ID NCAM2_HUMAN Reviewed; 837 AA. AC O15394; A8MQ06; B7Z841; Q7Z7F2; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 2. DT 27-MAR-2024, entry version 201. DE RecName: Full=Neural cell adhesion molecule 2; DE Short=N-CAM-2; DE Short=NCAM-2; DE Flags: Precursor; GN Name=NCAM2; Synonyms=NCAM21; 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), AND VARIANT PRO-350. RC TISSUE=Brain; RX PubMed=9226371; DOI=10.1006/geno.1997.4782; RA Paoloni-Giacobino A., Chen H., Antonarakis S.E.; RT "Cloning of a novel human neural cell adhesion molecule gene (NCAM2) that RT maps to chromosome region 21q21 and is potentially involved in Down RT syndrome."; RL Genomics 43:43-51(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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., 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP GLYCOSYLATION AT ASN-445 AND ASN-562. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [6] RP STRUCTURE BY NMR OF 486-591. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the fibronectin type-III domain of human neural cell RT adhesion molecule 2."; RL Submitted (OCT-2006) to the PDB data bank. CC -!- FUNCTION: May play important roles in selective fasciculation and zone- CC to-zone projection of the primary olfactory axons. CC -!- INTERACTION: CC O15394; O15394: NCAM2; NbExp=3; IntAct=EBI-2679983, EBI-2679983; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O15394-1; Sequence=Displayed; CC Name=2; CC IsoId=O15394-2; Sequence=VSP_056637, VSP_056638, VSP_056639; CC -!- TISSUE SPECIFICITY: Expressed most strongly in adult and fetal brain. 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; U75330; AAB80803.1; -; mRNA. DR EMBL; AK302870; BAH13827.1; -; mRNA. DR EMBL; AP001114; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001115; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001136; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001137; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001138; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001252; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC052946; AAH52946.1; -; mRNA. DR CCDS; CCDS42910.1; -. [O15394-1] DR RefSeq; NP_004531.2; NM_004540.3. [O15394-1] DR RefSeq; XP_016883847.1; XM_017028358.1. DR PDB; 2DOC; NMR; -; A=486-591. DR PDB; 2JLL; X-ray; 2.30 A; A=301-689. DR PDB; 2KBG; NMR; -; A=592-693. DR PDB; 2V5T; X-ray; 2.00 A; A=115-301. DR PDB; 2VAJ; X-ray; 2.70 A; A=21-113. DR PDB; 2WIM; X-ray; 3.00 A; A/B=19-301. DR PDB; 2XY1; X-ray; 1.90 A; A=209-398. DR PDB; 2XY2; X-ray; 1.77 A; A=19-207. DR PDB; 2XYC; X-ray; 2.65 A; A=301-591. DR PDBsum; 2DOC; -. DR PDBsum; 2JLL; -. DR PDBsum; 2KBG; -. DR PDBsum; 2V5T; -. DR PDBsum; 2VAJ; -. DR PDBsum; 2WIM; -. DR PDBsum; 2XY1; -. DR PDBsum; 2XY2; -. DR PDBsum; 2XYC; -. DR AlphaFoldDB; O15394; -. DR SMR; O15394; -. DR BioGRID; 110765; 8. DR DIP; DIP-56211N; -. DR IntAct; O15394; 16. DR STRING; 9606.ENSP00000383392; -. DR UniLectin; O15394; -. DR GlyConnect; 1546; 7 N-Linked glycans (3 sites). DR GlyCosmos; O15394; 8 sites, 7 glycans. DR GlyGen; O15394; 11 sites, 7 N-linked glycans (3 sites). DR iPTMnet; O15394; -. DR PhosphoSitePlus; O15394; -. DR SwissPalm; O15394; -. DR BioMuta; NCAM2; -. DR jPOST; O15394; -. DR MassIVE; O15394; -. DR MaxQB; O15394; -. DR PaxDb; 9606-ENSP00000383392; -. DR PeptideAtlas; O15394; -. DR ProteomicsDB; 48635; -. [O15394-1] DR ProteomicsDB; 6923; -. DR Antibodypedia; 22282; 359 antibodies from 38 providers. DR DNASU; 4685; -. DR Ensembl; ENST00000400546.6; ENSP00000383392.1; ENSG00000154654.15. [O15394-1] DR GeneID; 4685; -. DR KEGG; hsa:4685; -. DR MANE-Select; ENST00000400546.6; ENSP00000383392.1; NM_004540.5; NP_004531.2. DR UCSC; uc002yld.3; human. [O15394-1] DR AGR; HGNC:7657; -. DR CTD; 4685; -. DR DisGeNET; 4685; -. DR GeneCards; NCAM2; -. DR HGNC; HGNC:7657; NCAM2. DR HPA; ENSG00000154654; Tissue enhanced (adrenal gland, brain). DR MIM; 602040; gene. DR neXtProt; NX_O15394; -. DR OpenTargets; ENSG00000154654; -. DR PharmGKB; PA31460; -. DR VEuPathDB; HostDB:ENSG00000154654; -. DR eggNOG; KOG3510; Eukaryota. DR GeneTree; ENSGT00940000157860; -. DR InParanoid; O15394; -. DR OMA; XPPAITM; -. DR OrthoDB; 5233206at2759; -. DR PhylomeDB; O15394; -. DR TreeFam; TF326195; -. DR PathwayCommons; O15394; -. DR SignaLink; O15394; -. DR BioGRID-ORCS; 4685; 12 hits in 1153 CRISPR screens. DR ChiTaRS; NCAM2; human. DR EvolutionaryTrace; O15394; -. DR GenomeRNAi; 4685; -. DR Pharos; O15394; Tbio. DR PRO; PR:O15394; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; O15394; Protein. DR Bgee; ENSG00000154654; Expressed in ventricular zone and 111 other cell types or tissues. DR ExpressionAtlas; O15394; baseline and differential. