ID A0A3Q2XHL1_HAPBU Unreviewed; 805 AA.
AC A0A3Q2XHL1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=SEL1L adaptor subunit of ERAD E3 ubiquitin ligase {ECO:0000313|Ensembl:ENSHBUP00000034995.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000034995.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000034995.1}
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 RefSeq; XP_005917670.1; XM_005917608.1.
DR AlphaFoldDB; A0A3Q2XHL1; -.
DR STRING; 8153.ENSHBUP00000034995; -.
DR Ensembl; ENSHBUT00000030297.1; ENSHBUP00000034995.1; ENSHBUG00000022971.1.
DR GeneID; 102303294; -.
DR CTD; 6400; -.
DR GeneTree; ENSGT00940000156671; -.
DR OrthoDB; 1378605at2759; -.
DR Proteomes; UP000264840; Unplaced.
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:SF147; FIBRONECTIN TYPE-II DOMAIN-CONTAINING PROTEIN; 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; 10.
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:UP000264840};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..805
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018566438"
FT DOMAIN 114..162
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT REGION 32..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..780
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 119..145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 133..160
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 805 AA; 90234 MW; 9ED1D6BB7297FA2D CRC64;
MGYKKCLKTA RRLYFWGILF IVFSKGVTAD EEQHQDEAPE LKSYHDPDSE EEDVRLSPEI
VAGISMTTDH SHPEEETQPP SEGLEGEEKE DLPDPPPPVE EKPKEVPVVN GGTAHGEPCI
FPFLFQETEY IECTTDGRGD GRLWCATTYD YDQDKKWGFC ETEEQAQQRL QAEEAEKQYQ
TVLRMLNSTT RKTQKKELYE KLLKVAEKGH QKAMEKVAYA MLFGDYMNQN ITKAREMFEK
LAMEGSPKAQ MALGFLYAAG LGVNSSQAKA LVYYTFGALG GNLLAHMILG YRYWGGVGVP
QSCESALTHY RLVANQVASD VSLTGGSAVQ RIRLLDEVEN PGSTSGMLEE DLIQYYQFLA
EKGDVQAQVG LGQLHLHGGR GVEQNHQRAY DYFNQAANAG NTHAMAFLGK MYSEGSEFLP
QNNETALQYF KKASDLGNPV GQSGLGMAYL YGRGVPVNYE LALKYFQKAA EQGWVDGQLQ
LGTMYYNGIG VKRDYKQALK FFNLASQAGH ILAFYNLAQM HATGTGVMRS CHTAVELFKN
VCERGRWSER LMTAYGSFKE GDMDAALVQY LLLAEQGYEV AQSNVAFILD QKGARIFSEN
ETYPRALLHW TRAAAQGYTV ARIKLGDYHF YGYGTDVDYE TAVIHYRLAS EQQHSAQAMF
NLGYMHEKGL GIKQDIHLAK RFYDMAAEAS PDAQVPVFLA LCKLGLIYAL QYLQDLNLKE
LISQVDLDQL LGPEWDLYLM TVIALLLGTV IAYRQRQHQI IVPPRPPAPA PPPRPPQEQP
QGQAEPQAQE ETPEQGPAQE EEEQH
//