ID XAF1_HUMAN Reviewed; 301 AA. AC Q6GPH4; A2T931; A2T932; A8K2L1; A8K9Y3; D3DTM6; Q6MZE8; Q8N557; Q99982; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 02-SEP-2026, entry version 155. DE RecName: Full=XIAP-associated factor 1; DE AltName: Full=BIRC4-binding protein; GN Name=XAF1; Synonyms=BIRC4BP, XIAPAF1; 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), FUNCTION, INTERACTION WITH BIRC4, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Placenta; RX PubMed=11175744; DOI=10.1038/35055027; RA Liston P., Fong W.G., Kelly N.L., Toji S., Miyazaki T., Conte D., Tamai K., RA Craig C.G., McBurney M.W., Korneluk R.G.; RT "Identification of XAF1 as an antagonist of XIAP anti-Caspase activity."; RL Nat. Cell Biol. 3:128-133(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND TISSUE SPECIFICITY. RX PubMed=17570219; DOI=10.1053/j.gastro.2007.04.024; RA Chung S.K., Lee M.G., Ryu B.K., Lee J.H., Han J., Byun D.S., Chae K.S., RA Lee K.Y., Jang J.Y., Kim H.J., Chi S.G.; RT "Frequent alteration of XAF1 in human colorectal cancers: implication for RT tumor cell resistance to apoptotic stresses."; RL Gastroenterology 132:2459-2477(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 6). RC TISSUE=Thymus; 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]. 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7). RC TISSUE=Testis; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-57. RC TISSUE=Endometrium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP FUNCTION, AND INDUCTION. RX PubMed=12029096; DOI=10.1074/jbc.m204851200; RA Leaman D.W., Chawla-Sarkar M., Vyas K., Reheman M., Tamai K., Toji S., RA Borden E.C.; RT "Identification of X-linked inhibitor of apoptosis-associated factor-1 as RT an interferon-stimulated gene that augments TRAIL Apo2L-induced RT apoptosis."; RL J. Biol. Chem. 277:28504-28511(2002). RN [8] RP ALTERNATIVE SPLICING (ISOFORM 5), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=16343440; DOI=10.1016/j.bbrc.2005.11.128; RA Yin W., Cheepala S., Clifford J.L.; RT "Identification of a novel splice variant of X-linked inhibitor of RT apoptosis-associated factor 1."; RL Biochem. Biophys. Res. Commun. 339:1148-1154(2006). RN [9] RP FUNCTION IN TNF-INDUCED APOPTOSIS, AND NEGATIVE INTERACTION WITH BIRC4. RX PubMed=16432762; DOI=10.1007/s11010-005-9094-2; RA Xia Y., Novak R., Lewis J., Duckett C.S., Phillips A.C.; RT "Xaf1 can cooperate with TNFalpha in the induction of apoptosis, RT independently of interaction with XIAP."; RL Mol. Cell. Biochem. 286:67-76(2006). RN [10] RP FUNCTION IN BIRC5 DEGRADATION, AND INTERACTION WITH BIRC1; BIRC2; BIRC3; RP BIRC4; BIRC7 AND BIRC8. RX PubMed=17613533; DOI=10.1074/jbc.m700776200; RA Arora V., Cheung H.H., Plenchette S., Micali O.C., Liston P., RA Korneluk R.G.; RT "Degradation of survivin by the X-linked inhibitor of apoptosis (XIAP)-XAF1 RT complex."; RL J. Biol. Chem. 282:26202-26209(2007). RN [11] RP FUNCTION IN TNF-INDUCED APOPTOSIS, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION. RX