SCAP_CRIGR
ID SCAP_CRIGR Reviewed; 1276 AA.
AC P97260; Q2WEK9;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Sterol regulatory element-binding protein cleavage-activating protein {ECO:0000303|PubMed:8898195};
DE Short=SCAP {ECO:0000303|PubMed:8898195};
DE Short=SREBP cleavage-activating protein {ECO:0000303|PubMed:8898195};
GN Name=SCAP {ECO:0000303|PubMed:8898195};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF ASP-443.
RC TISSUE=Ovary;
RX PubMed=8898195; DOI=10.1016/s0092-8674(00)81362-8;
RA Hua X., Nohturfft A., Goldstein J.L., Brown M.S.;
RT "Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-
RT activating protein.";
RL Cell 87:415-426(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 56-522, FUNCTION, INTERACTION WITH INSIG1 AND
RP INSIG2, AND MUTAGENESIS OF TYR-298; LEU-315 AND ASP-443.
RC TISSUE=Ovary;
RX PubMed=12482938; DOI=10.1073/pnas.262669399;
RA Yabe D., Xia Z.-P., Adams C.M., Rawson R.B.;
RT "Three mutations in sterol-sensing domain of SCAP block interaction with
RT insig and render SREBP cleavage insensitive to sterols.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16672-16677(2002).
RN [3]
RP INTERACTION WITH SREBF2.
RX PubMed=9488713; DOI=10.1074/jbc.273.10.5785;
RA Sakai J., Nohturfft A., Goldstein J.L., Brown M.S.;
RT "Cleavage of sterol regulatory element-binding proteins (SREBPs) at site-1
RT requires interaction with SREBP cleavage-activating protein. Evidence from
RT in vivo competition studies.";
RL J. Biol. Chem. 273:5785-5793(1998).
RN [4]
RP TOPOLOGY, AND GLYCOSYLATION AT ASN-263; ASN-590 AND ASN-641.
RX PubMed=9642295; DOI=10.1074/jbc.273.27.17243;
RA Nohturfft A., Brown M.S., Goldstein J.L.;
RT "Topology of SREBP cleavage-activating protein, a polytopic membrane
RT protein with a sterol-sensing domain.";
RL J. Biol. Chem. 273:17243-17250(1998).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10497220; DOI=10.1074/jbc.274.40.28549;
RA Rawson R.B., DeBose-Boyd R., Goldstein J.L., Brown M.S.;
RT "Failure to cleave sterol regulatory element-binding proteins (SREBPs)
RT causes cholesterol auxotrophy in Chinese hamster ovary cells with genetic
RT absence of SREBP cleavage-activating protein.";
RL J. Biol. Chem. 274:28549-28556(1999).
RN [6]
RP SUBCELLULAR LOCATION, CLEAVAGE BY MBTPS1, AND MUTAGENESIS OF TYR-298.
RC TISSUE=Ovary;
RX PubMed=10500160; DOI=10.1073/pnas.96.20.11235;
RA Nohturfft A., DeBose-Boyd R.A., Scheek S., Goldstein J.L., Brown M.S.;
RT "Sterols regulate cycling of SREBP cleavage-activating protein (SCAP)
RT between endoplasmic reticulum and Golgi.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11235-11240(1999).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=10896675; DOI=10.1074/jbc.m005439200;
RA Yang T., Goldstein J.L., Brown M.S.;
RT "Overexpression of membrane domain of SCAP prevents sterols from inhibiting
RT SCAP.SREBP exit from endoplasmic reticulum.";
RL J. Biol. Chem. 275:29881-29886(2000).
RN [8]
RP INTERACTION WITH THE SEC23/SEC24 COMPLEX.
RX PubMed=12193656; DOI=10.1073/pnas.182412799;
RA Espenshade P.J., Li W.-P., Yabe D.;
RT "Sterols block binding of COPII proteins to SCAP, thereby controlling SCAP
RT sorting in ER.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11694-11699(2002).
RN [9]
RP FUNCTION, INTERACTION WITH CHOLESTEROL, AND MUTAGENESIS OF TYR-298.
RX PubMed=15260976; DOI=10.1016/j.molcel.2004.06.019;
RA Radhakrishnan A., Sun L.-P., Kwon H.J., Brown M.S., Goldstein J.L.;
RT "Direct binding of cholesterol to the purified membrane region of SCAP:
RT mechanism for a sterol-sensing domain.";
RL Mol. Cell 15:259-268(2004).
