DERL3_HUMAN
ID DERL3_HUMAN Reviewed; 235 AA.
AC Q96Q80; F2Z3B6; Q6ICJ6; Q6PEX0; Q6ZUB5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Derlin-3 {ECO:0000303|PubMed:15215855};
DE AltName: Full=Degradation in endoplasmic reticulum protein 3;
DE Short=DERtrin-3;
DE AltName: Full=Der1-like protein 3 {ECO:0000303|PubMed:15215855};
GN Name=DERL3 {ECO:0000312|HGNC:HGNC:14236};
GN Synonyms=C22orf14 {ECO:0000312|HGNC:HGNC:14236}, DER3,
GN LLN2 {ECO:0000312|EMBL:BAB68409.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 3).
RA Shimizu N., Minosima S., Kawasaki K., Sasaki T.;
RT "Molecular cloning of a novel member of the NADH oxidoreductase complex I
RT subunit homolog.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT LEU-149.
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT VAL-211.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION.
RX PubMed=15215855; DOI=10.1038/nature02592;
RA Lilley B.N., Ploegh H.L.;
RT "A membrane protein required for dislocation of misfolded proteins from the
RT ER.";
RL Nature 429:834-840(2004).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY,
RP OLIGOMERIZATION, INTERACTION WITH VCP AND EDEM1, AND INDUCTION.
RX PubMed=16449189; DOI=10.1083/jcb.200507057;
RA Oda Y., Okada T., Yoshida H., Kaufman R.J., Nagata K., Mori K.;
RT "Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein
RT response and are required for ER-associated degradation.";
RL J. Cell Biol. 172:383-393(2006).
RN [9]
RP INTERACTION WITH SELENOK AND SELENOS.
RX PubMed=22016385; DOI=10.1074/jbc.m111.310920;
RA Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L.,
RA Gladyshev V.N.;
RT "Selenoprotein K binds multiprotein complexes and is involved in the
RT regulation of endoplasmic reticulum homeostasis.";
RL J. Biol. Chem. 286:42937-42948(2011).
RN [10]
RP FUNCTION IN ERAD PATHWAY.
RX PubMed=22607976; DOI=10.1016/j.molcel.2012.04.015;
RA Sato T., Sako Y., Sho M., Momohara M., Suico M.A., Shuto T., Nishitoh H.,
RA Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M., Chosa K., Koga T.,
RA Morino-Koga S., Wada I., Kai H.;
RT "STT3B-dependent posttranslational N-glycosylation as a surveillance system
RT for secretory protein.";
RL Mol. Cell 47:99-110(2012).
RN [11]
RP FUNCTION, AND SUBUNIT.
RX PubMed=26565908; DOI=10.1016/j.celrep.2015.09.047;
RA Kadowaki H., Nagai A., Maruyama T., Takami Y., Satrimafitrah P., Kato H.,
RA Honda A., Hatta T., Natsume T., Sato T., Kai H., Ichijo H., Nishitoh H.;
RT "Pre-emptive quality control protects the ER from protein overload via the
RT proximity of ERAD components and SRP.";
RL Cell Rep. 13:944-956(2015).
CC -!- FUNCTION: Functional component of endoplasmic reticulum-associated
CC degradation (ERAD) for misfolded lumenal glycoproteins, but not that of
CC misfolded nonglycoproteins. May act by forming a channel that allows
CC the retrotranslocation of misfolded glycoproteins into the cytosol
CC where they are ubiquitinated and degraded by the proteasome. May
CC mediate the interaction between VCP and the misfolded glycoproteins
CC (PubMed:16449189, PubMed:22607976). May be involved in endoplasmic
CC reticulum stress-induced pre-emptive quality control, a mechanism that
CC selectively attenuates the translocation of newly synthesized proteins
CC into the endoplasmic reticulum and reroutes them to the cytosol for
CC proteasomal degradation (PubMed:26565908).
CC {ECO:0000269|PubMed:16449189, ECO:0000269|PubMed:22607976,
CC ECO:0000269|PubMed:26565908}.
CC -!- SUBUNIT: Forms homo- and heterooligomers with DERL2 and, to a lesser
CC extent, with DERL1 (PubMed:16449189). Interacts with VCP and EDEM1
CC (PubMed:16449189). Interacts with SELENOK and SELENOS
CC (PubMed:22016385). Interacts with the signal recognition particle/SRP
CC and the SRP receptor; in the process of endoplasmic reticulum stress-
CC induced pre-emptive quality control (PubMed:26565908).
CC {ECO:0000269|PubMed:16449189, ECO:0000269|PubMed:22016385,
CC ECO:0000269|PubMed:26565908}.
