FXL19_HUMAN
ID FXL19_HUMAN Reviewed; 694 AA.
AC Q6PCT2; A8MT10; Q8N789; Q9NT14;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=F-box/LRR-repeat protein 19;
DE AltName: Full=F-box and leucine-rich repeat protein 19;
GN Name=FBXL19; Synonyms=FBL19;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-694 (ISOFORM 2).
RC TISSUE=Duodenum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-694 (ISOFORM 3).
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] OF 545-694 (ISOFORM 1).
RC TISSUE=Testis;
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 [5]
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 [6] {ECO:0007744|PDB:6ASB}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 31-153 IN COMPLEX WITH DNA,
RP FUNCTION, DOMAIN CXXC-TYPE ZINC-FINGER, AND ZINC-BINDING.
RX PubMed=29276034; DOI=10.1016/j.str.2017.11.022;
RA Xu C., Liu K., Lei M., Yang A., Li Y., Hughes T.R., Min J.;
RT "DNA Sequence Recognition of Human CXXC Domains and Their Structural
RT Determinants.";
RL Structure 26:85-95.e3(2018).
CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box
CC protein)-type E3 ubiquitin ligase complex (By similarity). Binds to DNA
CC containing unmethylated cytidine-phosphate-guanosine (CpG)
CC dinucleotides (PubMed:29276034). {ECO:0000250,
CC ECO:0000269|PubMed:29276034}.
CC -!- SUBUNIT: Directly interacts with SKP1 and CUL1.
CC {ECO:0000250|UniProtKB:Q6P050}.
CC -!- INTERACTION:
CC Q6PCT2; P14719: Il1rl1; Xeno; NbExp=3; IntAct=EBI-6664563, EBI-525078;
CC Q6PCT2-2; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-11959077, EBI-11743294;
CC Q6PCT2-2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-11959077, EBI-11096309;
CC Q6PCT2-2; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-11959077, EBI-12831978;
CC Q6PCT2-2; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-11959077, EBI-2349927;
CC Q6PCT2-2; O43639: NCK2; NbExp=3; IntAct=EBI-11959077, EBI-713635;
CC Q6PCT2-2; P61289: PSME3; NbExp=3; IntAct=EBI-11959077, EBI-355546;
CC Q6PCT2-2; Q9NS64: RPRM; NbExp=3; IntAct=EBI-11959077, EBI-1052363;
CC Q6PCT2-2; O60504: SORBS3; NbExp=3; IntAct=EBI-11959077, EBI-741237;
CC Q6PCT2-2; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-11959077, EBI-11528917;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6PCT2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PCT2-2; Sequence=VSP_013015;
CC Name=3;
CC IsoId=Q6PCT2-3; Sequence=VSP_040503;
CC -!- DOMAIN: The CXXC zinc finger mediates binding to DNA containing
CC unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides.
CC {ECO:0000269|PubMed:29276034}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-21 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH59173.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC05410.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC135048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059173; AAH59173.1; ALT_INIT; mRNA.
DR EMBL; AK098777; BAC05410.1; ALT_INIT; mRNA.
DR EMBL; AL137589; CAB70830.1; -; mRNA.
DR CCDS; CCDS45465.1; -. [Q6PCT2-1]
DR PIR; T46301; T46301.
DR RefSeq; NP_001093254.2; NM_001099784.2. [Q6PCT2-1]
DR RefSeq; NP_001269280.1; NM_001282351.1.
DR PDB; 6ASB; X-ray; 2.85 A; C/F/I/L=31-153.
DR PDBsum; 6ASB; -.
DR AlphaFoldDB; Q6PCT2; -.
DR SMR; Q6PCT2; -.
DR BioGRID; 120078; 103.
DR IntAct; Q6PCT2; 42.
DR MINT; Q6PCT2; -.
DR STRING; 9606.ENSP00000369666; -.
DR iPTMnet; Q6PCT2; -.
DR PhosphoSitePlus; Q6PCT2; -.
DR BioMuta; FBXL19; -.
DR DMDM; 322510127; -.
DR EPD; Q6PCT2; -.
DR jPOST; Q6PCT2; -.
DR MassIVE; Q6PCT2; -.
DR MaxQB; Q6PCT2; -.
DR PaxDb; Q6PCT2; -.
DR PeptideAtlas; Q6PCT2; -.
DR PRIDE; Q6PCT2; -.
DR ProteomicsDB; 67065; -. [Q6PCT2-1]
DR ProteomicsDB; 67066; -. [Q6PCT2-2]
DR ProteomicsDB; 67067; -. [Q6PCT2-3]
DR Antibodypedia; 56437; 110 antibodies from 17 providers.
DR DNASU; 54620; -.
DR Ensembl; ENST00000562319.7; ENSP00000455529.2; ENSG00000099364.18. [Q6PCT2-1]
DR GeneID; 54620; -.
DR KEGG; hsa:54620; -.
DR UCSC; uc002eab.2; human. [Q6PCT2-1]
DR CTD; 54620; -.
