ID A0A068S3L2_9FUNG Unreviewed; 1441 AA.
AC A0A068S3L2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Sterol regulatory element-binding protein cleavage-activating protein {ECO:0000256|ARBA:ARBA00019541};
GN ORFNames=LCOR_07957.1 {ECO:0000313|EMBL:CDH56958.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH56958.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH56958.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000256|ARBA:ARBA00004557}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004557}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004653}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the WD repeat SCAP family.
CC {ECO:0000256|ARBA:ARBA00007410}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDH56958.1}.
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DR EMBL; CBTN010000042; CDH56958.1; -; Genomic_DNA.
DR STRING; 1263082.A0A068S3L2; -.
DR VEuPathDB; FungiDB:LCOR_07957.1; -.
DR OrthoDB; 1422944at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032934; F:sterol binding; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032933; P:SREBP signaling pathway; IEA:InterPro.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR030225; SCAP.
DR InterPro; IPR000731; SSD.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR46378; STEROL REGULATORY ELEMENT-BINDING PROTEIN CLEAVAGE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR46378:SF1; STEROL REGULATORY ELEMENT-BINDING PROTEIN CLEAVAGE-ACTIVATING PROTEIN; 1.
DR Pfam; PF12349; Sterol-sensing; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50156; SSD; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
PE 3: Inferred from homology;
KW Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT TRANSMEM 261..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 613..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 260..418
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REPEAT 1016..1038
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 680..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1441 AA; 160646 MW; EE0DDB85F36A8553 CRC64;
MAISIAKLNA SFAAFGRASA ARKYTLLFFS LTIALFLSCP TIQRLRDSLY AASITANTDN
DHFWQYSSHV HPAPFHHNAL SDSLVAYQIR LAAMTTHQQQ QQQPVTQHFL TRAQAWYRAF
TTTKVAIDDQ YYSLIDLPAS QIMLYSPFDD SYWQQQTDIP EQWETTLASI INGSTHALDP
LSVFDNVTLD KHGRFVCADS IIITALLHQD NGSRLAERVW KAVVEQHVNT LSSWKIRQLD
APVQTWQYKF KPFDYDIPLK VYLFLVVHTI IFFLVSGAFG KTQFVKSQYG LGLAAVFTSI
TCVAVTLAVL DWFGAKVDAV PWYLFPLVAN VATLENVLLL TNAVLNAGCD MQVKEKVGRG
LQSVGVPMLG TLVAELIILE IGRAMDVPTI KQFCLFAQAA LIVEYLLDMT FFIAILAIDV
NRAELADLDD RQVSKRLREL AIAGTDPDQR PPDYCPVQDD DDEGDVTMTC ADCKEFKTHR
AMNALMLCLV ILGISMFHST LEKYMVPETF MLPPAVNQRV PLPSSMILKT ERLRTMSNQF
WDTINPERQT QWIRVEPPYV ATFSMESAID NSPIWTSYEE QYLERSLSLA QKNLGKRPPS
RLRSFVLGHV QRLIVLLWHI NLPICALSIV LIGMLLWLNP SSRDQWLAPM FKKVAFKLLS
QNFMSCNIIA RRIRDHFSEQ SSSNQESVQQ QQQQQQQQQQ REHVTIKTLS GQHVADVRRF
DANAKHQLAV SCGQDDRIVM WDMEKGRATG RLEDSADSSS SSAKHIKIDQ GNKWVVGAMS
SGVVRIWSAC TSKMVRDFYI EREELASVTT SLFPSTNMMR NRRTGNAITP ITSTTSSSTI
TTTTATHSSN HSNNNSNNHH RLALGPLDRV LDVQFLGAVA EYCHPAVEQV AAKAQQGGVI
KSQNYVVSVH KSGMLREWDI LSGACMQTIP SGHTRDVSIL HVVESKRPHR KHGVSWVFTA
GKDGRVTCWE RQLVSLGGDE NDQVSQWTCA YTFVGHEGHA VTSLATELPV GGMGILVTGA
SNGTVKVWNF ETGAFVCALT TEESTKDDTA MMVTTSGNNS IVQLTVTRYC EVEYGGRGMC
RGCDTCFGNG FLIAACTTHD RVDTWRLERV GGGGNHHGSC TLCSKDYHRT QYRSSRRRRA
DSNASASSST SSTSSPAVAM RRKRRHVMRG PPKRQQQQQN QHDQGNDHDI LTGLLDIEQL
AGEGEIELTS TYLGSIDQPA GRGITFCGSN KLLAGVRRSS SSSTQSNSQW QVWFAQLQYF
DPPGEMPIDT FDLETNEEEN TMEQQQHHES RDSSLFGLFG SNSITSSQRR PSMQKARNHS
NKSLLKKMDD IQEDDEEFDE EAYELLPFSM VRHVLPLDGL GLACDFGNFI KLIYLDREQS
SKRMGGGVGA ATMEDCSKSS LQSSGTNSAV CAVPPSACSI LPNCPKASEC RAIASKKHLF
S
//
