ID FBLN4_HUMAN Reviewed; 443 AA. AC O95967; A8K7R4; B3KM31; B3KQT1; O75967; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 3. DT 13-FEB-2019, entry version 194. DE RecName: Full=EGF-containing fibulin-like extracellular matrix protein 2; DE AltName: Full=Fibulin-4; DE Short=FIBL-4; DE AltName: Full=Protein UPH1; DE Flags: Precursor; GN Name=EFEMP2; Synonyms=FBLN4; ORFNames=UNQ200/PRO226; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-259. RC TISSUE=Melanoma; RX PubMed=10601734; DOI=10.1016/S0945-053X(99)00038-4; RA Giltay R., Timpl R., Kostka G.; RT "Sequence, recombinant expression and tissue localization of two novel RT extracellular matrix proteins, fibulin-3 and fibulin-4."; RL Matrix Biol. 18:469-480(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-259. RA Zemel R., Shaul Y.; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-259. RX PubMed=10982184; DOI=10.1007/s004390051011; RA Katsanis N., Venable S., Smith J.R., Lupski J.R.; RT "Isolation of a paralog of the Doyne honeycomb retinal dystrophy gene RT from the multiple retinopathy critical region on 11q13."; RL Hum. Genet. 106:66-72(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-259. RC TISSUE=Embryo, and Synovium; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-259. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-259. RC TISSUE=Placenta; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full- RT length human cDNAs encoding secretion or membrane proteins from oligo- RT capped cDNA libraries."; RL DNA Res. 12:117-126(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-259. RC TISSUE=Brain; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP INTERACTION WITH FBN1. RX PubMed=17255108; DOI=10.1074/jbc.M608204200; RA El-Hallous E., Sasaki T., Hubmacher D., Getie M., Tiedemann K., RA Brinckmann J., Baetge B., Davis E.C., Reinhardt D.P.; RT "Fibrillin-1 interactions with fibulins depend on the first hybrid RT domain and provide an adaptor function to tropoelastin."; RL J. Biol. Chem. 282:8935-8946(2007). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP STRUCTURE BY NMR OF 54-123, AND DISULFIDE BONDS. RG Northeast structural genomics consortium (NESG); RT "Solution NMR structure of the EGF-like 1 domain of human fibulin-4."; RL Submitted (JUL-2009) to the PDB data bank. RN [12] RP VARIANT ARCL1B LYS-57. RX PubMed=16685658; DOI=10.1086/504304; RA Hucthagowder V., Sausgruber N., Kim K.H., Angle B., Marmorstein L.Y., RA Urban Z.; RT "Fibulin-4: a novel gene for an autosomal recessive cutis laxa RT syndrome."; RL Am. J. Hum. Genet. 78:1075-1080(2006). RN [13] RP VARIANT ARCL1B CYS-279. RX PubMed=17937443; DOI=10.1002/ajmg.a.31980; RA Dasouki M., Markova D., Garola R., Sasaki T., Charbonneau N.L., RA Sakai L.Y., Chu M.L.; RT "Compound heterozygous mutations in fibulin-4 causing neonatal lethal RT pulmonary artery occlusion, aortic aneurysm, arachnodactyly, and mild RT cutis laxa."; RL Am. J. Med. Genet. A 143:2635-2641(2007). RN [14] RP VARIANT ARCL1B TYR-267. RX PubMed=19664000; DOI=10.1111/j.1399-0004.2009.01204.x; RA Hoyer J., Kraus C., Hammersen G., Geppert J.P., Rauch A.; RT "Lethal cutis laxa with contractural arachnodactyly, overgrowth and RT soft tissue bleeding due to a novel homozygous fibulin-4 gene RT mutation."; RL Clin. Genet. 