DR DisGeNET; 54620; -.
DR GeneCards; FBXL19; -.
DR HGNC; HGNC:25300; FBXL19.
DR HPA; ENSG00000099364; Low tissue specificity.
DR MIM; 609085; gene.
DR neXtProt; NX_Q6PCT2; -.
DR OpenTargets; ENSG00000099364; -.
DR PharmGKB; PA134911396; -.
DR VEuPathDB; HostDB:ENSG00000099364; -.
DR eggNOG; KOG1632; Eukaryota.
DR eggNOG; KOG1633; Eukaryota.
DR eggNOG; KOG1947; Eukaryota.
DR GeneTree; ENSGT00940000161914; -.
DR InParanoid; Q6PCT2; -.
DR OMA; TEIPNCW; -.
DR OrthoDB; 324938at2759; -.
DR PhylomeDB; Q6PCT2; -.
DR TreeFam; TF338452; -.
DR PathwayCommons; Q6PCT2; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q6PCT2; -.
DR BioGRID-ORCS; 54620; 28 hits in 1091 CRISPR screens.
DR ChiTaRS; FBXL19; human.
DR GenomeRNAi; 54620; -.
DR Pharos; Q6PCT2; Tbio.
DR PRO; PR:Q6PCT2; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6PCT2; protein.
DR Bgee; ENSG00000099364; Expressed in cortical plate and 96 other tissues.
DR ExpressionAtlas; Q6PCT2; baseline and differential.
DR Genevisible; Q6PCT2; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:MGI.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045322; F:unmethylated CpG binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:MGI.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR002857; Znf_CXXC.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF16866; PHD_4; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 2.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Leucine-rich repeat;
KW Metal-binding; Reference proteome; Repeat; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..694
FT /note="F-box/LRR-repeat protein 19"
FT /id="PRO_0000119868"
FT DOMAIN 418..464
FT /note="F-box"
FT REPEAT 492..517
FT /note="LRR 1"
FT REPEAT 518..541
FT /note="LRR 2"
FT REPEAT 581..606
FT /note="LRR 3"
FT REPEAT 607..636
FT /note="LRR 4"
FT REPEAT 637..661
FT /note="LRR 5"
FT REPEAT 662..694
FT /note="LRR 6"
FT ZN_FING 32..78
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034"
FT ZN_FING 85..151
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146,
FT ECO:0000269|PubMed:29276034"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:6ASB"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:6ASB"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:6ASB"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:6ASB"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:6ASB"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:6ASB"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:6ASB"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:6ASB"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:6ASB"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:6ASB"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:6ASB"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:6ASB"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:6ASB"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:6ASB"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:6ASB"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29276034,
FT ECO:0007744|PDB:6ASB"
FT VAR_SEQ 241..283
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013015"
FT VAR_SEQ 643..694
FT /note="HCLPLFRRCPRLRRLDLRSCRQLSPEACARLAAAGPPGPFRCPEEKLLLKDS
FT -> PAGLGPWAPGLYNTVCYKTQNLP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040503"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:6ASB"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:6ASB"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6ASB"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:6ASB"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6ASB"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:6ASB"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6ASB"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6ASB"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6ASB"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6ASB"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6ASB"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:6ASB"
SQ SEQUENCE 694 AA; 75707 MW; 8D8A3BC4C86AD396 CRC64;
MGMKVPGKGE SGPSALLTPP MSSSSRGPGA GARRRRTRCR RCRACVRTEC GDCHFCRDMK
KFGGPGRMKQ SCLLRQCTAP VLPHTAVCLL CGEAGKEDTV EGEEEKFGLS LMECTICNEI
VHPGCLKMGK AEGVINAEIP NCWECPRCTQ EGRTSKDSGE GPGRRRADNG EEGASLGSGW
KLTEEPPLPP PPPRRKGPLP AGPPPEDVPG PPKRKEREAG NEPPTPRKKV KGGRERHLKK
VGGDACLLRG SDPGGPGLLP PRVLNPSQAF SSCHPGLPPE NWEKPKPPLA SAEGPAVPSP
SPQREKLERF KRMCQLLERV PDTSSSSSDS DSDSDSSGTS LSEDEAPGEA RNGRRPARGS
SGEKENRGGR RAVRPGSGGP LLSWPLGPAP PPRPPQLERH VVRPPPRSPE PDTLPLAAGS
DHPLPRAAWL RVFQHLGPRE LCICMRVCRT WSRWCYDKRL WPRMDLSRRK SLTPPMLSGV
VRRQPRALDL SWTGVSKKQL MWLLNRLQGL QELVLSGCSW LSVSALGSAP LPALRLLDLR
WIEDVKDSQL RELLLPPPDT KPGQTESRGR LQGVAELRLA GLELTDASLR LLLRHAPQLS
ALDLSHCAHV GDPSVHLLTA PTSPLRETLV HLNLAGCHRL TDHCLPLFRR CPRLRRLDLR
SCRQLSPEAC ARLAAAGPPG PFRCPEEKLL LKDS