CC -!- INTERACTION:
CC Q96Q80; Q08426: EHHADH; NbExp=3; IntAct=EBI-12831318, EBI-2339219;
CC Q96Q80; Q05329: GAD2; NbExp=3; IntAct=EBI-12831318, EBI-9304251;
CC Q96Q80; P22749: GNLY; NbExp=3; IntAct=EBI-12831318, EBI-17844792;
CC Q96Q80; Q96P66: GPR101; NbExp=3; IntAct=EBI-12831318, EBI-17935713;
CC Q96Q80; Q6UWB1: IL27RA; NbExp=3; IntAct=EBI-12831318, EBI-19045531;
CC Q96Q80; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-12831318, EBI-11978907;
CC Q96Q80; Q96DX8: RTP4; NbExp=3; IntAct=EBI-12831318, EBI-12275482;
CC Q96Q80; O00560: SDCBP; NbExp=3; IntAct=EBI-12831318, EBI-727004;
CC Q96Q80; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-12831318, EBI-12808018;
CC Q96Q80; P02808: STATH; NbExp=3; IntAct=EBI-12831318, EBI-738687;
CC Q96Q80; Q17RD7: SYT16; NbExp=3; IntAct=EBI-12831318, EBI-10238936;
CC Q96Q80; Q8N6K0: TEX29; NbExp=3; IntAct=EBI-12831318, EBI-19027521;
CC Q96Q80; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-12831318, EBI-11724423;
CC Q96Q80; Q6UXU6: TMEM92; NbExp=3; IntAct=EBI-12831318, EBI-10975829;
CC Q96Q80; Q9BZM5: ULBP2; NbExp=3; IntAct=EBI-12831318, EBI-3919993;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16449189}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16449189}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96Q80-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96Q80-2; Sequence=VSP_011088;
CC Name=3;
CC IsoId=Q96Q80-3; Sequence=VSP_011089;
CC Name=4;
CC IsoId=Q96Q80-4; Sequence=VSP_011086, VSP_011087;
CC Name=5;
CC IsoId=Q96Q80-5; Sequence=VSP_046330;
CC -!- TISSUE SPECIFICITY: Unlike DERL1 and DERL2, restricted to several
CC tissues. Expressed at high levels in placenta, pancreas, spleen and
CC small intestine. {ECO:0000269|PubMed:16449189}.
CC -!- INDUCTION: Up-regulated in response to endoplasmic reticulum stress via
CC the ERN1-XBP1 pathway of the unfolded protein response (UPR).
CC {ECO:0000269|PubMed:16449189}.
CC -!- SIMILARITY: Belongs to the derlin family. {ECO:0000305}.
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DR EMBL; AB049213; BAB68409.1; -; Genomic_DNA.
DR EMBL; AL389876; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK125830; BAC86311.1; -; mRNA.
DR EMBL; CR456372; CAG30258.1; -; mRNA.
DR EMBL; AP000350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057830; AAH57830.1; -; mRNA.
DR CCDS; CCDS33615.1; -. [Q96Q80-1]
DR CCDS; CCDS42986.1; -. [Q96Q80-5]
DR CCDS; CCDS46672.1; -. [Q96Q80-2]
DR RefSeq; NP_001002862.1; NM_001002862.2. [Q96Q80-1]
DR RefSeq; NP_001129223.1; NM_001135751.1. [Q96Q80-2]
DR RefSeq; NP_940842.2; NM_198440.3. [Q96Q80-5]
DR RefSeq; XP_011528808.1; XM_011530506.2.
DR AlphaFoldDB; Q96Q80; -.
DR SMR; Q96Q80; -.
DR BioGRID; 124816; 27.
DR IntAct; Q96Q80; 17.
DR STRING; 9606.ENSP00000384744; -.
DR TCDB; 3.A.16.1.4; the endoplasmic reticular retrotranslocon (er-rt) family.
DR BioMuta; DERL3; -.
DR DMDM; 50400613; -.
DR jPOST; Q96Q80; -.
DR MassIVE; Q96Q80; -.
DR MaxQB; Q96Q80; -.
DR PeptideAtlas; Q96Q80; -.
DR PRIDE; Q96Q80; -.
DR ProteomicsDB; 23934; -.
DR ProteomicsDB; 77832; -. [Q96Q80-1]
DR ProteomicsDB; 77833; -. [Q96Q80-2]
DR ProteomicsDB; 77834; -. [Q96Q80-3]
DR ProteomicsDB; 77835; -. [Q96Q80-4]
DR Antibodypedia; 23832; 74 antibodies from 21 providers.
DR DNASU; 91319; -.
