GULP1_HUMAN
ID GULP1_HUMAN Reviewed; 304 AA.
AC Q9UBP9; B2RB51; B4DQ40; B8ZZ72; D3DPH1; E9PB86; Q53PC1; Q53RF3; Q9BVL3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=PTB domain-containing engulfment adapter protein 1;
DE AltName: Full=Cell death protein 6 homolog;
DE AltName: Full=PTB domain adapter protein CED-6;
DE AltName: Full=Protein GULP;
GN Name=GULP1; Synonyms=CED6, GULP;
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 [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=10574771; DOI=10.1016/s0960-9822(00)80061-5;
RA Liu Q.A., Hengartner M.O.;
RT "Human CED-6 encodes a functional homologue of the Caenorhabditis elegans
RT engulfment protein CED-6.";
RL Curr. Biol. 9:1347-1350(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10574763; DOI=10.1016/s0960-9822(00)80062-7;
RA Smits E., Van Criekinge W., Plaetinck G., Bogaert T.;
RT "The human homologue of Caenorhabditis elegans CED-6 specifically promotes
RT phagocytosis of apoptotic cells.";
RL Curr. Biol. 9:1351-1354(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Neuroblastoma, and Trachea;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 SUBUNIT, AND MUTAGENESIS OF LEU-176 AND LEU-183.
RX PubMed=10734103; DOI=10.1074/jbc.275.13.9542;
RA Su H.P., Brugnera E., Van Criekinge W., Smits E., Hengartner M.,
RA Bogaert T., Ravichandran K.S.;
RT "Identification and characterization of a dimerization domain in CED-6, an
RT adapter protein involved in engulfment of apoptotic cells.";
RL J. Biol. Chem. 275:9542-9549(2000).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16497666; DOI=10.1074/jbc.m600621200;
RA Kiss R.S., Ma Z., Nakada-Tsukui K., Brugnera E., Vassiliou G.,
RA McBride H.M., Ravichandran K.S., Marcel Y.L.;
RT "The lipoprotein receptor-related protein-1 (LRP) adapter protein GULP
RT mediates trafficking of the LRP ligand prosaposin, leading to sphingolipid
RT and free cholesterol accumulation in late endosomes and impaired efflux.";
RL J. Biol. Chem. 281:12081-12092(2006).
RN [9]
RP INTERACTION WITH MEGF10.
RX PubMed=17205124; DOI=10.1371/journal.pone.0000120;
RA Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V.,
RA Zhou Z., Chimini G.;
RT "Cooperation between engulfment receptors: the case of ABCA1 and MEGF10.";
RL PLoS ONE 1:E120-E120(2006).
RN [10]
RP FUNCTION, INTERACTION WITH ARF6 AND ACAP1, AND IDENTIFICATION IN A COMPLEX
RP WITH ACAP1 AND ARF6.
RX PubMed=17398097; DOI=10.1016/j.cub.2007.03.014;
RA Ma Z., Nie Z., Luo R., Casanova J.E., Ravichandran K.S.;
RT "Regulation of Arf6 and ACAP1 signaling by the PTB-domain-containing
RT adaptor protein GULP.";
RL Curr. Biol. 17:722-727(2007).
RN [11]
RP INTERACTION WITH MEGF10.
RX PubMed=17643423; DOI=10.1016/j.yexcr.2007.06.015;
RA Suzuki E., Nakayama M.;
RT "MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin
RT assembly protein complex 2 medium chain and induces large vacuole
RT formation.";
RL Exp. Cell Res. 313:3729-3742(2007).
RN [12]
RP INTERACTION WITH STAB2.
RX PubMed=18230608; DOI=10.1074/jbc.m709105200;
RA Park S.Y., Kang K.B., Thapa N., Kim S.Y., Lee S.J., Kim I.S.;
RT "Requirement of adaptor protein GULP during stabilin-2-mediated cell corpse
RT engulfment.";
RL J. Biol. Chem. 283:10593-10600(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May function as an adapter protein. Required for efficient
CC phagocytosis of apoptotic cells. Modulates cellular glycosphingolipid
CC and cholesterol transport. May play a role in the internalization and
CC endosomal trafficking of various LRP1 ligands, such as PSAP. Increases
CC cellular levels of GTP-bound ARF6. {ECO:0000269|PubMed:10574763,
CC ECO:0000269|PubMed:10574771, ECO:0000269|PubMed:16497666,
CC ECO:0000269|PubMed:17398097}.