PubMed=17329253; DOI=10.1074/jbc.m609038200; RA Straszewski-Chavez S.L., Visintin I.P., Karassina N., Los G., Liston P., RA Halaban R., Fadiel A., Mor G.; RT "XAF1 mediates tumor necrosis factor-alpha-induced apoptosis and X-linked RT inhibitor of apoptosis cleavage by acting through the mitochondrial RT pathway."; RL J. Biol. Chem. 282:13059-13072(2007). RN [12] RP INTERACTION WITH RNF114. RX PubMed=23645206; DOI=10.1038/cdd.2013.33; RA Han J., Kim Y.L., Lee K.W., Her N.G., Ha T.K., Yoon S., Jeong S.I., RA Lee J.H., Kang M.J., Lee M.G., Ryu B.K., Baik J.H., Chi S.G.; RT "ZNF313 is a novel cell cycle activator with an E3 ligase activity RT inhibiting cellular senescence by destabilizing p21(WAF1.)."; RL Cell Death Differ. 20:1055-1067(2013). CC -!- FUNCTION: Seems to function as a negative regulator of members of the CC IAP (inhibitor of apoptosis protein) family. Inhibits anti-caspase CC activity of BIRC4. Induces cleavage and inactivation of BIRC4 CC independent of caspase activation. Mediates TNF-induced apoptosis and CC is involved in apoptosis in trophoblast cells. May inhibit BIRC4 CC indirectly by activating the mitochondrial apoptosis pathway. After CC translocation to mitochondria, promotes translocation of BAX to CC mitochondria and cytochrome c release from mitochondria. Seems to CC promote the redistribution of BIRC4 from the cytoplasm to the nucleus, CC probably independent of BIRC4 inactivation which seems to occur in the CC cytoplasm. The BIRC4-XAF1 complex mediates down-regulation of CC BIRC5/survivin; the process requires the E3 ligase activity of BIRC4. CC Seems to be involved in cellular sensitivity to the proapoptotic CC actions of TRAIL. May be a tumor suppressor by mediating apoptosis CC resistance of cancer cells. {ECO:0000269|PubMed:11175744, CC ECO:0000269|PubMed:12029096, ECO:0000269|PubMed:16432762, CC ECO:0000269|PubMed:17329253, ECO:0000269|PubMed:17613533}. CC -!- SUBUNIT: Interacts with BIRC4; the interaction is not detected in CC (PubMed:16432762). Interacts with BIRC1, BIRC2, BIRC3, BIRC7 and BIRC8. CC Part of an complex consisting of BIRC4, XAF1 and BIRC5; the complex CC formation requires IFN-beta stimulation. Interacts with RNF114, the CC interaction increases XAF1 stability and proapoptotic effects, and may CC regulate IFN signaling. {ECO:0000269|PubMed:11175744, CC ECO:0000269|PubMed:16432762, ECO:0000269|PubMed:17613533, CC ECO:0000269|PubMed:23645206}. CC -!- INTERACTION: CC Q6GPH4; P31749: AKT1; NbExp=4; IntAct=EBI-2815120, EBI-296087; CC Q6GPH4; Q96CA5: BIRC7; NbExp=3; IntAct=EBI-2815120, EBI-517623; CC Q6GPH4; Q9UI32: GLS2; NbExp=3; IntAct=EBI-2815120, EBI-3938654; CC Q6GPH4; Q6UWE0: LRSAM1; NbExp=3; IntAct=EBI-2815120, EBI-720984; CC Q6GPH4; P40937: RFC5; NbExp=3; IntAct=EBI-2815120, EBI-712376; CC Q6GPH4; Q9Y508: RNF114; NbExp=8; IntAct=EBI-2815120, EBI-723587; CC Q6GPH4; Q96A37: RNF166; NbExp=4; IntAct=EBI-2815120, EBI-2130320; CC Q6GPH4; P49903: SEPHS1; NbExp=3; IntAct=EBI-2815120, EBI-714091; CC