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl. DR GO; GO:0007158; P:neuron cell-cell adhesion; TAS:ProtInc. DR CDD; cd00063; FN3; 2. DR CDD; cd00096; Ig; 1. DR CDD; cd20970; IgI_1_MuSK; 1. DR CDD; cd05866; IgI_1_NCAM-2; 1. DR CDD; cd05870; IgI_NCAM-2; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 7. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013106; Ig_V-set. DR InterPro; IPR009138; Neural_cell_adh. DR PANTHER; PTHR12231; CTX-RELATED TYPE I TRANSMEMBRANE PROTEIN; 1. DR PANTHER; PTHR12231:SF231; NEURAL CELL ADHESION MOLECULE 2; 1. DR Pfam; PF00041; fn3; 2. DR Pfam; PF07679; I-set; 4. DR Pfam; PF13927; Ig_3; 1. DR PRINTS; PR01838; NCAMFAMILY. DR SMART; SM00060; FN3; 2. DR SMART; SM00409; IG; 5. DR SMART; SM00408; IGc2; 5. DR SMART; SM00406; IGv; 3. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR SUPFAM; SSF48726; Immunoglobulin; 5. DR PROSITE; PS50853; FN3; 2. DR PROSITE; PS50835; IG_LIKE; 5. DR Genevisible; O15394; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane; KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..837 FT /note="Neural cell adhesion molecule 2" FT /id="PRO_0000015018" FT TOPO_DOM 20..697 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 698..718 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 719..837 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 21..108 FT /note="Ig-like C2-type 1" FT DOMAIN 113..202 FT /note="Ig-like C2-type 2" FT DOMAIN 208..297 FT /note="Ig-like C2-type 3" FT DOMAIN 302..396 FT /note="Ig-like C2-type 4" FT DOMAIN 401..491 FT /note="Ig-like C2-type 5" FT DOMAIN 498..591 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 593..688 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 764..818 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 764..784 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 800..816 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 765 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35136" FT MOD_RES 780 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O35136" FT MOD_RES 786 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35136" FT CARBOHYD 177 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 219 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 309 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 406 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 419 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 445 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519" FT CARBOHYD 474 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 562 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519" FT DISULFID 42..93 FT /evidence="ECO:0000305" FT DISULFID 136..186 FT /evidence="ECO:0000305" FT DISULFID 232..281 FT /evidence="ECO:0000305" FT DISULFID 322..380 FT /evidence="ECO:0000305" FT DISULFID 422..475 FT /evidence="ECO:0000305" FT VAR_SEQ 1..18 FT /note="MSLLLSFYLLGLLVSSGQ -> MVRSDSGGQVYLDYHNRQGLFVDWKYNEAL FT YLEEGQPETYYRT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056637" FT VAR_SEQ 399 FT /note="Y -> S (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056638" FT VAR_SEQ 400..837 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056639" FT VARIANT 347 FT /note="D -> N (in dbSNP:rs35654962)" FT /id="VAR_047897" FT VARIANT 350 FT /note="L -> P (in dbSNP:rs232518)" FT /evidence="ECO:0000269|PubMed:9226371" FT /id="VAR_047898" FT CONFLICT 49 FT /note="E -> R (in Ref. 1; AAB80803)" FT /evidence="ECO:0000305" FT CONFLICT 72 FT /note="E -> G (in Ref. 1; AAB80803)" FT /evidence="ECO:0000305" FT CONFLICT 163 FT /note="F -> L (in Ref. 1; AAB80803)" FT /evidence="ECO:0000305" FT CONFLICT 374 FT /note="D -> G (in Ref. 1; AAB80803)" FT /evidence="ECO:0000305" FT CONFLICT 662..667 FT /note="YEVQIT -> MKFRLP (in Ref. 1; AAB80803)" FT /evidence="ECO:0000305" FT STRAND 20..26 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 28..33 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 38..46 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 49..54 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 65..72 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 75..80 FT /evidence="ECO:0007829|PDB:2XY2" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 89..96 