ID SE1L1_MESAU Reviewed; 794 AA.
AC Q9ESM7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 87.
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 Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wada M., Moriyama T.;
RT "Hamster kidney SEL1L.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
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. May play a role in Notch signaling.
CC {ECO:0000250|UniProtKB:Q9Z2G6}.
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}.
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DR EMBL; AB048195; BAB12403.1; -; mRNA.
DR RefSeq; NP_001268291.1; NM_001281362.1.
DR AlphaFoldDB; Q9ESM7; -.
DR SMR; Q9ESM7; -.
DR STRING; 10036.ENSMAUP00000015080; -.
DR GlyCosmos; Q9ESM7; 5 sites, No reported glycans.
DR GeneID; 101834260; -.
DR KEGG; maua:101834260; -.
DR CTD; 6400; -.
DR eggNOG; KOG1550; Eukaryota.
DR OrthoDB; 1378605at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; ISS:UniProtKB.
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:0006641; P:triglyceride metabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Notch signaling pathway; Phosphoprotein; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..794
FT /note="Protein sel-1 homolog 1"
FT /id="PRO_0000022295"
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 20..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 22..737
FT /note="Interaction with ERLEC1, OS9 and SYVN1"
FT /evidence="ECO:0000250"
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 768..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..83
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..794
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV2"
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:0000255"
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; 88554 MW; 610F6930114FE2CC CRC64;
MQVHVGLTLL LCAVLLSSAT ASSDDESNQD ESIDSKSSLP ADESVKDHST TGRVVAGQIF
VDSEDPEVES PLQEEEESSK TEEEVSVGEE ISFVESPSLS SKSYEEAKRA RKPVLTAIEG
TAHGEPCHFP FLFLDKEYDE CTSDGRQDGR LWCATTYDYK TDEKWGFCET EEDAAKRRQM
QEAEMIYQAG MKILNGSNRK SQKREAYRYL QKAAGMNHTK ALERVSYALL FGDYLTQNIQ
AAKEMFEKLT EEGSPKGQTA LGFLYVSGLG VNSSQAKALV YYTFGALGGN LIAHMVLGYR
YWAGIGVLQS CESVLTHYRL VANHVASDIS LTGGSVVQRI RLPDEVENPG MNSGMLEEDL
IQYYQFLAEK GDVQAQVGLG QLHLHGGRGV EQNHQRAFDY FNLAANAGNS HAMAFLGKMY
SEGSDIVPQS NETALHYFKK AADMGNPVGQ SGLGMAYLYG RGIQVNYDLA LKYFQKAAEQ
GWVDGQLQLG SMYYNGIGVK RDYKQALKYF NLASQGGHIL AFYNLAQMHA SGTGVMRSCH
TAVELFKNVC ERGRWSERLM TAYNSYKDGD YNAAVVQYLL LAEQGYEVAQ SNAAFILDQR
EATIVGENET YPRALLHWNR AASQGYTVAR IKLGDYHFYG FGTDVDYETA FIHYRLASEQ
QHSAQAMFNL GYMHEKGLGI KQDIHLAKRF YDMAAEASPD AQVPVFLALC KLGVVYFLQY
IREANIRDIF TQLDMDQLLG PEWDLYLMTI IALLLGTVIA YRQRQHQDVP VPRPPGPWPA
PPQQEGPPEQ QPPQ
//