Q6GPH4; P19474: TRIM21; NbExp=3; IntAct=EBI-2815120, EBI-81290; CC Q6GPH4; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-2815120, EBI-9867283; CC Q6GPH4; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-2815120, EBI-2130429; CC Q6GPH4; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-2815120, EBI-11059915; CC Q6GPH4; Q14CS0: UBXN2B; NbExp=3; IntAct=EBI-2815120, EBI-1993619; CC Q6GPH4; P55072: VCP; NbExp=3; IntAct=EBI-2815120, EBI-355164; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion. Note=Found in CC the cytoplasm and nucleus of placental syncytiotrophoblasts. CC Translocates to mitochondria upon TNF treatment. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=XAF1(A); CC IsoId=Q6GPH4-1; Sequence=Displayed; CC Name=2; Synonyms=XAF1B; CC IsoId=Q6GPH4-2; Sequence=VSP_032919; CC Name=3; Synonyms=D; CC IsoId=Q6GPH4-3; Sequence=VSP_032923; CC Name=4; Synonyms=E; CC IsoId=Q6GPH4-4; Sequence=VSP_032919, VSP_032923; CC Name=5; Synonyms=XAF1C; CC IsoId=Q6GPH4-5; Sequence=VSP_032922; CC Name=6; CC IsoId=Q6GPH4-6; Sequence=VSP_032918, VSP_032921; CC Name=7; CC IsoId=Q6GPH4-7; Sequence=VSP_032920; CC -!- TISSUE SPECIFICITY: Widely expressed. Expression is frequently down- CC regulated in cancer cell lines. Isoform 5 is widely expressed. CC Expressed in placenta (at protein level). {ECO:0000269|PubMed:11175744, CC ECO:0000269|PubMed:16343440, ECO:0000269|PubMed:17329253, CC ECO:0000269|PubMed:17570219}. CC -!- DEVELOPMENTAL STAGE: Selectively expressed in third trimester placenta. CC {ECO:0000269|PubMed:17329253}. CC -!- INDUCTION: Up-regulated by IFNB1/IFN-beta in cell lines sensitive to CC the proapoptotic effects of IFNB1 but not in apoptosis-resistant cells. CC Up-regulated by TNF in trophoblast cells. {ECO:0000269|PubMed:12029096, CC ECO:0000269|PubMed:17329253}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH32776.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA68030.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44095/XAF1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X99699; CAA68030.1; ALT_FRAME; mRNA. DR EMBL; EF028165; ABM74556.1; -; mRNA. DR EMBL; EF028166; ABM74557.1; -; mRNA. DR EMBL; AK290276; BAF82965.1; -; mRNA. DR EMBL; AK292710; BAF85399.1; -; mRNA. DR EMBL; AK292848; BAF85537.1; -; mRNA. DR EMBL; CH471108; EAW90288.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90289.1; -; Genomic_DNA. DR EMBL; BC032776; AAH32776.1; ALT_INIT; mRNA. DR EMBL; BC073156; AAH73156.1; -; mRNA. DR EMBL; BX649188; CAE46206.1; -; mRNA. DR CCDS; CCDS11080.1; -. [Q6GPH4-1] DR CCDS; CCDS11081.1; -. [Q6GPH4-2] DR RefSeq; NP_001340064.1; NM_001353135.1. [Q6GPH4-1] DR RefSeq; NP_059993.2; NM_017523.5. [Q6GPH4-1] DR RefSeq; NP_954590.1; NM_199139.4. [Q6GPH4-2] DR RefSeq; XP_047292274.1; XM_047436318.1. [Q6GPH4-6] DR RefSeq; XP_054172520.1; XM_054316545.1. [Q6GPH4-6] DR PDB; 2LXW; NMR; -; A=251-301. DR AlphaFoldDB; Q6GPH4; -. DR BMRB; Q6GPH4; -. DR SMR; Q6GPH4; -. DR BioGRID; 120121; 44. DR CORUM; Q6GPH4; -. DR FunCoup; Q6GPH4; 