RN [10]
RP FUNCTION, ER EXPORT SIGNAL, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP TYR-298; LEU-449; 445-ARG-ARG-446; 447-MET-GLU-448 AND 451-ASP-LEU-452.
RX PubMed=15899885; DOI=10.1074/jbc.m504041200;
RA Sun L.-P., Li L., Goldstein J.L., Brown M.S.;
RT "Insig required for sterol-mediated inhibition of Scap/SREBP binding to
RT COPII proteins in vitro.";
RL J. Biol. Chem. 280:26483-26490(2005).
RN [11]
RP FUNCTION, INTERACTION WITH INSIG1 AND INSIG2, AND MUTAGENESIS OF ASP-428.
RX PubMed=15728349; DOI=10.1073/pnas.0500206102;
RA Feramisco J.D., Radhakrishnan A., Ikeda Y., Reitz J., Brown M.S.,
RA Goldstein J.L.;
RT "Intramembrane aspartic acid in SCAP protein governs cholesterol-induced
RT conformational change.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3242-3247(2005).
RN [12]
RP FUNCTION, MUTAGENESIS OF VAL-439; ARG-446; ASN-453; 437-THR-THR-438;
RP 439-VAL-LEU-440; 444-ILE-ARG-445 AND 363-PRO--PRO-492, AND DOMAIN.
RX PubMed=17428919; DOI=10.1073/pnas.0700907104;
RA Sun L.-P., Seemann J., Goldstein J.L., Brown M.S.;
RT "Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi:
RT Insig renders sorting signal in Scap inaccessible to COPII proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:6519-6526(2007).
RN [13]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF TYR-234 AND TYR-640.
RX PubMed=27068746; DOI=10.1074/jbc.m116.729798;
RA Zhang Y., Lee K.M., Kinch L.N., Clark L., Grishin N.V., Rosenbaum D.M.,
RA Brown M.S., Goldstein J.L., Radhakrishnan A.;
RT "Direct Demonstration That Loop1 of Scap Binds to Loop7: A crucial event in
RT cholesterol homeostasis.";
RL J. Biol. Chem. 291:12888-12896(2016).
CC -!- FUNCTION: Escort protein required for cholesterol as well as lipid
CC homeostasis (PubMed:8898195, PubMed:10497220, PubMed:12482938,
CC PubMed:15728349, PubMed:15899885, PubMed:17428919). Regulates export of
CC the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon
CC low cholesterol, thereby regulating the processing of sterol regulatory
CC element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2
CC (PubMed:8898195, PubMed:10497220, PubMed:12482938, PubMed:15728349,
CC PubMed:15899885, PubMed:17428919, PubMed:27068746). At high sterol
CC concentrations, formation of a ternary complex with INSIG (INSIG1 or
CC INSIG2) leads to mask the ER export signal in SCAP, promoting retention
CC of the complex in the endoplasmic reticulum (PubMed:12482938,
CC PubMed:15728349, PubMed:15899885, PubMed:27068746). Low sterol
CC concentrations trigger release of INSIG, a conformational change in the
CC SSD domain of SCAP, unmasking of the ER export signal, promoting
CC recruitment into COPII-coated vesicles and transport of the SCAP-SREBP
CC to the Golgi: in the Golgi, SREBPs are then processed, releasing the
CC transcription factor fragment of SREBPs from the membrane, its import
CC into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate
CC pathway (PubMed:15728349, PubMed:15899885, PubMed:17428919,
CC PubMed:27068746). Binds cholesterol via its SSD domain
CC (PubMed:15260976, PubMed:27068746). {ECO:0000269|PubMed:10497220,
CC ECO:0000269|PubMed:12482938, ECO:0000269|PubMed:15260976,
CC ECO:0000269|PubMed:15728349, ECO:0000269|PubMed:15899885,
CC ECO:0000269|PubMed:17428919, ECO:0000269|PubMed:27068746,
CC ECO:0000269|PubMed:8898195}.
CC -!- SUBUNIT: Membrane region forms a homotetramer (PubMed:15260976).
CC Component of the SCAP-SREBP complex (composed of SCAP and SREBF1/SREBP1
CC or SREBF2/SREBP2); interacts with SREBF1/SREBP1 or SREBF2/SREBP2
CC through its C-terminal cytoplasmic domain (PubMed:9488713). Forms a
CC ternary complex with INSIG1 or INSIG2 through its transmembrane domains
CC at high sterol concentrations (PubMed:12482938, PubMed:15728349).
