ID APOH_HUMAN Reviewed; 345 AA. AC P02749; B2R9M3; Q9UCN7; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 3. DT 03-NOV-2009, entry version 127. DE RecName: Full=Beta-2-glycoprotein 1; DE AltName: Full=Beta-2-glycoprotein I; DE Short=Beta(2)GPI; DE Short=B2GPI; DE AltName: Full=Apolipoprotein H; DE Short=Apo-H; DE AltName: Full=Activated protein C-binding protein; DE AltName: Full=APC inhibitor; DE AltName: Full=Anticardiolipin cofactor; DE Flags: Precursor; GN Name=APOH; Synonyms=B2G1; 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]. RC TISSUE=Liver; RX MEDLINE=91315408; PubMed=1650181; RA Steinkasserer A., Estaller C., Weiss E., Sim R.B., Day A.J.; RT "Complete nucleotide and deduced amino acid sequence of human beta 2- RT glycoprotein I."; RL Biochem. J. 277:387-391(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=92008618; PubMed=1655523; DOI=10.1016/0014-5793(91)81065-G; RA Kristensen T., Schousboe I., Boel E., Mulvihill E.M., Hansen R.R., RA Moeller K.B., Moeller N.P.H., Sottrup-Jensen L.; RT "Molecular cloning and mammalian expression of human beta 2- RT glycoprotein I cDNA."; RL FEBS Lett. 289:183-186(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=92084151; PubMed=1748314; DOI=10.1016/0378-1119(91)90449-L; RA Mehdi H., Nunn M., Steel D.M., Whitehead A.S., Perez M., Walker L., RA Peeples M.E.; RT "Nucleotide sequence and expression of the human gene encoding RT apolipoprotein H (beta 2-glycoprotein I)."; RL Gene 108:293-298(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92273779; PubMed=1339416; DOI=10.1007/BF02591656; RA Day J.R., O'Hara P.J., Grant F.J., Lofton-Day C.E., Berkaw M.N., RA Werner P., Arnaud P.; RT "Molecular cloning and sequence analysis of the cDNA encoding human RT apolipoprotein H (beta 2-glycoprotein I)."; RL Int. J. Clin. Lab. Res. 21:256-263(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92135065; PubMed=1777418; DOI=10.1093/intimm/3.12.1217; RA Matsuura E., Igarashi M., Igarashi Y., Nagae H., Ichikawa K., RA Yasuda T., Koike T.; RT "Molecular definition of human beta 2-glycoprotein I (beta 2-GPI) by RT cDNA cloning and inter-species differences of beta 2-GPI in RT alternation of anticardiolipin binding."; RL Int. Immunol. 3:1217-1221(1991). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=99115472; PubMed=9914524; RX DOI=10.1046/j.1432-1327.1999.00063.x; RA Okkels H., Rasmussen T.E., Sanghera D.K., Kamboh M.I., Kristensen T.; RT "Structure of the human beta2-glycoprotein I (apolipoprotein H) RT gene."; RL Eur. J. Biochem. 259:435-440(1999). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-107. RC TISSUE=Liver; 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 [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-107; HIS-154; RP LEU-266 AND SER-335. RG SeattleSNPs variation discovery resource; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; 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 [10] RP PROTEIN SEQUENCE OF 20-345, GLYCOSYLATION AT ASN-162; ASN-183; ASN-193 RP AND ASN-253, AND DISULFIDE BONDS. RX MEDLINE=84222015; PubMed=6587378; DOI=10.1073/pnas.81.12.3640; RA Lozier J., Takahashi N., Putnam F.W.; RT "Complete amino acid sequence of human plasma beta 2-glycoprotein I."; RL Proc. Natl. Acad. Sci. U.S.A. 81:3640-3644(1984). RN [11] RP PROTEIN SEQUENCE OF 20-44. RX PubMed=1602135; RA Matsuura E., Igarashi Y., Fujimoto M., Ichikawa K., Suzuki T., RA Sumida T., Yasuda T., Koike T.; RT "Heterogeneity of anticardiolipin antibodies defined by the RT anticardiolipin cofactor."; RL J. Immunol. 