LOCUS       NP_808794                793 aa            linear   ROD 03-APR-2024
DEFINITION  protein sel-1 homolog 1 precursor [Rattus norvegicus].
ACCESSION   NP_808794
VERSION     NP_808794.2
DBSOURCE    REFSEQ: accession NM_177933.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Hosokawa,N. and Wada,I.
  TITLE     Association of the SEL1L protein transmembrane domain with HRD1
            ubiquitin ligase regulates ERAD-L
  JOURNAL   FEBS J 283 (1), 157-172 (2016)
   PUBMED   26471130
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Zhong,Y., Shen,H., Wang,Y., Yang,Y., Yang,P. and Fang,S.
  TITLE     Identification of ERAD components essential for dislocation of the
            null Hong Kong variant of alpha-1-antitrypsin (NHK)
  JOURNAL   Biochem Biophys Res Commun 458 (2), 424-428 (2015)
   PUBMED   25660456
REFERENCE   3  (residues 1 to 793)
  AUTHORS   Sha,H., Sun,S., Francisco,A.B., Ehrhardt,N., Xue,Z., Liu,L.,
            Lawrence,P., Mattijssen,F., Guber,R.D., Panhwar,M.S., Brenna,J.T.,
            Shi,H., Xue,B., Kersten,S., Bensadoun,A., Peterfy,M., Long,Q. and
            Qi,L.
  TITLE     The ER-associated degradation adaptor protein Sel1L regulates LPL
            secretion and lipid metabolism
  JOURNAL   Cell Metab 20 (3), 458-470 (2014)
   PUBMED   25066055
REFERENCE   4  (residues 1 to 793)
  AUTHORS   Iida,Y., Fujimori,T., Okawa,K., Nagata,K., Wada,I. and Hosokawa,N.
  TITLE     SEL1L protein critically determines the stability of the HRD1-SEL1L
            endoplasmic reticulum-associated degradation (ERAD) complex to
            optimize the degradation kinetics of ERAD substrates
  JOURNAL   J Biol Chem 286 (19), 16929-16939 (2011)
   PUBMED   21454652
REFERENCE   5  (residues 1 to 793)
  AUTHORS   Francisco,A.B., Singh,R., Li,S., Vani,A.K., Yang,L., Munroe,R.J.,
            Diaferia,G., Cardano,M., Biunno,I., Qi,L., Schimenti,J.C. and
            Long,Q.
  TITLE     Deficiency of suppressor enhancer Lin12 1 like (SEL1L) in mice
            leads to systemic endoplasmic reticulum stress and embryonic
            lethality
  JOURNAL   J Biol Chem 285 (18), 13694-13703 (2010)
   PUBMED   20197277
REFERENCE   6  (residues 1 to 793)
  AUTHORS   Cattaneo,M., Orlandini,S., Beghelli,S., Moore,P.S., Sorio,C.,
            Bonora,A., Bassi,C., Talamini,G., Zamboni,G., Orlandi,R.,
            Menard,S., Bernardi,L.R., Biunno,I. and Scarpa,A.
  TITLE     SEL1L expression in pancreatic adenocarcinoma parallels SMAD4
            expression and delays tumor growth in vitro and in vivo
  JOURNAL   Oncogene 22 (41), 6359-6368 (2003)
   PUBMED   14508516
REFERENCE   7  (residues 1 to 793)
  AUTHORS   Furue,M., Zhang,Y., Okamoto,T., Hata,R.I. and Asashima,M.
  TITLE     Activin A induces expression of rat Sel-1l mRNA, a negative
            regulator of notch signaling, in rat salivary gland-derived
            epithelial cells
  JOURNAL   Biochem Biophys Res Commun 282 (3), 745-749 (2001)
   PUBMED   11401526
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Oct 17, 2007 this sequence version replaced NP_808794.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.23500.1, AF304853.2
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q31"
     Protein         1..793
                     /product="protein sel-1 homolog 1 precursor"
                     /note="protein sel-1 homolog 1; sel-1L; suppressor of
                     lin-12-like protein 1; Sel1 (suppressor of lin-12) 1
                     homolog; SEL1L adaptor subunit of ERAD E3 ubiquitin
                     ligase; sel-1 suppressor of lin-12-like; SEL1L ERAD E3
                     ligase adaptor subunit"
                     /calculated_mol_wt=86331
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2211
     Region          23..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80Z70.2)"
     Region          72..104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80Z70.2)"
     Region          119..167
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(130,132,137,151,158,164,166)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Site            194
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80Z70.2)"
     Region          204..230
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Site            216
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80Z70.2)"
     Region          237..266
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          254..289
                     /region_name="SEL1"
                     /note="Sel1-like repeats; smart00671"
                     /db_xref="CDD:214772"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80Z70.2)"
     Region          273..302
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          351..536
                     /region_name="Important for homodimerization and
                     oligomerization. /evidence=ECO:0000250|UniProtKB:Q9Z2G6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80Z70.2)"
     Region          <362..551
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          392..421
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          429..458
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Site            430
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80Z70.2)"
     Region          465..494
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          569..598
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          605..638
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Site            607
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q80Z70.2)"
     Region          628..661
                     /region_name="SEL1"
                     /note="Sel1-like repeats; smart00671"
                     /db_xref="CDD:214772"
     Region          642..722
                     /region_name="Interaction with SYVN1.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2G6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80Z70.2)"
     Region          645..675
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          663..696
                     /region_name="Sel1"
                     /note="Sel1 repeat; pfam08238"
                     /db_xref="CDD:429881"
     Region          737..793
                     /region_name="Mediates retention in the endoplasmic
                     reticulum. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80Z70.2)"
     Site            738..758
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80Z70.2)"
     Region          766..793
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80Z70.2)"
     CDS             1..793
                     /gene="Sel1l"
                     /gene_synonym="Sel1h"
                     /coded_by="NM_177933.5:93..2474"
                     /db_xref="GeneID:314352"
                     /db_xref="RGD:620147"
ORIGIN      
        1 mqvrvrllll lcavllgsaa assdeetnqd esldskgalp tdgsvkdhtt gkvvagqrfv
       61 dsedsevesl lqdeeessks qeevsvtedi sfldspnpss ktyeelkrvr kpvltaiegt
      121 ahgepchfpf lfldkeydec tsdgredgrl wcattydykt dekwgfcete edaakrrqmq
      181 eaeaiyqsgm kilngstrkn qkreayrylq kaagmnhtka lervsyallf gdyltqniqa
      241 akemfeklte egspkgqtgl gflyasglgv nssqakalvy ytfgalggnl iahmvlgyry
      301 wagigvlqsc esalthyrlv anhvasdisl tggsvvqrir lpdevenpgm nsgmleedli
      361 qyyqflaekg dvqaqvglgq lhlhggrgve qnhqrafdyf nlaanagnsh amaflgkmys
      421 egsdivpqsn etalhyfkka admgnpvgqs glgmaylygr gvqvnydlal kyfqkaaeqg
      481 wvdgqlqlgs myyngigvkr dykqalkyfn lasqgghila fynlaqmhas gtgvmrscht
      541 avelfknvce rgrwserlmt aynsykdddy naavvqylll aeqgyevaqs naafildqre
      601 ativgenety prallhwnra asqgytvari klgdyhfygf gtdvdyetaf ihyrlaseqq
      661 hsaqamfnlg ymhekglgik qdihlakrfy dmaaeaspda qvpvflalck lgvvyflqyi
      721 reanirdlft qldmdqllgp ewdlylmtii alllgtviay rqrqhqdipv prppgprpap
      781 pqqegppeqq ppq
//