CC -!- SUBUNIT: Homodimer. Interacts with clathrin. Interacts with GDP-bound
CC ARF6, but not with GTP-bound ARF6. Part of a complex composed of GULP1,
CC ACAP1 and ARF6. Interacts with ACAP1, LRP1, MEGF10 and STAB2.
CC {ECO:0000269|PubMed:10734103, ECO:0000269|PubMed:17205124,
CC ECO:0000269|PubMed:17398097, ECO:0000269|PubMed:17643423,
CC ECO:0000269|PubMed:18230608}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16497666}. Note=May
CC associate with the cytoplasmic side of the plasma membrane and early
CC endosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UBP9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBP9-2; Sequence=VSP_027250, VSP_027251;
CC Name=3;
CC IsoId=Q9UBP9-3; Sequence=VSP_044703;
CC Name=4;
CC IsoId=Q9UBP9-4; Sequence=VSP_045540;
CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in macrophages,
CC pancreas, kidney, skeletal muscle, heart, colon, intestine, lung,
CC placenta and ovary. {ECO:0000269|PubMed:10574763}.
CC -!- SIMILARITY: Belongs to the ced-6 family. {ECO:0000305}.
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DR EMBL; AF200715; AAF08006.1; -; mRNA.
DR EMBL; AF191771; AAF18975.1; -; mRNA.
DR EMBL; AK055718; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK298626; BAG60802.1; -; mRNA.
DR EMBL; AK314498; BAG37098.1; -; mRNA.
DR EMBL; AC092598; AAX93242.1; -; Genomic_DNA.
DR EMBL; AC125490; AAY24122.1; -; Genomic_DNA.
DR EMBL; AC104131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471058; EAX10913.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10914.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10915.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10917.1; -; Genomic_DNA.
DR EMBL; BC001103; AAH01103.1; -; mRNA.
DR CCDS; CCDS2295.1; -. [Q9UBP9-1]
DR CCDS; CCDS58742.1; -. [Q9UBP9-4]
DR CCDS; CCDS58743.1; -. [Q9UBP9-3]
DR RefSeq; NP_001239597.1; NM_001252668.1. [Q9UBP9-4]
DR RefSeq; NP_001239598.1; NM_001252669.1. [Q9UBP9-3]
DR RefSeq; NP_057399.1; NM_016315.3. [Q9UBP9-1]
DR RefSeq; XP_016859795.1; XM_017004306.1. [Q9UBP9-1]
DR PDB; 6ITU; X-ray; 2.17 A; A=1-168.
DR PDBsum; 6ITU; -.
DR AlphaFoldDB; Q9UBP9; -.
DR SMR; Q9UBP9; -.
DR BioGRID; 119550; 61.
DR ELM; Q9UBP9; -.
DR IntAct; Q9UBP9; 10.
DR MINT; Q9UBP9; -.
DR STRING; 9606.ENSP00000386289; -.
DR iPTMnet; Q9UBP9; -.
DR PhosphoSitePlus; Q9UBP9; -.
DR BioMuta; GULP1; -.
DR DMDM; 74720076; -.
DR EPD; Q9UBP9; -.
DR jPOST; Q9UBP9; -.
DR MassIVE; Q9UBP9; -.
DR MaxQB; Q9UBP9; -.
DR PaxDb; Q9UBP9; -.
DR PeptideAtlas; Q9UBP9; -.
DR PRIDE; Q9UBP9; -.
DR ProteomicsDB; 19167; -.
DR ProteomicsDB; 7320; -.
DR ProteomicsDB; 84028; -. [Q9UBP9-1]
DR ProteomicsDB; 84029; -. [Q9UBP9-2]
DR Antibodypedia; 19788; 199 antibodies from 32 providers.
DR DNASU; 51454; -.
DR Ensembl; ENST00000359135.7; ENSP00000352047.3; ENSG00000144366.16. [Q9UBP9-1]
DR Ensembl; ENST00000409580.5; ENSP00000386289.1; ENSG00000144366.16. [Q9UBP9-1]
DR Ensembl; ENST00000409609.5; ENSP00000386867.1; ENSG00000144366.16. [Q9UBP9-1]
DR Ensembl; ENST00000409637.7; ENSP00000386402.3; ENSG00000144366.16. [Q9UBP9-2]
DR Ensembl; ENST00000409805.5; ENSP00000387171.1; ENSG00000144366.16. [Q9UBP9-3]
DR Ensembl; ENST00000409830.6; ENSP00000386732.1; ENSG00000144366.16. [Q9UBP9-1]
DR Ensembl; ENST00000409843.5; ENSP00000387144.1; ENSG00000144366.16. [Q9UBP9-4]
DR Ensembl; ENST00000410051.5; ENSP00000387013.1; ENSG00000144366.16. [Q9UBP9-2]
DR GeneID; 51454; -.
