RBCC

NCAM2 (NCAM21) [Confidence: low (only semi-automatic identification from reviews)]
Neural cell adhesion molecule 2; N-CAM-2; NCAM-2; Flags: Precursor

UniProt O15394
ID NCAM2_HUMAN Reviewed; 837 AA.
AC O15394; A8MQ06; Q7Z7F2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-JUL-2008, sequence version 2.
DT 22-JAN-2014, entry version 132.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], 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)
RT that maps to chromosome region 21q21 and is potentially involved in
RT Down syndrome.";
RL Genomics 43:43-51(1997).
RN [2]
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.,
RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
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 [5]
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
RT cell adhesion molecule 2.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: May play important roles in selective fasciculation and
CC zone-to-zone projection of the primary olfactory axons.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Expressed most strongly in adult and fetal
CC brain.
CC -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC -!- SIMILARITY: Contains 5 Ig-like C2-type (immunoglobulin-like)
CC domains.
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DR EMBL; U75330; AAB80803.1; -; mRNA.
DR EMBL; AP001138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052946; AAH52946.1; -; mRNA.
DR RefSeq; NP_004531.2; NM_004540.3.
DR UniGene; Hs.473450; -.
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 ProteinModelPortal; O15394; -.
DR SMR; O15394; 19-693.
DR DIP; DIP-56211N; -.
DR IntAct; O15394; 2.
DR STRING; 9606.ENSP00000383392; -.
DR PhosphoSite; O15394; -.
DR PaxDb; O15394; -.
DR PRIDE; O15394; -.
DR Ensembl; ENST00000400546; ENSP00000383392; ENSG00000154654.
DR GeneID; 4685; -.
DR KEGG; hsa:4685; -.
DR UCSC; uc002yld.2; human.
DR CTD; 4685; -.
DR GeneCards; GC21P022370; -.
DR H-InvDB; HIX0027799; -.
DR HGNC; HGNC:7657; NCAM2.
DR HPA; HPA030900; -.
DR MIM; 602040; gene.
DR neXtProt; NX_O15394; -.
DR PharmGKB; PA31460; -.
DR eggNOG; NOG308439; -.
DR HOGENOM; HOG000074124; -.
DR HOVERGEN; HBG052579; -.
DR InParanoid; O15394; -.
DR KO; K06491; -.
DR OMA; EPTISWY; -.
DR OrthoDB; EOG75MVVH; -.
DR ChiTaRS; NCAM2; human.
DR EvolutionaryTrace; O15394; -.
DR GenomeRNAi; 4685; -.
DR NextBio; 18068; -.
DR PRO; PR:O15394; -.
DR ArrayExpress; O15394; -.
DR Bgee; O15394; -.
DR CleanEx; HS_NCAM2; -.
DR Genevestigator; O15394; -.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0007158; P:neuron cell-cell adhesion; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR003961; Fibronectin_type3.
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; Cell adhesion; Cell membrane; Complete proteome;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Polymorphism; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 19 Potential.
FT CHAIN 20 837 Neural cell adhesion molecule 2.
FT /FTId=PRO_0000015018.
FT TOPO_DOM 20 697 Extracellular (Potential).
FT TRANSMEM 698 718 Helical; (Potential).
FT TOPO_DOM 719 837 Cytoplasmic (Potential).
FT DOMAIN 21 108 Ig-like C2-type 1.
FT DOMAIN 113 202 Ig-like C2-type 2.
FT DOMAIN 208 297 Ig-like C2-type 3.
FT DOMAIN 302 396 Ig-like C2-type 4.
FT DOMAIN 401 491 Ig-like C2-type 5.
FT DOMAIN 498 591 Fibronectin type-III 1.
FT DOMAIN 593 688 Fibronectin type-III 2.
FT CARBOHYD 177 177 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 219 219 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 309 309 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 406 406 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 419 419 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 445 445 N-linked (GlcNAc...).
FT CARBOHYD 474 474 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 562 562 N-linked (GlcNAc...).
FT DISULFID 42 93 Probable.
FT DISULFID 136 186 Probable.
FT DISULFID 232 281 Probable.
FT DISULFID 322 380 Probable.
FT DISULFID 422 475 Probable.
FT VARIANT 347 347 D -> N (in dbSNP:rs35654962).
FT /FTId=VAR_047897.
FT VARIANT 350 350 L -> P (in dbSNP:rs232518).
FT /FTId=VAR_047898.
FT CONFLICT 49 49 E -> R (in Ref. 1; AAB80803).
FT CONFLICT 72 72 E -> G (in Ref. 1; AAB80803).
FT CONFLICT 163 163 F -> L (in Ref. 1; AAB80803).
FT CONFLICT 374 374 D -> G (in Ref. 1; AAB80803).
FT CONFLICT 662 667 YEVQIT -> MKFRLP (in Ref. 1; AAB80803).
FT STRAND 20 26
FT STRAND 28 33
FT STRAND 38 46
FT STRAND 49 54
FT STRAND 65 72
FT STRAND 75 80
FT HELIX 85 87
FT STRAND 89 96
FT STRAND 98 100
FT STRAND 102 112
FT STRAND 116 119
FT STRAND 123 127
FT STRAND 132 134
FT STRAND 137 139
FT STRAND 145 150
FT STRAND 152 154
FT STRAND 163 165
FT STRAND 171 173
FT HELIX 178 180
FT STRAND 182 190
FT TURN 191 194
FT STRAND 195 206
FT STRAND 210 212
FT STRAND 217 221
FT STRAND 222 224
FT STRAND 228 231
FT STRAND 233 235
FT STRAND 241 246
FT STRAND 254 260
FT TURN 261 264
FT STRAND 265 268
FT HELIX 273 275
FT STRAND 277 285
FT STRAND 288 307
FT STRAND 310 312
FT STRAND 317 328
FT STRAND 331 336
FT TURN 337 340
FT STRAND 341 343
FT STRAND 350 352
FT STRAND 354 359
FT STRAND 362 369
FT HELIX 372 374
FT STRAND 376 384
FT STRAND 387 397
FT STRAND 409 412
FT STRAND 418 422
FT STRAND 424 428
FT STRAND 431 436
FT STRAND 439 442
FT STRAND 449 453
FT STRAND 458 462
FT STRAND 469 479
FT STRAND 482 492
FT STRAND 500 507
FT STRAND 512 517
FT STRAND 527 536
FT STRAND 543 546
FT STRAND 548 550
FT STRAND 552 556
FT STRAND 564 575
FT STRAND 576 580
FT STRAND 584 587
FT STRAND 599 604
FT TURN 605 607
FT STRAND 608 613
FT STRAND 619 621
FT STRAND 625 631
FT STRAND 640 645
FT TURN 646 648
FT STRAND 650 653
FT STRAND 661 670
FT STRAND 678 683
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
//

