ID G1PGS4_MYOLU Unreviewed; 835 AA.
AC G1PGS4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=SEL1L adaptor subunit of ERAD E3 ubiquitin ligase {ECO:0000313|Ensembl:ENSMLUP00000009849.2};
GN Name=SEL1L {ECO:0000313|Ensembl:ENSMLUP00000009849.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000009849.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000009849.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000009849.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the sel-1 family.
CC {ECO:0000256|ARBA:ARBA00038101}.
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DR EMBL; AAPE02014226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PGS4; -.
DR STRING; 59463.ENSMLUP00000009849; -.
DR Ensembl; ENSMLUT00000010805.2; ENSMLUP00000009849.2; ENSMLUG00000010767.2.
DR eggNOG; KOG1550; Eukaryota.
DR GeneTree; ENSGT00940000156671; -.
DR HOGENOM; CLU_007931_2_1_1; -.
DR InParanoid; G1PGS4; -.
DR OMA; DMLAKPR; -.
DR TreeFam; TF315257; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IEA:Ensembl.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IEA:Ensembl.
DR GO; GO:0009306; P:protein secretion; IEA:Ensembl.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR CDD; cd00062; FN2; 1.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11102:SF70; PROTEIN SEL-1 HOMOLOG 1; 1.
DR PANTHER; PTHR11102; SEL-1-LIKE PROTEIN; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF08238; Sel1; 11.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00671; SEL1; 11.
DR SUPFAM; SSF81901; HCP-like; 3.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479}; Reference proteome {ECO:0000313|Proteomes:UP000001074}.
FT DOMAIN 163..211
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..835
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 168..194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 182..209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 835 AA; 92413 MW; 0415407E327D6833 CRC64;
GRGGGRDASR KSSGEAAAAA ESVVPEAKAT APGGGGSPES RMRVRVGLTL LLCAVLLGTA
SASSDDESSQ DESLDSKTSL PSDEPVKDHS TAGRVVAGQI FLDSEESELE SPIQEEEDSL
RSQEGESGTE EISFLESSNP ENKDYEEPTK VRKPALTAIE GTAHGEPCHF PFLFLDKEYD
ECTSDGREDG RLWCATTYDY KADEKWGFCE TEEEATKRRQ MQEAEVMYQT GMKILNGSNK
KSQKREAYRY LQKAASMNHT KALERVSYAL LFGDYLTQNL QTAKEMFEKL TEEGSPKGQT
ALGFLYASGL GVNSSQAKAL VYYTFGALGG NLIAHMILGY RYWAGIGVLQ SCESALTHYR
LVANHVASDI SLTGGSVVQR IRLPDEVENP GMNSGMLEED LIQYYQFLAE KGDVQAQVGL
GQLHLHGGRG VEQNHQRAFD YFNLAANAGN SHAMAFLGKM YSEGSDIVPQ SNETALHYFK
KAADMGNPVG QSGLGMAYLY GRGVQVNYDL ALKYFQKAAE QGWVDGQLQL GSMYYNGIGV
KRDYKQALKY FNLASQGGHI LAFYNLAQMH ASGTGVMRSC HNAVELFKNV CERGRWSERL
MTAYNSYKDG DYNAAVIQYL LLAEQGYEVA QSNAAFILDQ REATIVGENE TYPRALLHWN
RAASQGYTVA RIKLGDYHFY GFGTDVDYET AFIHYRLASE QQHSAQAMFN LGYMHEKGLG
IKQDIHLAKR FYDMAAEASP DAQVPVFLAL CKLGVVYFLQ YIREANIRDV FTQVDMDQLL
GPEWDLYLMT IIALLLGTVI AYRQRQHQDM PGPRPPGPRP APPQQEAPPE QQPPQ
//
