ID NCAM1_HUMAN Reviewed; 858 AA. AC P13591; A8K8T8; P13592; P13593; Q05C58; Q15829; Q16180; Q16209; AC Q59FL7; Q86X47; Q96CJ3; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 3. DT 04-FEB-2015, entry version 164. DE RecName: Full=Neural cell adhesion molecule 1; DE Short=N-CAM-1; DE Short=NCAM-1; DE AltName: CD_antigen=CD56; DE Flags: Precursor; GN Name=NCAM1; Synonyms=NCAM; 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] (ISOFORM 3). RC TISSUE=Skeletal muscle; RX PubMed=3253057; RA Barton C.H., Dickson G., Gower H.J., Rowett L.H., Putt W., Elsom V., RA Moore S.E., Goridis C., Walsh F.S.; RT "Complete sequence and in vitro expression of a tissue-specific RT phosphatidylinositol-linked N-CAM isoform from skeletal muscle."; RL Development 104:165-173(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=1710251; RA Lanier L.L., Chang C., Azuma M., Ruitenberg J.J., Hemperly J.J., RA Phillips J.H.; RT "Molecular and functional analysis of human natural killer cell- RT associated neural cell adhesion molecule (N-CAM/CD56)."; RL J. Immunol. 146:4421-4426(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=8075973; DOI=10.1016/0169-5002(94)90660-2; RA Saito S., Tanio Y., Tachibana I., Hayashi S., Kishimoto T., Kawase I.; RT "Complementary DNA sequence encoding the major neural cell adhesion RT molecule isoform in a human small cell lung cancer cell line."; RL Lung Cancer 10:307-318(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; 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] (ISOFORM 4). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND VARIANT RP ASP-679. RC TISSUE=Brain, Kidney, and Ovary; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 347-369. RX PubMed=1339414; DOI=10.1002/ijc.2910500124; RA van Duijnhoven H.L., Helfrich W., de Leij L., Roebroek A.J., RA van de Ven W.J., Healey K., Culverwell A., Rossell R.J., RA Kemshead J.T., Patel K.; RT "Splicing of the VASE exon of neural cell adhesion molecule (NCAM) in RT human small-cell lung carcinoma (SCLC)."; RL Int. J. Cancer 50:118-123(1992). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 501-858 (ISOFORMS 1/2 AND 3). RC TISSUE=Skeletal muscle; RX PubMed=2887295; DOI=10.1016/0092-8674(87)90178-4; RA Dickson G., Gower H.J., Barton C.H., Prentice H.M., Elsom V.L., RA Moore S.E., Cox R.D., Quinn C., Putt W., Walsh F.S.; RT "Human muscle neural cell adhesion molecule (N-CAM): identification of RT a muscle-specific sequence in the extracellular domain."; RL Cell 50:1119-1130(1987). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 501-858 (ISOFORM 5). RX PubMed=3203385; DOI=10.1016/0092-8674(88)90241-3; RA Gower H.J., Barton C.H., Elsom V.L., Thompson J., Moore S.E., RA Dickson G., Walsh F.S.; RT "Alternative splicing generates a secreted form of N-CAM in muscle and RT brain."; RL Cell 55:955-964(1988). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-459. 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). CC -!- FUNCTION: This protein is a cell adhesion molecule involved in CC neuron-neuron adhesion, neurite fasciculation, outgrowth of CC neurites, etc. CC -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I CC membrane protein. CC -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I CC membrane protein. CC -!- SUBCELLULAR LOCATION: Isoform 3: Cell membrane; Lipid-anchor, GPI- CC anchor. CC -!- SUBCELLULAR LOCATION: Isoform 4: Cell membrane {ECO:0000305}; CC Lipid-anchor, GPI-anchor {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Isoform 5: Secreted. CC -!- SUBCELLULAR LOCATION: Isoform 6: Secreted {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=P13591-2; Sequence=Displayed; CC Name=2; Synonyms=N-CAM 140; CC IsoId=P13591-1; Sequence=VSP_034818; CC Name=3; Synonyms=N-CAM 120; CC IsoId=P13591-3, P13592-2; CC Sequence=VSP_034818, VSP_034822, VSP_034824, VSP_034825; CC Note=GPI-anchor amidated asparagine on Asn-741.; CC Name=4; CC IsoId=P13591-4; Sequence=VSP_034818, VSP_034824, VSP_034825; CC Note=GPI-anchor amidated asparagine on Asn-706.; CC Name=5; Synonyms=C; CC IsoId=P13591-5, P13592-1; CC Sequence=VSP_034821, VSP_034823; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=6; CC IsoId=P13591-6; Sequence=VSP_034819, VSP_034820; CC -!- SIMILARITY: Contains 2 fibronectin type-III domains. CC {ECO:0000255|PROSITE-ProRule:PRU00316}. CC -!- SIMILARITY: Contains 5 Ig-like C2-type (immunoglobulin-like) CC domains. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD92680.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=NCAM entry; CC URL="http://en.wikipedia.org/wiki/NCAM"; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=N-CAM 140; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_264"; 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; X16841; CAA34739.1; -; mRNA. DR EMBL; U63041; AAB04558.1; -; mRNA. DR EMBL; S71824; AAB31836.1; -; mRNA. DR EMBL; AK292453; BAF85142.1; -; mRNA. DR EMBL; AB209443; BAD92680.1; ALT_INIT; mRNA. DR EMBL; BC014205; AAH14205.2; -; mRNA. DR EMBL; BC029119; AAH29119.1; -; mRNA. DR EMBL; BC047244; AAH47244.1; -; mRNA. DR EMBL; S73101; AAB20698.1; -; mRNA. DR EMBL; M17410; AAA59913.1; -; mRNA. DR EMBL; M17409; AAA59912.1; -; mRNA. DR EMBL; M22094; AAA59910.1; -; mRNA. DR EMBL; M22092; AAA59911.1; -; Genomic_DNA. DR EMBL; M22091; AAA59911.1; JOINED; Genomic_DNA. DR CCDS; CCDS73385.1; -. [P13591-2] DR CCDS; CCDS73386.1; -. [P13591-3] DR CCDS; CCDS73387.1; -. [P13591-4] DR CCDS; CCDS73388.1; -. [P13591-1] DR PIR; A31635; A31635. DR PIR; I54773; I54773. DR PIR; S07784; IJHUNG. DR RefSeq; NP_000606.3; NM_000615.6. [P13591-1] DR RefSeq; NP_001070150.1; NM_001076682.3. [P13591-3] DR RefSeq; NP_001229537.1; NM_001242608.1. [P13591-4] DR