DR Ensembl; ENST00000318109.12; ENSP00000315303.8; ENSG00000099958.15. [Q96Q80-1]
DR Ensembl; ENST00000406855.7; ENSP00000384744.3; ENSG00000099958.15. [Q96Q80-2]
DR Ensembl; ENST00000476077.1; ENSP00000419399.1; ENSG00000099958.15. [Q96Q80-5]
DR Ensembl; ENST00000620697.3; ENSP00000483693.2; ENSG00000274437.4. [Q96Q80-2]
DR Ensembl; ENST00000628868.1; ENSP00000485763.1; ENSG00000274437.4. [Q96Q80-5]
DR Ensembl; ENST00000631305.2; ENSP00000486587.1; ENSG00000274437.4. [Q96Q80-1]
DR GeneID; 91319; -.
DR KEGG; hsa:91319; -.
DR MANE-Select; ENST00000318109.12; ENSP00000315303.8; NM_001002862.3; NP_001002862.1.
DR UCSC; uc002zyh.4; human. [Q96Q80-1]
DR CTD; 91319; -.
DR DisGeNET; 91319; -.
DR GeneCards; DERL3; -.
DR HGNC; HGNC:14236; DERL3.
DR HPA; ENSG00000099958; Tissue enhanced (lymphoid tissue, pancreas, salivary gland).
DR MIM; 610305; gene.
DR neXtProt; NX_Q96Q80; -.
DR OpenTargets; ENSG00000099958; -.
DR PharmGKB; PA25883; -.
DR VEuPathDB; HostDB:ENSG00000099958; -.
DR eggNOG; KOG0858; Eukaryota.
DR GeneTree; ENSGT00530000063156; -.
DR HOGENOM; CLU_051898_5_2_1; -.
DR InParanoid; Q96Q80; -.
DR OMA; WSKRNPL; -.
DR OrthoDB; 1609512at2759; -.
DR PhylomeDB; Q96Q80; -.
DR TreeFam; TF314715; -.
DR PathwayCommons; Q96Q80; -.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR SignaLink; Q96Q80; -.
DR BioGRID-ORCS; 91319; 5 hits in 1074 CRISPR screens.
DR GeneWiki; Derlin-3; -.
DR GenomeRNAi; 91319; -.
DR Pharos; Q96Q80; Tbio.
DR PRO; PR:Q96Q80; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q96Q80; protein.
DR Bgee; ENSG00000099958; Expressed in bone marrow cell and 96 other tissues.
DR ExpressionAtlas; Q96Q80; baseline and differential.
DR Genevisible; Q96Q80; HS.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0005047; F:signal recognition particle binding; IDA:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:UniProtKB.
DR GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
DR InterPro; IPR007599; DER1.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR Pfam; PF04511; DER1; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..235
FT /note="Derlin-3"
FT /id="PRO_0000219048"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..58
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..157
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 216..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011086"
FT VAR_SEQ 110..205
FT /note="LLGLLGSLFFLGQALMAMLVYVWSRRSPRVRVNFFGLLTFQAPFLPWALMGF
FT SLLLGNSILVDLLGIAVGHIYYFLEDVFPNQPGGKRLLQTPGFL -> VSFPQALEPRA
FT RAPRRPACVGPGANTAMPERDTVAVSSLVCVEGPLCAQLQGSGLDLQCCMQNTKPRTKE
FT PGTVPALGAHGLLAAAGQLHPRGPAGDCGGPYLLLPGGRLPQPAWRQEAPADPWLPVSV
FT ESPPSLSPPSEGSPPMGTCAGLCSTRAPPHR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011087"
FT VAR_SEQ 206..235
FT /note="KLLLDAPAEDPNYLPLPEEQPGPHLPPPQQ -> GLQSSKAPAGSSLTIWTQ
FT QSQGGPGTAGELAAPS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15461802"
FT /id="VSP_011088"
FT VAR_SEQ 206..235
FT /note="KLLLDAPAEDPNYLPLPEEQPGPHLPPPQQ -> LATAQQCPHRTGPSAGDF
FT RAARPQLAVA (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_011089"
FT VAR_SEQ 206..235
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_046330"
FT VARIANT 149
FT /note="F -> L (in dbSNP:rs3177243)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_048897"
FT VARIANT 211
FT /note="A -> V (in dbSNP:rs1128127)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_019517"
SQ SEQUENCE 235 AA; 26679 MW; 2DC5F02487C4B824 CRC64;
MAWQGLAAEF LQVPAVTRAY TAACVLTTAA VQLELLSPFQ LYFNPHLVFR KFQVWRLVTN
FLFFGPLGFS FFFNMLFVFR YCRMLEEGSF RGRTADFVFM FLFGGVLMTL LGLLGSLFFL
GQALMAMLVY VWSRRSPRVR VNFFGLLTFQ APFLPWALMG FSLLLGNSIL VDLLGIAVGH
IYYFLEDVFP NQPGGKRLLQ TPGFLKLLLD APAEDPNYLP LPEEQPGPHL PPPQQ