770. DR IntAct; Q6GPH4; 26. DR NDEx; IQUERY-CP-XAF1; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000354822; -. DR GlyGen; Q6GPH4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6GPH4; -. DR PhosphoSitePlus; Q6GPH4; -. DR BioMuta; XAF1; -. DR DMDM; 74736479; -. DR jPOST; Q6GPH4; -. DR MassIVE; Q6GPH4; -. DR PaxDb; 9606-ENSP00000354822; -. DR PeptideAtlas; Q6GPH4; -. DR ProteomicsDB; 66307; -. [Q6GPH4-1] DR ProteomicsDB; 66308; -. [Q6GPH4-2] DR ProteomicsDB; 66309; -. [Q6GPH4-3] DR ProteomicsDB; 66310; -. [Q6GPH4-4] DR ProteomicsDB; 66311; -. [Q6GPH4-5] DR ProteomicsDB; 66312; -. [Q6GPH4-6] DR ProteomicsDB; 66313; -. [Q6GPH4-7] DR Antibodypedia; 23838; 252 antibodies from 32 providers. DR DNASU; 54739; -. DR Ensembl; ENST00000346752.8; ENSP00000341029.4; ENSG00000132530.18. [Q6GPH4-2] DR Ensembl; ENST00000361842.8; ENSP00000354822.3; ENSG00000132530.18. [Q6GPH4-1] DR Ensembl; ENST00000571673.1; ENSP00000461196.1; ENSG00000132530.18. [Q6GPH4-4] DR Ensembl; ENST00000574962.5; ENSP00000458229.1; ENSG00000132530.18. [Q6GPH4-3] DR Ensembl; ENST00000941934.1; ENSP00000611993.1; ENSG00000132530.18. [Q6GPH4-2] DR Ensembl; ENST00000941937.1; ENSP00000611996.1; ENSG00000132530.18. [Q6GPH4-2] DR GeneID; 54739; -. DR KEGG; hsa:54739; -. DR MANE-Select; ENST00000361842.8; ENSP00000354822.3; NM_017523.5; NP_059993.2. DR UCSC; uc002gdn.4; human. [Q6GPH4-1] DR AGR; HGNC:30932; -. DR ClinPGx; PA162409299; -. DR CTD; 54739; -. DR DisGeNET; 54739; -. DR GeneCards; XAF1; -. DR HGNC; HGNC:30932; XAF1. DR HPA; ENSG00000132530; Low tissue specificity. DR MIM; 606717; gene. DR OpenTargets; ENSG00000132530; -. DR VEuPathDB; HostDB:ENSG00000132530; -. DR eggNOG; ENOG502QQRU; Eukaryota. DR GeneTree; ENSGT00530000063869; -. DR HOGENOM; CLU_066148_0_0_1; -. DR InParanoid; Q6GPH4; -. DR OMA; MDHEADE; -. DR OrthoDB; 422728at2759; -. DR PAN-GO; Q6GPH4; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q6GPH4; -. DR PathwayCommons; Q6GPH4; -. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR SignaLink; Q6GPH4; -. DR SIGNOR; Q6GPH4; -. DR Agora; ENSG00000132530; -. DR BioGRID-ORCS; 54739; 7 hits in 1151 CRISPR screens. DR ChiTaRS; XAF1; human. DR EvolutionaryTrace; Q6GPH4; -. DR GeneWiki; XAF1; -. DR GenomeRNAi; 54739; -. DR Pharos; Q6GPH4; Tbio. DR PRO; PR:Q6GPH4; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q6GPH4; protein. DR Bgee; ENSG00000132530; Expressed in apex of heart and 183 other cell types or tissues. DR ExpressionAtlas; Q6GPH4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IC:UniProt. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0140313; F:molecular sequestering activity; IDA:UniProt. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006915; P:apoptotic process; IEA:InterPro. DR GO; GO:0032480; P:negative regulation of type I interferon production; IDA:UniProt. DR GO; GO:0035456; P:response to interferon-beta; IDA:BHF-UCL. DR Gene3D; 6.10.250.1730; -; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2. DR InterPro; IPR051986; Innate_Immune_Apopt_Reg. DR InterPro; IPR049439; TRAFD1-XIAF1_Znf. DR InterPro; IPR041386; XAF1_C. DR InterPro; IPR031220; XAF1_C_sf. