(data stored in ACNUC603 zone)

HOGENOM: CAVPO132_2_PE17

ID   CAVPO132_2_PE17                      STANDARD;      PRT;   229 AA.
AC   CAVPO132_2_PE17; Q60490; Q9QV23;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase; EC=5.3.3
DE   5;AltName: Full=Cholestenol Delta-isomerase;AltName:
DE   Full=Delta(8)-Delta(7) sterol isomerase; Short=D8-D7 sterol
DE   isomerase;AltName: Full=Emopamil-binding protein; (CAVPO132_2.PE17).
GN   Name=EBP;
OS   CAVIA PORCELLUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Hystricognathi; Caviidae; Cavia.
OX   NCBI_TaxID=10141;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CAVPO132_2.PE17.
CC       Cavia porcellus scaffold scaffold_132 cavPor3 partial sequence
CC       1000001..2000000 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:EBP_CAVPO
CC   -!- FUNCTION: Catalyzes the conversion of Delta(8)-sterols to their
CC       corresponding Delta(7)-isomers (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5-alpha-cholest-7-en-3-beta-ol = 5-alpha-
CC       cholest-8-en-3-beta-ol.
CC   -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver, bowel, adrenal
CC       gland, testis, ovary, and uterus and less expressed in brain,
CC       cerebellum, skeletal muscle, and heart.
CC   -!- MISCELLANEOUS: Binds to the phenylalkylamine calcium-ion
CC       antagonist emopamil, an anti-ischemic drug.
CC   -!- SIMILARITY: Belongs to the EBP family.
CC   -!- GENE_FAMILY: HOG000204543 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Cavia_porcellus;ENSCPOG00000014151;ENSCPOT00000014293;ENSCPOP00000012749.
DR   EMBL; Z37985; - ;
DR   UniProtKB/Swiss-Prot; Q60490; Q9QV23; -.
DR   EMBL; Z37985; CAA86067.1; -; mRNA.
DR   PIR; A56122; A56122.
DR   RefSeq; NP_001166416.1; NM_001172945.1.
DR   STRING; Q60490; -.
DR   Ensembl; ENSCPOT00000014293; ENSCPOP00000012749; ENSCPOG00000014151.
DR   GeneID; 100135518; -.
DR   CTD; 10682; -.
DR   eggNOG; roNOG13731; -.
DR   GeneTree; ENSGT00530000063715; -.
DR   InParanoid; Q60490; -.
DR   OMA; PTWHILA; -.
DR   OrthoDB; EOG45490D; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047750; F:cholestenol delta-isomerase activity; IEA:EC.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR007905; EBP.
DR   PANTHER; PTHR14207; EBP; 1.
DR   Pfam; PF05241; EBP; 1.
DR   HOGENOMDNA; CAVPO132_2.PE17; -.
KW   ENSCPOG00000014151fold_1320000031; ENSCPOP00000012749fold_1320000031;
KW   Z37985;
KW   Cholesterol biosynthesis; Direct protein sequencing;
KW   Endoplasmic reticulum; Isomerase; Lipid synthesis; Membrane;
KW   Steroid biosynthesis; Sterol biosynthesis; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   229 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MATTSTGPLH PYWPRHLRLD HFVPNDLSAW YIVTVLFTVF GALVVTMWLL SSRASVVPLG
     TWRRLSVCWF AVCAFVHLVI EGWFVLYQKA ILGDQAFLSQ LWKEYAKGDS RYIIEDNFII
     CMESITVVLW GPLSLWAVIA FLRQHPSRYV LQFVISLGQI YGDLLYFLTE YRDGFQHGEM
     GHPIYFWFYF FFMNVLWLVI PGVLFFDSVK QFYGAQNALD TKVMKSKGK
//

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