SE1L1_RAT
ID SE1L1_RAT Reviewed; 794 AA.
AC Q80Z70;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein sel-1 homolog 1;
DE AltName: Full=Suppressor of lin-12-like protein 1;
DE Short=Sel-1L;
DE Flags: Precursor;
GN Name=Sel1l; Synonyms=Sel1h;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Salivary gland;
RX PubMed=11401526; DOI=10.1006/bbrc.2001.4633;
RA Furue M., Zhang Y., Okamoto T., Hata R., Asashima M.;
RT "Activin A induces expression of rat Sel-1l mRNA, a negative regulator of
RT notch signaling, in rat salivary gland-derived epithelial cells.";
RL Biochem. Biophys. Res. Commun. 282:745-749(2001).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-608, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Plays a role in the endoplasmic reticulum quality control
CC (ERQC) system also called ER-associated degradation (ERAD) involved in
CC ubiquitin-dependent degradation of misfolded endoplasmic reticulum
CC proteins. Enhances SYVN1 stability. Plays a role in LPL maturation and
CC secretion. Required for normal differentiation of the pancreas
CC epithelium, and for normal exocrine function and survival of pancreatic
CC cells (By similarity). May play a role in Notch signaling
CC (PubMed:11401526). {ECO:0000250|UniProtKB:Q9Z2G6,
CC ECO:0000305|PubMed:11401526}.
CC -!- SUBUNIT: Homodimer and homooligomer (By similarity). May form a complex
CC with ERLEC1, HSPA5, OS9, and SYVN1 (By similarity). Interacts with
CC FOXRED2 and EDEM1 (By similarity). Interacts with LPL and LMF1; may
CC stabilize the complex formed by LPL and LMF1 and thereby promote the
CC export of LPL dimers (By similarity). Component of the HRD1 complex,
CC which comprises at least SYNV1/HRD1, DERL1/2, FAM8A1, HERPUD1/HERP,
CC OS9, SEL1L and UBE2J1 (By similarity). SYNV1 assembles with SEL1L and
CC FAM8A1 through its transmembrane domains, but interaction with its
CC cytoplasmic domain is required to confer stability to FAM8A1 and
CC enhance recruitment of HERPUD1 (By similarity). The interaction with
CC SYNV1/HRD1 is direct (By similarity). {ECO:0000250|UniProtKB:Q9UBV2,
CC ECO:0000250|UniProtKB:Q9Z2G6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9UBV2}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9UBV2}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9UBV2}.
CC -!- SIMILARITY: Belongs to the sel-1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO65770.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF304853; AAO65770.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q80Z70; -.
DR SMR; Q80Z70; -.
DR BioGRID; 260692; 1.
DR STRING; 10116.ENSRNOP00000043232; -.
DR GlyGen; Q80Z70; 5 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q80Z70; -.
DR PhosphoSitePlus; Q80Z70; -.
DR SwissPalm; Q80Z70; -.
DR jPOST; Q80Z70; -.
DR PaxDb; Q80Z70; -.
DR PRIDE; Q80Z70; -.
DR UCSC; RGD:620147; rat.
DR RGD; 620147; Sel1l.
DR eggNOG; KOG1550; Eukaryota.
DR InParanoid; Q80Z70; -.
DR PhylomeDB; Q80Z70; -.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-5358346; Hedgehog ligand biogenesis.
DR PRO; PR:Q80Z70; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009306; P:protein secretion; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISS:UniProtKB.
DR CDD; cd00062; FN2; 1.
DR Gene3D; 1.25.40.10; -; 3.
DR Gene3D; 2.10.10.10; -; 1.
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 Pfam; PF00040; fn2; 1.
DR Pfam; PF08238; Sel1; 12.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00671; SEL1; 11.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Notch signaling pathway; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..794
FT /note="Protein sel-1 homolog 1"
FT /id="PRO_0000022297"
FT TOPO_DOM 22..738
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 739..759
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 760..794
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 122..170
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT REPEAT 183..218
FT /note="Sel1-like 1"
FT REPEAT 219..254
FT /note="Sel1-like 2"
FT REPEAT 255..290
FT /note="Sel1-like 3"
FT REPEAT 291..326
FT /note="Sel1-like 4"
FT REPEAT 373..409
FT /note="Sel1-like 5"
FT REPEAT 410..446
FT /note="Sel1-like 6"
FT REPEAT 447..482
FT /note="Sel1-like 7"
FT REPEAT 483..518
FT /note="Sel1-like 8"
FT REPEAT 519..554
FT /note="Sel1-like 9"
FT REPEAT 627..662
FT /note="Sel1-like 10"
FT REPEAT 664..699
FT /note="Sel1-like 11"
FT REGION 22..737
FT /note="Interaction with ERLEC1, OS9 and SYVN1"
FT /evidence="ECO:0000250"
FT REGION 23..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..537
FT /note="Important for homodimerization and oligomerization"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2G6"
FT REGION 643..723
FT /note="Interaction with SYVN1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2G6"
FT REGION 738..794
FT /note="Mediates retention in the endoplasmic reticulum"
FT /evidence="ECO:0000250"
FT REGION 767..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..794
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT DISULFID 127..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 141..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 794 AA; 88683 MW; F0049AC1F8A9035E CRC64;
MQVRVRLLLL LCAVLLGSAA ASSDEETNQD ESLDSKGALP TDGSVKDHTT GKVVLLARDL
LILKDSEVES LLQDEEESSK SQEEVSVTED ISFLDSPNPS SKTYEELKRV RKPVLTAIEG
TAHGEPCHFP FLFLDKEYDE CTSDGREDGR LWCATTYDYK TDEKWGFCET EEDAAKRRQM
QEAEAIYQSG MKILNGSTRK NQKREAYRYL QKAAGMNHTK ALERVSYALL FGDYLTQNIQ
AAKEMFEKLT EEGSPKGQTG LGFLYASGLG VNSSQAKALV YYTFGALGGN LIAHMVLGYR
YWAGIGVLQS CESALTHYRL VANHVASDIS LTGGSVVQRI RLPDEVENPG MNSGMLEEDL
IQYYQFLAEK GDVQAQVGLG QLHLHGGRGV EQNHQRAFDY FNLAANAGNS HAMAFLGKMY
SEGSDIVPQS NETALHYFKK AADMGNPVGQ SGLGMAYLYG RGVQVNYDLA LKYFQKAAEQ
GWVDGQLQLG SMYYNGIGVK RDYKQALKYF NLASQGGHIL AFYNLAQMHA SGTGVMRSCH
TAVELFKNVC ERGRWSERLM TAYNSYKDDD YNAAVVQYLL LAEQGYEVAQ SNAAFILDQR
EATIVGENET YPRALLHWNR AASQGYTVAR IKLGDYHFYG FGTDVDYETA FIHYRLASEQ
QHSAQAMFNL GYMHEKGLGI KQDIHLAKRF YDMAAEASPD AQVPVFLALC KLGVVYFLQY
IREANIRDLF TQLDMDQLLG PEWDLYLMTI IALLLGTVIA YRQRQHQDIP VPRPPGPRPA
PPQQEGPPEQ QPPQ
