RHDF2_XENTR
ID RHDF2_XENTR Reviewed; 826 AA.
AC A0JPA1;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Inactive rhomboid protein 2;
DE Short=iRhom2;
DE AltName: Full=Rhomboid family member 2;
GN Name=rhbdf2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates ADAM17 protease, a sheddase of the epidermal growth
CC factor (EGF) receptor ligands and TNF, thereby plays a role in sleep,
CC cell survival, proliferation, migration and inflammation. Does not
CC exhibit any protease activity on its own.
CC {ECO:0000250|UniProtKB:Q80WQ6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q80WQ6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q80WQ6}. Cell membrane
CC {ECO:0000250|UniProtKB:Q6PJF5}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; BC127321; AAI27322.1; -; mRNA.
DR RefSeq; NP_001090673.1; NM_001097204.1.
DR RefSeq; XP_012826936.1; XM_012971482.2.
DR AlphaFoldDB; A0JPA1; -.
DR STRING; 8364.ENSXETP00000023104; -.
DR MEROPS; S54.953; -.
DR PaxDb; A0JPA1; -.
DR DNASU; 100036646; -.
DR GeneID; 100036646; -.
DR KEGG; xtr:100036646; -.
DR CTD; 79651; -.
DR Xenbase; XB-GENE-966769; rhbdf2.
DR eggNOG; KOG2290; Eukaryota.
DR HOGENOM; CLU_011531_1_1_1; -.
DR InParanoid; A0JPA1; -.
DR OrthoDB; 1253228at2759; -.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000019523; Expressed in early embryo and 15 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR InterPro; IPR022241; Rhomboid_SP.
DR Pfam; PF01694; Rhomboid; 1.
DR Pfam; PF12595; Rhomboid_SP; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Endoplasmic reticulum; Growth factor binding; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..826
FT /note="Inactive rhomboid protein 2"
FT /id="PRO_0000341940"
FT TOPO_DOM 1..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..626
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 663..683
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 684..685
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..706
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 707..717
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..738
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 739..743
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 744..764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 765..774
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 775..795
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 796..826
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 93843 MW; 30A271D7B3F87DA5 CRC64;
MASLKKNGSS SRLQDRKPPN LSITIPPVEG ERDPKLMQPL TKPVFQKSVS LQEPRGHVAE
GGTADVRPGF KRQTSLSQSI KRGTAQWFGV SNDWEGKRQQ WQRKSLHHCS LRYGKLKPQY
QRDIELPSQE TPSFQATESP ATHRLPKIVD PLARGRPFRH PDEVDRPRTP HVGLPPQTPG
MLSLASFTSV RSGYSRFPRR KRESVAHMSF RAAAALIKGR PILDTPHSRK AGQKRSFIYP
SFMDEDTVDA AETLDSSFFS KVDMHDETFS MPDDVFDSPP MSASYFRAPL PIPELMPGAA
IEAAKEPVKS VQVYTPDHRR GKRIASQVKH FAFDRKKRLY GLGVVGSWLN RTYRRSISST
VQSQLEHFNS HRPYFAYWIT FVHILITILA IATYGIAPIG FAQHTTSELV LRNKGVYESV
KYIQQENFWI GPSSIALIHL GAKFSPCIRY DEQIKNLIEK QHGLERESGC CIQNDKSGCV
QTHRKDCSET LATFIKWPEH DAPVLDEVTG MKRTSGAVCH QDPRTCEEPA SIQPHVWADD
ITKWPICTYQ AMNNHTGIRH MDCEIKGRPC CIGTKGSCEI TTREYCTFMH GYFHEEATLC
SQVHCLDEVC GLLPFLNPEY PDQFYRLWLS LFLHAGVIHC CVSVVFQMTV LRDLEKLAGW
LRISIIYILS GITGNLASAL FLPYRAEVGP AGSQFGLLAC LFVELFQSWQ ILAKPWKAFL
KLLGIVLFLF LFGLLPWIDN IAHIFGFLSG LLLSFSFLPY ITFGTADKFR KRAMIIISLL
VFVGLFASLV IWLYVYPINW AWIEYLTCLP FTNKFCEKYD IDQVLH