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR001293; Znf_TRAF. DR PANTHER; PTHR16295; TRAF-TYPE ZINC FINGER PROTEIN-RELATED; 1. DR PANTHER; PTHR16295:SF17; XIAP-ASSOCIATED FACTOR 1; 1. DR Pfam; PF21366; TRAFD1-XIAF1_ZnF; 1. DR Pfam; PF18608; XAF1_C; 1. DR Pfam; PF23580; Znf_XAF1_N; 1. DR PROSITE; PS50145; ZF_TRAF; 1. DR PDBsum; 2LXW; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm; Metal-binding; KW Mitochondrion; Nucleus; Proteomics identification; Reference proteome; KW Tumor suppressor; Zinc; Zinc-finger. FT CHAIN 1..301 FT /note="XIAP-associated factor 1" FT /id="PRO_0000329028" FT ZN_FING 22..99 FT /note="TRAF-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207" FT REGION 189..257 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 193..205 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..102 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_032918" FT VAR_SEQ 57..75 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:17570219" FT /id="VSP_032919" FT VAR_SEQ 57..74 FT /note="VGCTMCQQSMQKSSLEFH -> GKEFQLLKGKSTVIIATK (in isoform FT 7)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_032920" FT VAR_SEQ 103..140 FT /note="SYCGSRTELCQGCGQFIMHRMLAQHRDVCRSEQAQLGK -> MSLHYGCCCP FT ECTSVAIKEMMWVIRPRVACVVKDAGSA (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_032921" FT VAR_SEQ 141..301 FT /note="GERISAPEREIYCHYCNQMIPENKYFHHMGKCCPDSEFKKHFPVGNPEILPS FT SLPSQAAENQTSTMEKDVRPKTRSINRFPLHSESSSKKAPRSKNKTLDPLLMSEPKPRT FT SSPRGDKAAYDILRRCSQCGILLPLPILNQHQEKCRWLASSKGKQVRNFS -> ETSPD FT PGKCLSITVAAALSAHLWPFT (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_032922" FT VAR_SEQ 142..301 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:17570219" FT /id="VSP_032923" FT VARIANT 85 FT /note="E -> G (in dbSNP:rs34195599)" FT /id="VAR_042616" FT VARIANT 132 FT /note="R -> H (in dbSNP:rs2271232)" FT /id="VAR_042617" FT VARIANT 188 FT /note="E -> K (in dbSNP:rs34625877)" FT /id="VAR_042618" FT VARIANT 219 FT /note="R -> I (in dbSNP:rs3736433)" FT /id="VAR_042619" FT CONFLICT 132 FT /note="R -> Q (in Ref. 3; BAF85537)" FT /evidence="ECO:0000305" FT CONFLICT 138 FT /note="L -> R (in Ref. 3; BAF85537)" FT /evidence="ECO:0000305" FT CONFLICT 196 FT /note="S -> R (in Ref. 3; BAF85537)" FT /evidence="ECO:0000305" FT TURN 261..263 FT /evidence="ECO:0007829|PDB:2LXW" FT STRAND 264..266 FT /evidence="ECO:0007829|PDB:2LXW" FT TURN 268..270 FT /evidence="ECO:0007829|PDB:2LXW" FT HELIX 279..292 FT /evidence="ECO:0007829|PDB:2LXW" SQ SEQUENCE 301 AA; 34626 MW; FC9D48BD07BE541D CRC64; MEGDFSVCRN CKRHVVSANF TLHEAYCLRF LVLCPECEEP VPKETMEEHC KLEHQQVGCT MCQQSMQKSS LEFHKANECQ ERPVECKFCK LDMQLSKLEL HESYCGSRTE LCQGCGQFIM HRMLAQHRDV CRSEQAQLGK GERISAPERE IYCHYCNQMI PENKYFHHMG KCCPDSEFKK HFPVGNPEIL PSSLPSQAAE NQTSTMEKDV RPKTRSINRF PLHSESSSKK APRSKNKTLD PLLMSEPKPR TSSPRGDKAA YDILRRCSQC GILLPLPILN QHQEKCRWLA SSKGKQVRNF S //