148:3885-3891(1992). RN [12] RP PROTEIN SEQUENCE OF 20-43. RX MEDLINE=90272666; PubMed=2349221; DOI=10.1073/pnas.87.11.4120; RA McNeil H.P., Simpson R.J., Chesterman C.N., Krilis S.A.; RT "Anti-phospholipid antibodies are directed against a complex antigen RT that includes a lipid-binding inhibitor of coagulation: beta 2- RT glycoprotein I (apolipoprotein H)."; RL Proc. Natl. Acad. Sci. U.S.A. 87:4120-4124(1990). RN [13] RP PROTEIN SEQUENCE OF 20-38. RC TISSUE=Ovarian follicular fluid; RX MEDLINE=21148139; PubMed=11250549; DOI=10.1016/S1096-4959(00)00359-6; RA Aleporou-Marinou V., Pappa H., Yalouris P., Patargias T.; RT "Purification of apolipoprotein H (beta 2-glycoprotein I)-like protein RT from human follicular fluid."; RL Comp. Biochem. Physiol. 128B:537-542(2001). RN [14] RP DISULFIDE BONDS IN C-TERMINAL DOMAIN. RX MEDLINE=93050249; PubMed=1426288; DOI=10.1016/0014-5793(92)81442-O; RA Steinkkasserer A., Barlow P.N., Willis A.C., Kertesz Z., RA Campbell I.D., Sim R.B., Norman D.G.; RT "Activity, disulphide mapping and structural modelling of the fifth RT domain of human beta 2-glycoprotein I."; RL FEBS Lett. 313:193-197(1992). RN [15] RP STRUCTURE OF CARBOHYDRATES. RX MEDLINE=97299942; PubMed=9155091; DOI=10.1023/A:1026378825391; RA Gambino R., Ruiu G., Pagano G., Cassader M.; RT "Qualitative analysis of the carbohydrate composition of RT apolipoprotein H."; RL J. Protein Chem. 16:205-212(1997). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-253, AND MASS RP SPECTROMETRY. RC TISSUE=Bile; RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200; RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; RT "A proteomic analysis of human bile."; RL Mol. Cell. Proteomics 3:715-728(2004). RN [17] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183 AND ASN-193, RP AND MASS SPECTROMETRY. RC TISSUE=Plasma; RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183; ASN-193 AND RP ASN-253, AND MASS SPECTROMETRY. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [19] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-253, AND MASS RP SPECTROMETRY. RC TISSUE=Saliva; RX PubMed=16740002; DOI=10.1021/pr050492k; RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., RA Loo J.A.; RT "Identification of N-linked glycoproteins in human saliva by RT glycoprotein capture and mass spectrometry."; RL J. Proteome Res. 5:1493-1503(2006). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183; ASN-193 AND RP ASN-253, AND MASS SPECTROMETRY. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RC TISSUE=Plasma; RX MEDLINE=99437994; PubMed=10508150; DOI=10.1093/emboj/18.19.5166; RA Bouma B., de Groot P.G., van Den Elsen J.M.H., Ravelli R.B.G., RA Schouten A., Simmelink M.J.A., Derksen R.H.W.M., Kroon J., Gros P.; RT "Adhesion mechanism of human beta(2)-glycoprotein I to phospholipids RT based on its crystal structure."; RL EMBO J. 18:5166-5174(1999). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS). RX MEDLINE=20031634; PubMed=10562535; DOI=10.1093/emboj/18.22.6228; RA Schwarzenbacher R., Zeth K., Diederichs K., Gries A., Kostner G.M., RA Laggner P., Prassl R.; RT "Crystal structure of human beta2-glycoprotein I: implications for RT phospholipid binding and the antiphospholipid syndrome."; RL EMBO J. 18:6228-6239(1999). RN [23] RP VARIANT LEU-266. RX MEDLINE=93273313; PubMed=8099061; DOI=10.1007/BF00217367; RA Steinkasserer A., Doerner C., Wuerzner R., Sim R.B.; RT "Human beta 2-glycoprotein I: molecular analysis of DNA and amino acid RT polymorphism."; RL Hum. Genet. 91:401-402(1993). RN [24] RP VARIANT ASN-107. RX MEDLINE=97369481; PubMed=9225969; DOI=10.1007/s004390050465; RA Sanghera D.K., Kristensen T., Hamman R.F., Kamboh M.I.; RT "Molecular basis of the apolipoprotein H (beta 2-glycoprotein I) RT protein polymorphism."; RL Hum. Genet. 