76:276-281(2009). CC -!- SUBUNIT: Interacts with FBN1 (via N-terminal domain) CC (PubMed:17255108). {ECO:0000269|PubMed:17255108}. CC -!- INTERACTION: CC Q08117-2:AES; NbExp=4; IntAct=EBI-743414, EBI-11741437; CC Q9Y4X0:AMMECR1; NbExp=3; IntAct=EBI-743414, EBI-8583355; CC P54259:ATN1; NbExp=3; IntAct=EBI-743414, EBI-945980; CC Q7Z6I8:C5orf24; NbExp=3; IntAct=EBI-743414, EBI-9995695; CC Q02930-3:CREB5; NbExp=7; IntAct=EBI-743414, EBI-10192698; CC P15502:ELN; NbExp=5; IntAct=EBI-743414, EBI-1222108; CC Q5TZK3:FAM74A6; NbExp=5; IntAct=EBI-743414, EBI-10247271; CC Q9UBX5:FBLN5; NbExp=3; IntAct=EBI-743414, EBI-947897; CC P35555:FBN1; NbExp=3; IntAct=EBI-743414, EBI-2505934; CC P56524:HDAC4; NbExp=3; IntAct=EBI-743414, EBI-308629; CC P09022:Hoxa1 (xeno); NbExp=3; IntAct=EBI-743414, EBI-3957603; CC Q5TA82:LCE2D; NbExp=3; IntAct=EBI-743414, EBI-10246750; CC Q5T5A8:LCE3C; NbExp=3; IntAct=EBI-743414, EBI-10245291; CC P28300:LOX; NbExp=7; IntAct=EBI-743414, EBI-3893481; CC P50222:MEOX2; NbExp=3; IntAct=EBI-743414, EBI-748397; CC Q7Z417:NUFIP2; NbExp=5; IntAct=EBI-743414, EBI-1210753; CC Q8WWY3:PRPF31; NbExp=5; IntAct=EBI-743414, EBI-1567797; CC P43115-12:PTGER3; NbExp=3; IntAct=EBI-743414, EBI-10234038; CC Q93062:RBPMS; NbExp=3; IntAct=EBI-743414, EBI-740322; CC Q9BQY4:RHOXF2; NbExp=4; IntAct=EBI-743414, EBI-372094; CC O43765:SGTA; NbExp=6; IntAct=EBI-743414, EBI-347996; CC Q96EQ0:SGTB; NbExp=6; IntAct=EBI-743414, EBI-744081; CC O75716:STK16; NbExp=5; IntAct=EBI-743414, EBI-749295; CC Q9UMX0:UBQLN1; NbExp=4; IntAct=EBI-743414, EBI-741480; CC Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-743414, EBI-10173939; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- DISEASE: Cutis laxa, autosomal recessive, 1B (ARCL1B) CC [MIM:614437]: A connective tissue disorder characterized by loose, CC hyperextensible skin with decreased resilience and elasticity CC leading to a premature aged appearance. Face, hands, feet, joints, CC and torso may be differentially affected. The clinical spectrum of CC autosomal recessive cutis laxa is highly heterogeneous with CC respect to organ involvement and severity. ARCL1B features include CC emphysema, lethal pulmonary artery occlusion, aortic aneurysm, CC cardiopulmonary insufficiency, birth fractures, arachnodactyly, CC and fragility of blood vessels. {ECO:0000269|PubMed:16685658, CC ECO:0000269|PubMed:17937443, ECO:0000269|PubMed:19664000}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}. 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; AJ132819; CAA10791.2; -; mRNA. DR EMBL; AF093119; AAC62108.1; -; mRNA. DR EMBL; AF109121; AAF65188.1; -; mRNA. DR EMBL; AK000980; BAG50843.1; -; mRNA. DR EMBL; AK292079; BAF84768.1; -; mRNA. DR EMBL; AY358899; AAQ89258.1; -; mRNA. DR EMBL; AK075453; BAG52143.1; -; mRNA. DR EMBL; AP001201; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC010456; AAH10456.1; -; mRNA. DR CCDS; CCDS8116.1; -. DR RefSeq; NP_058634.4; NM_016938.4. DR UniGene; Hs.731454; -. DR PDB; 2KL7; NMR; -; A=54-123. DR PDBsum; 2KL7; -. DR ProteinModelPortal; O95967; -. DR SMR; O95967; -. DR