MIM 602040
*RECORD*
*FIELD* NO
602040
*FIELD* TI
*602040 CELL ADHESION MOLECULE, NEURAL, 2; NCAM2
*FIELD* TX

CLONING

In order to identify genes on human chromosome 21, Paoloni-Giacobino et
read moreal. (1997) performed exon trapping from chromosome 21-specific cosmids.
They identified a novel trapped exon that showed homology to NCAM1
(116930). They cloned the corresponding cDNA from a human fetal brain
cDNA library and reported that it encodes an 837-amino acid polypeptide
containing 5 immunoglobulin-like domains, 2 fibronectin type III
domains, and 1 predicted transmembrane domain. The overall size and
structure of the predicted protein are similar to the shorter isoform of
NCAM1. The authors were unable to identify any longer cDNAs.
Paoloni-Giacobino et al. (1997) showed by Northern blot analysis that
the NCAM2 gene is expressed as mRNAs of 9.5 and 4.4 kb in fetal and
adult brain; they observed these and other transcript sizes at lower
levels in several other tissues.

MAPPING

Paoloni-Giacobino et al. (1997) screened somatic cell hybrid panels to
map the NCAM2 gene to human chromosome 21q21. They stated that this gene
may be involved in some Down syndrome phenotypes.

*FIELD* RF
1. Paoloni-Giacobino, A.; Chen, H.; Antonarakis, S. E.: Cloning of
a novel human neural cell adhesion molecule gene (NCAM2) that maps
to chromosome region 21q21 and is potentially involved in Down syndrome. Genomics 43:
43-51, 1997.

*FIELD* CD
Jennifer P. Macke: 10/9/1997

*FIELD* ED
alopez: 08/25/2009
alopez: 10/10/1997
alopez: 10/9/1997

RBCC Red Blood Cell Collection

Full text data of NCAM2