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:2WIM" FT STRAND 102..112 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 116..119 FT /evidence="ECO:0007829|PDB:2V5T" FT STRAND 123..127 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:2V5T" FT STRAND 145..150 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 163..165 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:2XY2" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 182..190 FT /evidence="ECO:0007829|PDB:2XY2" FT TURN 191..194 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 195..206 FT /evidence="ECO:0007829|PDB:2XY2" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:2WIM" FT STRAND 228..231 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 233..235 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 241..246 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 254..260 FT /evidence="ECO:0007829|PDB:2XY1" FT TURN 261..264 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:2XY1" FT HELIX 273..275 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 277..285 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 288..307 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 310..312 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 317..328 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 331..336 FT /evidence="ECO:0007829|PDB:2XY1" FT TURN 337..340 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 341..343 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:2XYC" FT STRAND 354..359 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 362..369 FT /evidence="ECO:0007829|PDB:2XY1" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 376..384 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 387..397 FT /evidence="ECO:0007829|PDB:2XY1" FT STRAND 409..412 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 418..422 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 424..428 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 431..436 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 439..442 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 449..453 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 458..462 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 469..479 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 482..492 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 500..507 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 512..517 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 527..536 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 543..546 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 548..550 FT /evidence="ECO:0007829|PDB:2DOC" FT STRAND 552..556 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 564..575 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 576..580 FT /evidence="ECO:0007829|PDB:2XYC" FT STRAND 584..587 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 599..604 FT /evidence="ECO:0007829|PDB:2JLL" FT TURN 605..607 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 608..613 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 619..621 FT /evidence="ECO:0007829|PDB:2KBG" FT STRAND 625..631 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 640..645 FT /evidence="ECO:0007829|PDB:2KBG" FT TURN 646..648 FT /evidence="ECO:0007829|PDB:2KBG" FT STRAND 650..653 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 661..670 FT /evidence="ECO:0007829|PDB:2JLL" FT STRAND 678..683 FT /evidence="ECO:0007829|PDB:2JLL" SQ SEQUENCE 837 AA; 93046 MW; 878EC1110562B3F3 CRC64; MSLLLSFYLL GLLVSSGQAL LQVTISLSKV ELSVGESKFF TCTAIGEPES IDWYNPQGEK IISTQRVVVQ KEGVRSRLTI YNANIEDAGI YRCQATDAKG QTQEATVVLE IYQKLTFREV VSPQEFKQGE DAEVVCRVSS SPAPAVSWLY HNEEVTTISD NRFAMLANNN LQILNINKSD EGIYRCEGRV EARGEIDFRD IIVIVNVPPA ISMPQKSFNA TAERGEEMTF SCRASGSPEP AISWFRNGKL IEENEKYILK GSNTELTVRN IINSDGGPYV CRATNKAGED EKQAFLQVFV QPHIIQLKNE TTYENGQVTL VCDAEGEPIP EITWKRAVDG FTFTEGDKSL DGRIEVKGQH GSSSLHIKDV KLSDSGRYDC EAASRIGGHQ KSMYLDIEYA PKFISNQTIY YSWEGNPINI SCDVKSNPPA SIHWRRDKLV LPAKNTTNLK TYSTGRKMIL EIAPTSDNDF GRYNCTATNH IGTRFQEYIL ALADVPSSPY GVKIIELSQT TAKVSFNKPD SHGGVPIHHY QVDVKEVASE IWKIVRSHGV QTMVVLNNLE PNTTYEIRVA AVNGKGQGDY SKIEIFQTLP VREPSPPSIH GQPSSGKSFK LSITKQDDGG APILEYIVKY RSKDKEDQWL EKKVQGNKDH IILEHLQWTM GYEVQITAAN RLGYSEPTVY EFSMPPKPNI IKDTLFNGLG LGAVIGLGVA ALLLILVVTD VSCFFIRQCG LLMCITRRMC GKKSGSSGKS KELEEGKAAY LKDGSKEPIV EMRTEDERVT NHEDGSPVNE PNETTPLTEP EKLPLKEEDG KEALNPETIE IKVSNDIIQS KEDDSKA //