XAF1_HUMAN
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 03-AUG-2022, entry version 137.
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-ALPHA-INDUCED APOPTOSIS, AND NEGATIVE INTERACTION WITH
RP 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-ALPHA-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-alpha-induced apoptosis
CC and 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=3; 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=7; IntAct=EBI-2815120, EBI-723587;
CC Q6GPH4; Q96A37: RNF166; NbExp=3; 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-alpha 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="http://atlasgeneticsoncology.org/Genes/XAF1ID44095ch17p13.html";
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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_059993.2; NM_017523.3. [Q6GPH4-1]
DR RefSeq; NP_954590.1; NM_199139.2. [Q6GPH4-2]
DR RefSeq; XP_005256765.1; XM_005256708.2. [Q6GPH4-6]
DR PDB; 2LXW; NMR; -; A=251-301.
DR PDBsum; 2LXW; -.
DR AlphaFoldDB; Q6GPH4; -.
DR BMRB; Q6GPH4; -.
DR SMR; Q6GPH4; -.
DR BioGRID; 120121; 40.
DR IntAct; Q6GPH4; 16.
DR STRING; 9606.ENSP00000354822; -.
DR iPTMnet; Q6GPH4; -.
DR PhosphoSitePlus; Q6GPH4; -.
DR BioMuta; XAF1; -.
DR DMDM; 74736479; -.
DR MassIVE; Q6GPH4; -.
DR MaxQB; Q6GPH4; -.
DR PaxDb; Q6GPH4; -.
DR PeptideAtlas; Q6GPH4; -.
DR PRIDE; 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 31 providers.
DR DNASU; 54739; -.
DR Ensembl; ENST00000346752.8; ENSP00000341029.4; ENSG00000132530.17. [Q6GPH4-2]
DR Ensembl; ENST00000361842.8; ENSP00000354822.3; ENSG00000132530.17. [Q6GPH4-1]
DR Ensembl; ENST00000571673.1; ENSP00000461196.1; ENSG00000132530.17. [Q6GPH4-4]
DR Ensembl; ENST00000574962.5; ENSP00000458229.1; ENSG00000132530.17. [Q6GPH4-3]
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 CTD; 54739; -.
DR DisGeNET; 54739; -.
DR GeneCards; XAF1; -.
DR HGNC; HGNC:30932; XAF1.
DR HPA; ENSG00000132530; Low tissue specificity.
DR MIM; 606717; gene.
DR neXtProt; NX_Q6GPH4; -.
DR OpenTargets; ENSG00000132530; -.
DR PharmGKB; PA162409299; -.
DR VEuPathDB; HostDB:ENSG00000132530; -.
DR eggNOG; ENOG502QQRU; Eukaryota.
DR GeneTree; ENSGT00530000063869; -.
DR HOGENOM; CLU_066148_0_0_1; -.
DR InParanoid; Q6GPH4; -.
DR OMA; AQHREVC; -.
DR OrthoDB; 1113262at2759; -.
DR PhylomeDB; Q6GPH4; -.
DR TreeFam; TF331416; -.
DR PathwayCommons; Q6GPH4; -.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR SignaLink; Q6GPH4; -.
DR SIGNOR; Q6GPH4; -.
DR BioGRID-ORCS; 54739; 7 hits in 1073 CRISPR screens.
DR ChiTaRS; XAF1; human.
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 181 other tissues.
DR ExpressionAtlas; Q6GPH4; baseline and differential.
DR Genevisible; Q6GPH4; HS.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0035456; P:response to interferon-beta; IDA:BHF-UCL.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR031220; XAF1.
DR InterPro; IPR041386; XAF1_C.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001293; Znf_TRAF.
DR PANTHER; PTHR16295:SF17; PTHR16295:SF17; 1.
DR Pfam; PF18608; XAF1_C; 1.
DR PROSITE; PS50145; ZF_TRAF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm; Metal-binding;
KW Mitochondrion; Nucleus; Reference proteome; Tumor suppressor; Zinc;
KW 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 190..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
