NCAM2_HUMAN
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 03-AUG-2022, entry version 192.
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; 7.
DR DIP; DIP-56211N; -.
DR IntAct; O15394; 6.
DR STRING; 9606.ENSP00000383392; -.
DR GlyConnect; 1546; 7 N-Linked glycans (3 sites).
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; O15394; -.
DR PeptideAtlas; O15394; -.
DR PRIDE; O15394; -.
DR ProteomicsDB; 48635; -. [O15394-1]
DR ProteomicsDB; 6923; -.
DR Antibodypedia; 22282; 310 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 CTD; 4685; -.
DR DisGeNET; 4685; -.
DR GeneCards; NCAM2; -.
DR HGNC; HGNC:7657; NCAM2.
DR HPA; ENSG00000154654; Group enriched (adrenal gland, brain, liver, testis).
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; CEANKGE; -.
DR OrthoDB; 129648at2759; -.
DR PhylomeDB; O15394; -.
DR TreeFam; TF326195; -.
DR PathwayCommons; O15394; -.
DR SignaLink; O15394; -.
DR BioGRID-ORCS; 4685; 11 hits in 1073 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 109 other tissues.
DR ExpressionAtlas; O15394; baseline and differential.
DR Genevisible; O15394; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
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 GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 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 Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 4.
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; SSF48726; SSF48726; 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 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