DR KEGG; hsa:51454; -.
DR MANE-Select; ENST00000409830.6; ENSP00000386732.1; NM_016315.4; NP_057399.1.
DR UCSC; uc002uqc.5; human. [Q9UBP9-1]
DR CTD; 51454; -.
DR DisGeNET; 51454; -.
DR GeneCards; GULP1; -.
DR HGNC; HGNC:18649; GULP1.
DR HPA; ENSG00000144366; Tissue enhanced (epididymis).
DR MIM; 608165; gene.
DR neXtProt; NX_Q9UBP9; -.
DR OpenTargets; ENSG00000144366; -.
DR PharmGKB; PA134993283; -.
DR VEuPathDB; HostDB:ENSG00000144366; -.
DR eggNOG; KOG3536; Eukaryota.
DR GeneTree; ENSGT00940000156186; -.
DR HOGENOM; CLU_024530_0_0_1; -.
DR InParanoid; Q9UBP9; -.
DR OMA; CLDPVDS; -.
DR PhylomeDB; Q9UBP9; -.
DR TreeFam; TF314159; -.
DR PathwayCommons; Q9UBP9; -.
DR SignaLink; Q9UBP9; -.
DR BioGRID-ORCS; 51454; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; GULP1; human.
DR GenomeRNAi; 51454; -.
DR Pharos; Q9UBP9; Tbio.
DR PRO; PR:Q9UBP9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UBP9; protein.
DR Bgee; ENSG00000144366; Expressed in corpus epididymis and 203 other tissues.
DR ExpressionAtlas; Q9UBP9; baseline and differential.
DR Genevisible; Q9UBP9; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0006911; P:phagocytosis, engulfment; IDA:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Coiled coil; Cytoplasm;
KW Lipid transport; Phagocytosis; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..304
FT /note="PTB domain-containing engulfment adapter protein 1"
FT /id="PRO_0000296679"
FT DOMAIN 21..176
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 223..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 158..202
FT /evidence="ECO:0000255"
FT COMPBIAS 223..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT VAR_SEQ 31..133
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044703"
FT VAR_SEQ 134..167
FT /note="AEEITLTIGQAFDLAYRKFLESGGKDVETRKQIA -> VSIPDVVGWFVLFY
FT KPGIVLLLALAKYLKMNNFL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027250"
FT VAR_SEQ 168..304
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027251"
FT VAR_SEQ 282..304
FT /note="EGFKMGLTLEGTVFCLDPLDSRC -> RQRWRGSKWD (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045540"
FT MUTAGEN 176
FT /note="L->P: Loss of dimerization; when associated with P-
FT 183."
FT /evidence="ECO:0000269|PubMed:10734103"
FT MUTAGEN 183
FT /note="L->P: Loss of dimerization; when associated with P-
FT 176."
FT /evidence="ECO:0000269|PubMed:10734103"
FT CONFLICT 292
FT /note="G -> S (in Ref. 3; BAG60802)"
FT /evidence="ECO:0000305"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:6ITU"
FT STRAND 25..40
FT /evidence="ECO:0007829|PDB:6ITU"
FT HELIX 43..62
FT /evidence="ECO:0007829|PDB:6ITU"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:6ITU"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:6ITU"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:6ITU"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:6ITU"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6ITU"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:6ITU"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:6ITU"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6ITU"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:6ITU"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6ITU"
FT HELIX 134..154
FT /evidence="ECO:0007829|PDB:6ITU"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:6ITU"
SQ SEQUENCE 304 AA; 34490 MW; 6FCDE040073DBE8B CRC64;
MNRAFSRKKD KTWMHTPEAL SKHFIPYNAK FLGSTEVEQP KGTEVVRDAV RKLKFARHIK
KSEGQKIPKV ELQISIYGVK ILEPKTKEVQ HNCQLHRISF CADDKTDKRI FTFICKDSES
NKHLCYVFDS EKCAEEITLT IGQAFDLAYR KFLESGGKDV ETRKQIAGLQ KRIQDLETEN
MELKNKVQDL ENQLRITQVS APPAGSMTPK SPSTDIFDMI PFSPISHQSS MPTRNGTQPP
PVPSRSTEIK RDLFGAEPFD PFNCGAADFP PDIQSKLDEM QEGFKMGLTL EGTVFCLDPL
DSRC
