmGKB; PA143485593; -.
DR VEuPathDB; HostDB:ENSG00000144468; -.
DR eggNOG; KOG2632; Eukaryota.
DR GeneTree; ENSGT00390000010744; -.
DR HOGENOM; CLU_075166_0_0_1; -.
DR InParanoid; Q8TEB9; -.
DR OMA; SIWFAYI; -.
DR PhylomeDB; Q8TEB9; -.
DR TreeFam; TF328476; -.
DR BRENDA; 3.4.21.105; 2681.
DR PathwayCommons; Q8TEB9; -.
DR SignaLink; Q8TEB9; -.
DR BioGRID-ORCS; 84236; 6 hits in 1074 CRISPR screens.
DR ChiTaRS; RHBDD1; human.
DR GenomeRNAi; 84236; -.
DR Pharos; Q8TEB9; Tbio.
DR PRO; PR:Q8TEB9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8TEB9; protein.
DR Bgee; ENSG00000144468; Expressed in bone marrow cell and 187 other tissues.
DR ExpressionAtlas; Q8TEB9; baseline and differential.
DR Genevisible; Q8TEB9; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0034620; P:cellular response to unfolded protein; IEP:ParkinsonsUK-UCL.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
DR GO; GO:0031293; P:membrane protein intracellular domain proteolysis; ISS:UniProtKB.
DR GO; GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB.
DR GO; GO:1904211; P:membrane protein proteolysis involved in retrograde protein transport, ER to cytosol; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0010954; P:positive regulation of protein processing; ISS:UniProtKB.
DR GO; GO:0051047; P:positive regulation of secretion; IMP:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR GO; GO:0048515; P:spermatid differentiation; ISS:UniProtKB.
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 3D-structure; Alternative splicing; Apoptosis; Differentiation;
KW Endoplasmic reticulum; Hydrolase; Membrane; Mitochondrion; Protease;
KW Reference proteome; Serine protease; Spermatogenesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..315
FT /note="Rhomboid-related protein 4"
FT /id="PRO_0000254189"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 269..284
FT /note="Ubiquitin-binding domain (UBD)"
FT /evidence="ECO:0000250"
FT REGION 283..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..315
FT /note="VCP/p97-interacting motif (VIM)"
FT /evidence="ECO:0000250"
FT COMPBIAS 301..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 195
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..209
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021203"
FT VAR_SEQ 210..218
FT /note="LKKIMEACA -> MPVFLFKPK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021204"
FT VARIANT 110
FT /note="A -> T (in dbSNP:rs35731955)"
FT /id="VAR_034454"
FT MUTAGEN 142
FT /note="G->A: Enzyme inactivation. Reduces the cleavage of
FT BIK."
FT /evidence="ECO:0000269|PubMed:18953687"
FT MUTAGEN 144
FT /note="S->A: Enzyme inactivation. Reduces the cleavage of
FT BIK and TSAP6. Increases TSAP6-mediated exosome secretion."
FT /evidence="ECO:0000269|PubMed:18953687,
FT ECO:0000269|PubMed:22624035"
FT CONFLICT 263
FT /note="T -> M (in Ref. 4; AAI01263)"
FT /evidence="ECO:0000305"
FT HELIX 301..313
FT /evidence="ECO:0007829|PDB:5EPP"
SQ 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