100:57-62(1997). RN [25] RP VARIANTS GLY-325 AND SER-335. RX MEDLINE=97217791; PubMed=9063752; DOI=10.1093/hmg/6.2.311; RA Sanghera D.K., Wagenknecht D.R., McIntyre J.A., Kamboh M.I.; RT "Identification of structural mutations in the fifth domain of RT apolipoprotein H (beta-2-glycoprotein I) which affect phospholipid RT binding."; RL Hum. Mol. Genet. 6:311-316(1997). CC -!- FUNCTION: Binds to various kinds of negatively charged substances CC such as heparin, phospholipids, and dextran sulfate. May prevent CC activation of the intrinsic blood coagulation cascade by binding CC to phospholipids on the surface of damaged cells. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- MISCELLANEOUS: In addition to the conflicts shown in the feature CC table, PubMed:6587378 reports an N-glycosylation site at Asn-188. CC -!- SIMILARITY: Contains 4 Sushi (CCP/SCR) domains. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/apoh/"; CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and CC polymorphism database; CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=APOH"; 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; X58100; CAA41113.1; -; mRNA. DR EMBL; X53595; CAA37664.1; -; mRNA. DR EMBL; X57847; CAA40977.1; -; mRNA. DR EMBL; M62839; AAA51766.1; -; mRNA. DR EMBL; S80305; AAB21330.1; -; mRNA. DR EMBL; Y11493; CAA72279.1; -; Genomic_DNA. DR EMBL; Y11494; CAA72279.1; JOINED; Genomic_DNA. DR EMBL; Y11495; CAA72279.1; JOINED; Genomic_DNA. DR EMBL; X53595; CAA72279.1; JOINED; mRNA. DR EMBL; Y11496; CAA72279.1; JOINED; Genomic_DNA. DR EMBL; Y11497; CAA72279.1; JOINED; Genomic_DNA. DR EMBL; Y11498; CAA72279.1; JOINED; Genomic_DNA. DR EMBL; Y17754; CAA76845.1; -; Genomic_DNA. DR EMBL; AK313838; BAG36570.1; -; mRNA. DR EMBL; AY322156; AAP72014.1; -; Genomic_DNA. DR EMBL; BC020703; AAH20703.1; -; mRNA. DR EMBL; BC026283; AAH26283.1; -; mRNA. DR IPI; IPI00298828; -. DR PIR; S17178; NBHU. DR RefSeq; NP_000033.2; -. DR UniGene; Hs.445358; -. DR PDB; 1C1Z; X-ray; 2.87 A; A=20-345. DR PDB; 1G4F; NMR; -; A=261-345. DR PDB; 1G4G; NMR; -; A=261-345. DR PDB; 1QUB; X-ray; 2.70 A; A=20-329. DR PDBsum; 1C1Z; -. DR PDBsum; 1G4F; -. DR PDBsum; 1G4G; -. DR PDBsum; 1QUB; -. DR IntAct; P02749; 7. DR STRING; P02749; -. DR PeptideAtlas; P02749; -. DR PRIDE; P02749; -. DR Ensembl; ENST00000205948; ENSP00000205948; ENSG00000091583; Homo sapiens. DR GeneID; 350; -. DR KEGG; hsa:350; -. DR UCSC; uc002jfn.2; human. DR CTD; 350; -. DR GeneCards; GC17M061638; -. DR H-InvDB; HIX0014098; -. DR HGNC; HGNC:616; APOH. DR HPA; CAB022214; -. DR HPA; HPA001654; -. DR HPA; HPA003732; -. DR MIM; 138700; gene. DR PharmGKB; PA24903; -. DR HOGENOM; P02749; -. DR HOVERGEN; P02749; -. DR OMA; CIDGTIE; -. DR NextBio; 1441; -. DR PMAP-CutDB; P02749; -. DR ArrayExpress; P02749; -. DR Bgee; P02749; -. DR CleanEx; HS_APOH; -. DR Genevestigator; P02749; -. DR GermOnline; ENSG00000091583; Homo sapiens. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0042627; C:chylomicron; IDA:UniProtKB. DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:UniProtKB. DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:UniProtKB. DR GO; GO:0043499; F:eukaryotic cell surface binding; IDA:UniProtKB. DR GO; GO:0001948; F:glycoprotein binding; IPI:UniProtKB. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW. DR GO; GO:0060230; F:lipoprotein lipase activator activity; IDA:UniProtKB. DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB. DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IDA:UniProtKB. DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB. DR GO; GO:0030195; P:negative regulation of blood coagulation; IDA:UniProtKB. DR GO; GO:0010596; P:negative regulation of endothelial cell mig...; IDA:UniProtKB. DR GO; GO:0001937; P:negative regulation of endothelial cell pro...; IDA:UniProtKB. DR GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:UniProtKB. DR GO; GO:0033033; P:negative regulation of myeloid cell apoptosis; IDA:UniProtKB. DR GO; GO:0034392; P:negative regulation of smooth muscle cell a...; IDA:UniProtKB. DR GO; GO:0031639; P:plasminogen activation; IDA:UniProtKB. DR GO; GO:0030194; P:positive regulation of blood coagulation; TAS:UniProtKB. DR GO; GO:0051006; P:positive regulation of lipoprotein lipase a...; IDA:UniProtKB. DR GO; GO:0006641; P:triglyceride metabolic process; IDA:UniProtKB. DR GO; GO:0034197; P:triglyceride transport; ISS:UniProtKB. DR InterPro; IPR016060; Complement_control_module. DR InterPro; IPR015104; Sushi_2. DR InterPro; IPR000436; Sushi_SCR_CCP. DR Gene3D; G3DSA:2.10.70.10; Complement_control_module; 5. DR Pfam; PF00084; Sushi; 4. DR Pfam; PF09014; Sushi_2; 1. DR SMART; SM00032; CCP; 4. DR PROSITE; PS50923; SUSHI; 4. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Heparin-binding; Polymorphism; Repeat; KW Secreted; Signal; Sushi. FT SIGNAL 1 19 FT CHAIN 20 345 Beta-2-glycoprotein 1. FT /FTId=PRO_0000002059. FT DOMAIN 21 81 Sushi 1. FT DOMAIN 82 139 Sushi 2. FT DOMAIN 140 202 Sushi 3. FT DOMAIN 203 262 Sushi 4. FT REGION 263 345 Sushi-like. FT CARBOHYD 149 149 O-linked (GalNAc...). FT CARBOHYD 162 162 N-linked (GlcNAc...). FT CARBOHYD 183 183 N-linked (GlcNAc...). FT CARBOHYD 193 193 N-linked (GlcNAc...). FT CARBOHYD 253 253 N-linked (GlcNAc...). FT DISULFID 23 66 FT DISULFID 51 79 FT DISULFID 84 124 FT DISULFID 110 137 FT DISULFID 142 188 FT DISULFID 174 200 FT DISULFID 205 248 FT DISULFID 234 260 FT DISULFID 264 315 FT DISULFID 300 325 FT DISULFID 307 345 FT VARIANT 5 5 V -> A (in dbSNP:rs3826358). FT /FTId=VAR_048316. FT VARIANT 107 107 S -> N (in allele APOH*1; FT dbSNP:rs1801692). FT /FTId=VAR_008169. FT VARIANT 154 154 R -> H (in dbSNP:rs8178847). FT /FTId=VAR_019155. FT VARIANT 266 266 V -> L (in 23% of the population; FT dbSNP:rs4581). FT /FTId=VAR_000673. FT VARIANT 325 325 C -> G (loss of phosphatidylserine- FT binding; dbSNP:rs1801689). FT /FTId=VAR_008170. FT VARIANT 335 335 W -> S (in allele APOH*3W; loss of FT phosphatidylserine-binding; FT dbSNP:rs1801690). FT /FTId=VAR_008171. FT CONFLICT 121 121 S -> C (in Ref. 10; AA sequence). FT CONFLICT 188 188 C -> N (in Ref. 10; AA sequence). FT STRAND 23 25 FT STRAND 32 36 FT STRAND 39 41 FT STRAND 46 51 FT STRAND 55 60 FT STRAND 63 65 FT STRAND 79 81 FT STRAND 93 96 FT STRAND 105 110 FT STRAND 114 118 FT STRAND 120 124 FT STRAND 128 132 FT STRAND 136 139 FT STRAND 151 155 FT STRAND 163 165 FT STRAND 169 174 FT STRAND 178 182 FT STRAND 184 188 FT STRAND 192 194 FT STRAND 199 202 FT STRAND 214 217 FT STRAND 229 234 FT STRAND 238 242 FT STRAND 244 248 FT STRAND 252 255 FT STRAND 260 262 FT STRAND 267 270 FT STRAND 272 275 FT STRAND 278 281 FT HELIX 282 285 FT TURN 286 288 FT STRAND 295 301 FT TURN 303 305 FT STRAND 308 314 FT TURN 331 333 FT HELIX 339 341 SQ SEQUENCE 345 AA; 38298 MW; 63101704F8EDFE3F CRC64; MISPVLILFS SFLCHVAIAG RTCPKPDDLP FSTVVPLKTF YEPGEEITYS CKPGYVSRGG MRKFICPLTG LWPINTLKCT PRVCPFAGIL ENGAVRYTTF EYPNTISFSC NTGFYLNGAD SAKCTEEGKW SPELPVCAPI ICPPPSIPTF ATLRVYKPSA GNNSLYRDTA VFECLPQHAM FGNDTITCTT HGNWTKLPEC REVKCPFPSR PDNGFVNYPA KPTLYYKDKA TFGCHDGYSL DGPEEIECTK LGNWSAMPSC KASCKVPVKK ATVVYQGERV KIQEKFKNGM LHGDKVSFFC KNKEKKCSYT EDAQCIDGTI EVPKCFKEHS SLAFWKTDAS DVKPC //