CC Interacts with the SEC23-SEC24 complex in a SAR1-GTP-dependent manner
CC through an ER export signal in its third cytoplasmic loop
CC (PubMed:12193656). Interacts with RNF139; the interaction inhibits the
CC interaction of SCAP with SEC24B and hampering the ER to Golgi transport
CC of the SCAP-SREBP complex (By similarity). Interacts with SPRING (By
CC similarity). {ECO:0000250|UniProtKB:Q12770,
CC ECO:0000269|PubMed:12193656, ECO:0000269|PubMed:12482938,
CC ECO:0000269|PubMed:15260976, ECO:0000269|PubMed:15728349,
CC ECO:0000269|PubMed:9488713}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10896675}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:10896675};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-
CC coated vesicle membrane {ECO:0000269|PubMed:15899885}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Moves from the endoplasmic
CC reticulum to the Golgi in the absence of sterols (PubMed:10896675).
CC Requires the presence of SPRING for proper localization to endoplasmic
CC reticulum (By similarity). {ECO:0000250|UniProtKB:Q12770,
CC ECO:0000269|PubMed:10896675}.
CC -!- DOMAIN: Loop-1 binds to loop-7, enabling interaction with COPII-coated
CC vesicles (PubMed:27068746). When levels of cholesterol in the
CC endoplasmic reticulum increase, Loop-1 binds to cholesterol instead,
CC thereby disrupting direct binding between the two loops and preventing
CC the SCAP-SREBP complex from exiting the endoplasmic reticulum
CC (PubMed:27068746). {ECO:0000269|PubMed:27068746}.
CC -!- DOMAIN: Cholesterol bound to SSD domain of SCAP or oxysterol bound to
CC INSIG (INSIG1 or INSIG2) leads to masking of an ER export signal (also
CC named MELADL motif) on SCAP possibly by moving the signal further away
CC from the ER membrane. {ECO:0000269|PubMed:17428919}.
CC -!- PTM: Ubiquitinated at Lys-454 and Lys-466. RNF145 triggers
CC ubiquitination of SCAP, likely inhibiting SCAP-SREBP complex transport
CC to the Golgi apparatus and the subsequent processing/maturation of
CC SREBF2/SREBP2. {ECO:0000250|UniProtKB:Q6GQT6}.
CC -!- DISRUPTION PHENOTYPE: CHO cells show loss of site-1 cleavage of
CC SREBF1/SREBP1 and SREBF2/SREBP2, reduced synthesis of cholesterol, a
CC reduced level of LDLR and cholesterol auxotrophy.
CC {ECO:0000269|PubMed:10497220}.
CC -!- SIMILARITY: Belongs to the WD repeat SCAP family. {ECO:0000305}.
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DR EMBL; U67060; AAB19103.1; -; mRNA.
DR EMBL; AF541996; AAQ11376.1; -; mRNA.
DR PIR; T18526; T18526.
DR RefSeq; NP_001230965.1; NM_001244036.1.
DR AlphaFoldDB; P97260; -.
DR SMR; P97260; -.
DR BioGRID; 1613731; 2.
DR CORUM; P97260; -.
DR DIP; DIP-60914N; -.
DR IntAct; P97260; 2.
DR STRING; 10029.NP_001230965.1; -.
DR TCDB; 2.A.6.6.4; the resistance-nodulation-cell division (rnd) superfamily.
DR iPTMnet; P97260; -.
DR GeneID; 100689048; -.
DR KEGG; cge:100689048; -.
DR CTD; 22937; -.
DR eggNOG; KOG1933; Eukaryota.
DR OrthoDB; 523786at2759; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0032936; C:SREBP-SCAP complex; IDA:UniProtKB.
DR GO; GO:0032937; C:SREBP-SCAP-Insig complex; IDA:UniProtKB.
DR GO; GO:0030120; C:vesicle coat; IMP:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0032934; F:sterol binding; IDA:UniProtKB.
DR GO; GO:0036315; P:cellular response to sterol; IMP:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; IDA:UniProtKB.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IMP:UniProtKB.
DR GO; GO:0032933; P:SREBP signaling pathway; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR030225; SCAP.
DR InterPro; IPR000731; SSD.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR46378; PTHR46378; 1.
DR Pfam; PF12349; Sterol-sensing; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50156; SSD; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cholesterol metabolism; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Isopeptide bond; Lipid metabolism;
KW Lipid-binding; Membrane; Methylation; Phosphoprotein; Repeat;
KW Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix;
KW Ubl conjugation; WD repeat.