RefSeq; NP_851996.2; NM_181351.4. [P13591-2] DR UniGene; Hs.503878; -. DR UniGene; Hs.711235; -. DR UniGene; Hs.733031; -. DR PDB; 2E3V; X-ray; 1.95 A; A/B/C=510-619. DR PDB; 2HAZ; X-ray; 1.70 A; A=508-608. DR PDB; 2VKW; X-ray; 2.30 A; A/B=506-702. DR PDB; 2VKX; X-ray; 2.70 A; A/B/C/D/E/F=506-702. DR PDB; 3MTR; X-ray; 1.80 A; A/B=414-611. DR PDBsum; 2E3V; -. DR PDBsum; 2HAZ; -. DR PDBsum; 2VKW; -. DR PDBsum; 2VKX; -. DR PDBsum; 3MTR; -. DR ProteinModelPortal; P13591; -. DR SMR; P13591; 20-706. DR BioGrid; 110764; 21. DR DIP; DIP-59530N; -. DR IntAct; P13591; 7. DR MINT; MINT-4103137; -. DR PhosphoSite; P13591; -. DR DMDM; 205830665; -. DR MaxQB; P13591; -. DR PaxDb; P13591; -. DR PRIDE; P13591; -. DR DNASU; 4684; -. DR Ensembl; ENST00000316851; ENSP00000318472; ENSG00000149294. [P13591-2] DR Ensembl; ENST00000529356; ENSP00000482205; ENSG00000149294. [P13591-6] DR Ensembl; ENST00000531044; ENSP00000484943; ENSG00000149294. [P13591-1] DR Ensembl; ENST00000531817; ENSP00000475074; ENSG00000149294. DR Ensembl; ENST00000621128; ENSP00000481083; ENSG00000149294. [P13591-4] DR Ensembl; ENST00000621850; ENSP00000480774; ENSG00000149294. [P13591-3] DR GeneID; 4684; -. DR KEGG; hsa:4684; -. DR UCSC; uc001pno.3; human. [P13591-6] DR UCSC; uc001pnp.3; human. [P13591-3] DR UCSC; uc001pnq.3; human. [P13591-2] DR UCSC; uc001pnr.3; human. [P13591-1] DR UCSC; uc021qqo.1; human. [P13591-4] DR CTD; 4684; -. DR GeneCards; GC11P112831; -. DR HGNC; HGNC:7656; NCAM1. DR HPA; CAB000142; -. DR HPA; CAB018071; -. DR HPA; HPA039835; -. DR MIM; 116930; gene. DR neXtProt; NX_P13591; -. DR PharmGKB; PA31459; -. DR eggNOG; NOG308439; -. DR GeneTree; ENSGT00780000121882; -. DR HOVERGEN; HBG052579; -. DR InParanoid; P13591; -. DR KO; K06491; -. DR PhylomeDB; P13591; -. DR TreeFam; TF326195; -. DR Reactome; REACT_163906; ECM proteoglycans. DR Reactome; REACT_18312; NCAM1 interactions. DR Reactome; REACT_18334; NCAM signaling for neurite out-growth. DR Reactome; REACT_22272; Signal transduction by L1. DR Reactome; REACT_25078; Interferon gamma signaling. DR ChiTaRS; NCAM1; human. DR EvolutionaryTrace; P13591; -. DR GeneWiki; Neural_cell_adhesion_molecule; -. DR GenomeRNAi; 4684; -. DR NextBio; 18060; -. DR PRO; PR:P13591; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; P13591; -. DR ExpressionAtlas; P13591; baseline and differential. DR Genevestigator; P13591; -. DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 7. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR009138; Neural_cell_adh. DR Pfam; PF00041; fn3; 2. DR Pfam; PF07679; I-set; 5. DR PRINTS; PR01838; NCAMFAMILY. DR SMART; SM00060; FN3; 2. DR SMART; SM00408; IGc2; 5. DR SUPFAM; SSF49265; SSF49265; 1. DR PROSITE; PS50853; FN3; 2. DR PROSITE; PS50835; IG_LIKE; 5. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane; KW Complete proteome; Disulfide bond; Glycoprotein; GPI-anchor; KW Immunoglobulin domain; Lipoprotein; Membrane; Phosphoprotein; KW Polymorphism; Reference proteome; Repeat; Secreted; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 19 {ECO:0000250}. FT CHAIN 20 858 Neural cell adhesion molecule 1. FT /FTId=PRO_0000015009. FT TOPO_DOM 20 718 Extracellular. {ECO:0000255}. FT TRANSMEM 719 739 Helical. {ECO:0000255}. FT TOPO_DOM 740 858 Cytoplasmic. {ECO:0000255}. FT DOMAIN 20 111 Ig-like C2-type 1. FT DOMAIN 116 205 Ig-like C2-type 2. FT DOMAIN 212 301 Ig-like C2-type 3. FT DOMAIN 308 413 Ig-like C2-type 4. FT DOMAIN 416 501 Ig-like C2-type 5. FT DOMAIN 509 608 Fibronectin type-III 1. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT DOMAIN 611 706 Fibronectin type-III 2. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT MOD_RES 784 784 Phosphoserine. {ECO:0000250}. FT CARBOHYD 222 222 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 315 315 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 347 347 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 433 433 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 459 459 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16335952}. FT CARBOHYD 488 488 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 41 96 {ECO:0000305}. FT DISULFID 139 189 {ECO:0000305}. FT DISULFID 235 287 {ECO:0000305}. FT DISULFID 329 395 {ECO:0000305}. FT DISULFID 436 489 {ECO:0000305}. FT VAR_SEQ 354 363 Missing (in isoform 2, isoform 3 and FT isoform 4). {ECO:0000303|PubMed:1710251, FT ECO:0000303|PubMed:2887295, FT ECO:0000303|PubMed:3253057, FT ECO:0000303|PubMed:8075973, FT ECO:0000303|Ref.5}. FT /FTId=VSP_034818. FT VAR_SEQ 364 364 T -> V (in isoform 6). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_034819. FT VAR_SEQ 365 858 Missing (in isoform 6). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_034820. FT VAR_SEQ 609 665 QGEPSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVRY FT RALSSEWKPEIRLPSG -> HSPPPPASASSSTPVPLSPPD FT TTWPLPALATTEPAKNIAQNHCCNMFQAGLHNALMK (in FT isoform 5). {ECO:0000303|PubMed:3203385}. FT /FTId=VSP_034821. FT VAR_SEQ 609 609 Q -> HSPPPPASASSSTPVPLSPPDTTWPLPALATTEPAK FT (in isoform 3). FT {ECO:0000303|PubMed:2887295, FT ECO:0000303|PubMed:3253057}. FT /FTId=VSP_034822. FT VAR_SEQ 666 858 Missing (in isoform 5). FT {ECO:0000303|PubMed:3203385}. FT /FTId=VSP_034823. FT VAR_SEQ 712 736 NGSPTSGLSTGAIVGILIVIFVLLL -> TLGGNSASYTFV FT SLLFSAVTLLLLC (in isoform 3 and isoform FT 4). {ECO:0000303|PubMed:2887295, FT ECO:0000303|PubMed:3253057, FT ECO:0000303|Ref.5}. FT /FTId=VSP_034824. FT VAR_SEQ 737 858 Missing (in isoform 3 and isoform 4). FT {ECO:0000303|PubMed:2887295, FT ECO:0000303|PubMed:3253057, FT ECO:0000303|Ref.5}. FT /FTId=VSP_034825. FT VARIANT 7 7 L -> F (in dbSNP:rs7105734). FT /FTId=VAR_061331. FT VARIANT 260 260 D -> N (in dbSNP:rs17115160). FT /FTId=VAR_049960. FT VARIANT 679 679 E -> D (in dbSNP:rs17115280). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_049961. FT VARIANT 834 834 T -> M (in dbSNP:rs17174409). FT /FTId=VAR_049962. FT CONFLICT 215 215 Q -> R (in Ref. 2; AAB04558). FT {ECO:0000305}. FT CONFLICT 239 239 G -> R (in Ref. 2; AAB04558). FT {ECO:0000305}. FT CONFLICT 500 500 L -> F (in Ref. 2; AAB04558). FT {ECO:0000305}. FT CONFLICT 560 560 Y -> H (in Ref. 4; BAF85142). FT {ECO:0000305}. FT CONFLICT 609 610 QG -> R (in Ref. 8; AAA59913). FT {ECO:0000305}. FT CONFLICT 730 731 Missing (in Ref. 8; AAA59913). FT {ECO:0000305}. FT CONFLICT 821 821 G -> A (in Ref. 8; AAA59913). FT {ECO:0000305}. FT CONFLICT 856 856 S -> N (in Ref. 6; AAH47244). FT {ECO:0000305}. FT STRAND 414 419 {ECO:0000244|PDB:3MTR}. FT STRAND 422 426 {ECO:0000244|PDB:3MTR}. FT STRAND 432 442 {ECO:0000244|PDB:3MTR}. FT STRAND 445 450 {ECO:0000244|PDB:3MTR}. FT STRAND 453 456 {ECO:0000244|PDB:3MTR}. FT STRAND 458 460 {ECO:0000244|PDB:3MTR}. FT STRAND 462 468 {ECO:0000244|PDB:3MTR}. FT STRAND 471 476 {ECO:0000244|PDB:3MTR}. FT HELIX 481 483 {ECO:0000244|PDB:3MTR}. FT STRAND 485 492 {ECO:0000244|PDB:3MTR}. FT STRAND 497 506 {ECO:0000244|PDB:3MTR}. FT STRAND 514 520 {ECO:0000244|PDB:2HAZ}. FT STRAND 525 530 {ECO:0000244|PDB:2HAZ}. FT STRAND 542 549 {ECO:0000244|PDB:2HAZ}. FT STRAND 556 561 {ECO:0000244|PDB:2HAZ}. FT HELIX 562 568 {ECO:0000244|PDB:2HAZ}. FT STRAND 569 573 {ECO:0000244|PDB:2HAZ}. FT STRAND 581 590 {ECO:0000244|PDB:2HAZ}. FT STRAND 601 604 {ECO:0000244|PDB:2HAZ}. FT STRAND 616 621 {ECO:0000244|PDB:2VKW}. FT STRAND 628 633 {ECO:0000244|PDB:2VKW}. FT STRAND 644 651 {ECO:0000244|PDB:2VKW}. FT STRAND 660 662 {ECO:0000244|PDB:2VKW}. FT STRAND 668 671 {ECO:0000244|PDB:2VKW}. FT STRAND 679 688 {ECO:0000244|PDB:2VKW}. FT STRAND 696 701 {ECO:0000244|PDB:2VKW}. SQ SEQUENCE 858 AA; 94574 MW; FD3B9DE80D802554 CRC64; MLQTKDLIWT LFFLGTAVSL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK DISWFSPNGE KLTPNQQRIS VVWNDDSSST LTIYNANIDD AGIYKCVVTG EDGSESEATV NVKIFQKLMF KNAPTPQEFR EGEDAVIVCD VVSSLPPTII WKHKGRDVIL KKDVRFIVLS NNYLQIRGIK KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPTIQARQNI VNATANLGQS VTLVCDAEGF PEPTMSWTKD GEQIEQEEDD EKYIFSDDSS QLTIKKVDKN DEAEYICIAE NKAGEQDATI HLKVFAKPKI TYVENQTAME LEEQVTLTCE ASGDPIPSIT WRTSTRNISS EEKASWTRPE KQETLDGHMV VRSHARVSSL TLKSIQYTDA GEYICTASNT IGQDSQSMYL EVQYAPKLQG PVAVYTWEGN QVNITCEVFA YPSATISWFR DGQLLPSSNY SNIKIYNTPS ASYLEVTPDS ENDFGNYNCT AVNRIGQESL EFILVQADTP SSPSIDQVEP YSSTAQVQFD EPEATGGVPI LKYKAEWRAV GEEVWHSKWY DAKEASMEGI VTIVGLKPET TYAVRLAALN GKGLGEISAA SEFKTQPVQG EPSAPKLEGQ MGEDGNSIKV NLIKQDDGGS PIRHYLVRYR ALSSEWKPEI RLPSGSDHVM LKSLDWNAEY EVYVVAENQQ GKSKAAHFVF RTSAQPTAIP ANGSPTSGLS TGAIVGILIV IFVLLLVVVD ITCYFLNKCG LFMCIAVNLC GKAGPGAKGK DMEEGKAAFS KDESKEPIVE VRTEEERTPN HDGGKHTEPN ETTPLTEPEK GPVEAKPECQ ETETKPAPAE VKTVPNDATQ TKENESKA //