BioGrid; 119026; 54. DR DIP; DIP-34518N; -. DR IntAct; O95967; 160. DR MINT; O95967; -. DR STRING; 9606.ENSP00000309953; -. DR GlyConnect; 1199; -. DR iPTMnet; O95967; -. DR PhosphoSitePlus; O95967; -. DR BioMuta; EFEMP2; -. DR jPOST; O95967; -. DR PaxDb; O95967; -. DR PeptideAtlas; O95967; -. DR PRIDE; O95967; -. DR ProteomicsDB; 51148; -. DR DNASU; 30008; -. DR Ensembl; ENST00000307998; ENSP00000309953; ENSG00000172638. DR Ensembl; ENST00000531972; ENSP00000435295; ENSG00000172638. DR GeneID; 30008; -. DR KEGG; hsa:30008; -. DR UCSC; uc001ofy.5; human. DR CTD; 30008; -. DR DisGeNET; 30008; -. DR EuPathDB; HostDB:ENSG00000172638.12; -. DR GeneCards; EFEMP2; -. DR GeneReviews; EFEMP2; -. DR HGNC; HGNC:3219; EFEMP2. DR HPA; HPA023270; -. DR MalaCards; EFEMP2; -. DR MIM; 604633; gene. DR MIM; 614437; phenotype. DR neXtProt; NX_O95967; -. DR OpenTargets; ENSG00000172638; -. DR Orphanet; 90349; Autosomal recessive cutis laxa type 1. DR Orphanet; 314718; Lethal arteriopathy syndrome due to fibulin-4 deficiency. DR PharmGKB; PA27653; -. DR eggNOG; ENOG410IR6U; Eukaryota. DR eggNOG; ENOG410ZNNG; LUCA. DR GeneTree; ENSGT00940000159437; -. DR HOGENOM; HOG000234337; -. DR HOVERGEN; HBG051560; -. DR InParanoid; O95967; -. DR KO; K19866; -. DR OMA; QECHNLP; -. DR OrthoDB; 1174178at2759; -. DR PhylomeDB; O95967; -. DR TreeFam; TF317514; -. DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres. DR SIGNOR; O95967; -. DR EvolutionaryTrace; O95967; -. DR GeneWiki; EFEMP2; -. DR GenomeRNAi; 30008; -. DR PRO; PR:O95967; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000172638; Expressed in 230 organ(s), highest expression level in tendon of biceps brachii. DR ExpressionAtlas; O95967; baseline and differential. DR Genevisible; O95967; HS. DR GO; GO:0005604; C:basement membrane; TAS:ProtInc. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL. DR GO; GO:0048251; P:elastic fiber assembly; IEA:InterPro. DR InterPro; IPR026823; cEGF. DR InterPro; IPR026824; Efemp2. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR037287; Fibulin_3/4/5. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR PANTHER; PTHR44074; PTHR44074; 1. DR PANTHER; PTHR44074:SF3; PTHR44074:SF3; 1. DR Pfam; PF12662; cEGF; 2. DR Pfam; PF07645; EGF_CA; 3. DR SMART; SM00181; EGF; 5. DR SMART; SM00179; EGF_CA; 6. DR SUPFAM; SSF57184; SSF57184; 2. DR PROSITE; PS00010; ASX_HYDROXYL; 4. DR PROSITE; PS01186; EGF_2; 4. DR PROSITE; PS50026; EGF_3; 4. DR PROSITE; PS01187; EGF_CA; 6. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Complete proteome; Disease mutation; KW Disulfide bond; EGF-like domain; Glycoprotein; Polymorphism; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 443 EGF-containing fibulin-like extracellular FT matrix protein 2. FT /FTId=PRO_0000007575. FT DOMAIN 36 81 EGF-like 1; atypical. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 123 163 EGF-like 2; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 164 202 EGF-like 3; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 203 242 EGF-like 4; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 243 282 EGF-like 5; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 283 328 EGF-like 6; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT CARBOHYD 198 198 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 394 394 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 58 121 {ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000269|Ref.11}. FT DISULFID 65 80 {ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000269|Ref.11}. FT DISULFID 71 109 {ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000269|Ref.11}. FT DISULFID 127 140 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 134 149 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 151 162 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 168 177 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 173 186 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 188 201 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 207 217 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 213 226 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 228 241 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 247 258 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 254 267 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 269 281 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 287 300 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 294 309 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 315 327 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT VARIANT 57 57 E -> K (in ARCL1B; dbSNP:rs119489101). FT {ECO:0000269|PubMed:16685658}. FT /FTId=VAR_027019. FT VARIANT 259 259 I -> V (in dbSNP:rs601314). FT {ECO:0000269|PubMed:10601734, FT ECO:0000269|PubMed:10982184, FT ECO:0000269|PubMed:12975309, FT ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16303743, FT ECO:0000269|Ref.2}. FT /FTId=VAR_027020. FT VARIANT 267 267 C -> Y (in ARCL1B; dbSNP:rs193302866). FT {ECO:0000269|PubMed:19664000}. FT /FTId=VAR_067069. FT VARIANT 279 279 R -> C (in ARCL1B; dbSNP:rs119489102). FT {ECO:0000269|PubMed:17937443}. FT /FTId=VAR_067070. FT CONFLICT 5 5 A -> T (in Ref. 1; CAA10791). FT {ECO:0000305}. FT CONFLICT 44 51 EWDPDSQH -> TQTAN (in Ref. 2; AAC62108). FT {ECO:0000305}. FT CONFLICT 46 46 D -> G (in Ref. 4; BAF84768). FT {ECO:0000305}. FT CONFLICT 96 96 P -> L (in Ref. 4; BAG50843). FT {ECO:0000305}. FT CONFLICT 103 111 AQHPNPCPP -> VNTQPLPT (in Ref. 2; FT AAC62108). {ECO:0000305}. FT CONFLICT 294 294 C -> W (in Ref. 2; AAC62108). FT {ECO:0000305}. FT CONFLICT 354 356 RSV -> AER (in Ref. 2; AAC62108). FT {ECO:0000305}. FT CONFLICT 355 355 S -> R (in Ref. 3; AAF65188). FT {ECO:0000305}. FT STRAND 68 73 {ECO:0000244|PDB:2KL7}. FT STRAND 78 82 {ECO:0000244|PDB:2KL7}. FT STRAND 113 116 {ECO:0000244|PDB:2KL7}. SQ SEQUENCE 443 AA; 49405 MW; 9315CFBBAA0FD3A7 CRC64; MLPCASCLPG SLLLWALLLL LLGSASPQDS EEPDSYTECT DGYEWDPDSQ HCRDVNECLT IPEACKGEMK CINHYGGYLC LPRSAAVIND LHGEGPPPPV PPAQHPNPCP PGYEPDDQDS CVDVDECAQA LHDCRPSQDC HNLPGSYQCT CPDGYRKIGP ECVDIDECRY RYCQHRCVNL PGSFRCQCEP GFQLGPNNRS CVDVNECDMG APCEQRCFNS YGTFLCRCHQ GYELHRDGFS CSDIDECSYS SYLCQYRCIN EPGRFSCHCP QGYQLLATRL CQDIDECESG AHQCSEAQTC VNFHGGYRCV DTNRCVEPYI QVSENRCLCP ASNPLCREQP SSIVHRYMTI TSERSVPADV FQIQATSVYP GAYNAFQIRA GNSQGDFYIR QINNVSAMLV LARPVTGPRE YVLDLEMVTM NSLMSYRASS VLRLTVFVGA YTF //