FT CHAIN 1..1276
FT /note="Sterol regulatory element-binding protein cleavage-
FT activating protein"
FT /id="PRO_0000051207"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9642295"
FT TRANSMEM 19..39
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..279
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:9642295"
FT TRANSMEM 280..300
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9642295"
FT TRANSMEM 313..333
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..344
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:9642295"
FT TRANSMEM 345..365
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9642295"
FT TRANSMEM 402..422
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:9642295"
FT TRANSMEM 424..444
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9642295"
FT TRANSMEM 519..539
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..708
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:9642295"
FT TRANSMEM 709..729
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 730..1276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9642295"
FT DOMAIN 284..442
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT REPEAT 771..811
FT /note="WD 1"
FT REPEAT 949..999
FT /note="WD 2"
FT REPEAT 1002..1039
FT /note="WD 3"
FT REPEAT 1074..1111
FT /note="WD 4"
FT REPEAT 1114..1152
FT /note="WD 5"
FT REPEAT 1155..1192
FT /note="WD 6"
FT REPEAT 1194..1232
FT /note="WD 7"
FT REGION 46..284
FT /note="Loop-1"
FT /evidence="ECO:0000269|PubMed:27068746"
FT REGION 60..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..710
FT /note="Loop-7"
FT /evidence="ECO:0000269|PubMed:27068746"
FT REGION 731..1276
FT /note="Interaction with SREBF2"
FT /evidence="ECO:0000269|PubMed:9488713"
FT REGION 816..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 447..452
FT /note="ER export signal"
FT /evidence="ECO:0000269|PubMed:15899885"
FT COMPBIAS 834..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12770"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12770"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GQT6"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12770"
FT MOD_RES 905
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12770"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12770"
FT MOD_RES 1048
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6GQT6"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9642295"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9642295"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9642295"
FT CROSSLNK 454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q6GQT6"
FT CROSSLNK 466
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q6GQT6"
FT MUTAGEN 234
FT /note="Y->A: Abolished interaction between loop-1 and loop-
FT 7."
FT /evidence="ECO:0000269|PubMed:27068746"
FT MUTAGEN 298
FT /note="Y->C: Loss of sterol-dependent ER retention due to
FT loss of interaction with INSIG. Constitutive interaction
FT with COPII coat and maturation of SREBF."
FT /evidence="ECO:0000269|PubMed:10500160,
FT ECO:0000269|PubMed:12482938, ECO:0000269|PubMed:15260976,
FT ECO:0000269|PubMed:15899885"
FT MUTAGEN 315
FT /note="L->F: Loss of sterol-dependent ER retention due to
FT loss of interaction with INSIG. Constitutive maturation of
FT SREBF."
FT /evidence="ECO:0000269|PubMed:12482938"
FT MUTAGEN 428
FT /note="D->A,N,K: Loss of release from ER retention and
FT maturation of SREBF. Constitutive interaction with INSIG."
FT /evidence="ECO:0000269|PubMed:15728349"
FT MUTAGEN 428
FT /note="D->E: Very mild reduction of SREBF maturation.
FT Slightly higher affinity for INSIG in the absence of
FT sterols."
FT /evidence="ECO:0000269|PubMed:15728349"
FT MUTAGEN 437..438
FT /note="TT->AA: No effect."
FT /evidence="ECO:0000269|PubMed:17428919"
FT MUTAGEN 437..438
FT /note="Missing: Loss of SREBF maturation and interaction
FT with COPII coat."
FT /evidence="ECO:0000269|PubMed:17428919"
FT MUTAGEN 439..440
FT /note="Missing: Loss of SREBF maturation."
FT /evidence="ECO:0000269|PubMed:17428919"
FT MUTAGEN 439
FT /note="V->VLL: Loss of SREBF maturation."
FT /evidence="ECO:0000269|PubMed:17428919"
FT MUTAGEN 443
FT /note="D->N: Loss of sterol-dependent ER retention due to
FT loss of interaction with INSIG."
FT /evidence="ECO:0000269|PubMed:12482938,
FT ECO:0000269|PubMed:8898195"
FT MUTAGEN 444..445
FT /note="Missing: Loss of SREBF maturation."
FT /evidence="ECO:0000269|PubMed:17428919"
FT MUTAGEN 445..446
FT /note="RR->AA: No effect."
FT /evidence="ECO:0000269|PubMed:15899885"
FT MUTAGEN 446
FT /note="R->RA,RAAAAA,RG,RGG,RGS: Loss of SREBF maturation."
FT /evidence="ECO:0000269|PubMed:17428919"
FT MUTAGEN 446
FT /note="R->RAA: Loss of SREBF maturation and interaction
FT with COPII coat."
FT /evidence="ECO:0000269|PubMed:17428919"
FT MUTAGEN 447..448
FT /note="ME->AA: Loss of SREBF maturation and interaction
FT with COPII coat."
FT /evidence="ECO:0000269|PubMed:15899885"
FT MUTAGEN 449
FT /note="L->A: Loss of SREBF maturation and interaction with
FT COPII coat."
FT /evidence="ECO:0000269|PubMed:15899885"
FT MUTAGEN 451..452
FT /note="DL->AA: Loss of SREBF maturation, interaction with
FT COPII coat and recruitment into COPII-coated vesicles."
FT /evidence="ECO:0000269|PubMed:15899885"
FT MUTAGEN 453
FT /note="N->NAAAAA: No effect."
FT /evidence="ECO:0000269|PubMed:17428919"
FT MUTAGEN 463..492
FT /note="Missing: No effect."
FT MUTAGEN 640
FT /note="Y->S: Abolished interaction between loop-1 and loop-
FT 7."
FT /evidence="ECO:0000269|PubMed:27068746"
SQ SEQUENCE 1276 AA; 139514 MW; A8693F7157FF5FFC CRC64;
MTLTERLREK ISQAFYNHGL LCASYPIPII LFTGLCILAC CYPLLKLPLP GTGPVEFSTP
VKDYSPPPVD SDHKQGEPSE QPEWYVGAPV AYIQQIFVKS SVSPWHKNLL AVDVFRLPLS
RAFQLVEEIR NHVLRDSSGT KSLEEVCLQV TDLLPGLRKL RNLLPEHGCL LLSPGNFWQN
DWERFHADPD IIGTIHQHEP KTLQTSATLK DLLFGVPGKY SGVSLYTRKR TVSYTITLVF
QRYHAKFLSS LRARLMLLHP SPNCSLRAEN LVHVHFKEEI GIAELIPLVT TYIILFAYIY
FSTRKIDMVK SKWGLALAAV VTVLSSLLMS VGLCTLFGLT PTLNGGEIFP YLVVVIGLEN
VLVLTKSVVS TPVDLEVKLR IAQGLSSESW SIMKNVATEL GIILIGYFTL VPAIQEFCLF
AVVGLVSDFF LQMFFFTTVL SIDIRRMELA DLNKRLPPES CLPSAKPVGR PARYERQLAV
RPAMPHTITL QPSSFRNLRL PKRLRVIYFL ARTRLAQRLI MAGTVVWIGI LVYTDPAGLR
TYLAAQVTEQ SPLGEGSLGP MPVPSGVLPA SRPDPAFSIF PPDAPKLPEN QTVPGELPEH
AAPAEGVHDS RAPEVTWGPE DEELWRRLSF RHWPTLFNYY NITLAKRYIS LLPVIPVTLR
LNPQEALEGR QPQDGRSAWA PPESLPAGLW EAGPKGPGGT QAHGDITLYK VAALGLAAGI
VLVLLLLCLY RVLCPRNYGQ PGGGAGRRRR GELPCDDYGY APPETEIVPL VLRGHLMDIE
CLASDGMLLV SCCLAGQVCV WDAQTGDCLT RIPRPGSRRD SCGGGAFETQ ENWERLSDGG
KTSPEEPGES PPLRHRPRGP PQPALFGDQP DLTCLIDTNF SVQLPPEPTQ PEPRHRAGCG
RARDSGYDFS RLVQRVYQEE GLAAVRMPAL RPPSPGSPLP QASQEDGAAP EKGSPPLAWA
PSTAGSIWSL ELQGNLIVVG RSSGRLEVWD AIEGVLCCSN DEVSSGITAL VFLDRRIVAA
RLNGSLDFFS LETHTSLSPL QFRGTPGRGS SPSSSVYSSS NTVACHLTHT VPCAHQKPIT
ALRAAAGRLV TGSQDHTLRV FRLEDSCCLF TLQGHSGAIT TVYIDQTMVL ASGGQDGAIC
LWDVLTGSRV SHTFAHRGDV TSLTCTTSCV ISSGLDDLIN IWDRSTGIKL YSIQQDLGCG
ASLGVISDNL LVTGGQGCVS FWDLNYGDLL QTVYLGKNSE AQPARQILVL DNAAIVCNFG
SELSLVYVPS VLEKLD
