ID A0A2K5D3S0_AOTNA Unreviewed; 1184 AA.
AC A0A2K5D3S0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Neuronal cell adhesion molecule {ECO:0000313|Ensembl:ENSANAP00000015601.1};
GN Name=NRCAM {ECO:0000313|Ensembl:ENSANAP00000015601.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000015601.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000015601.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000256|ARBA:ARBA00008588}.
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DR AlphaFoldDB; A0A2K5D3S0; -.
DR Ensembl; ENSANAT00000033442.1; ENSANAP00000015601.1; ENSANAG00000025315.1.
DR GeneTree; ENSGT00940000155419; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 4.
DR CDD; cd05868; Ig4_NrCAM; 1.
DR CDD; cd05874; IgI_NrCAM; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 10.
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; IPR026966; Neurofascin/L1/NrCAM_C.
DR PANTHER; PTHR44170:SF15; NEURONAL CELL ADHESION MOLECULE; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 3.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1184
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014469719"
FT TRANSMEM 1049..1070
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..136
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 143..237
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 250..339
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 344..431
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 437..524
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 528..615
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 622..717
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 719..816
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 821..923
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 927..1024
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 1079..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1184 AA; 130978 MW; 34FCFAC926EC8539 CRC64;
MQLKIMPKKK RLSAGRVPLI LFLCQMISAL EVPLDPKLLE DCKLVQPPTI TQQSPKDYII
DPRENIVIQC EAKGKPPPSF SWTRNGTHFD IDKDPLVTMK PGTGTLIINI MSEGKAETYE
GVYQCTARNE RGAAISNNIV VRPSRSPLWT KEKLEPITLQ NGQSLVLPCR PPIGLPPPII
FWMDNSFQRL PQSERVSQGL NGDLYFSNVL PEDTREDYIC YARFNHTQTI QQKQPISVKV
ISAKSNRERP PTFLTPEGNA SNKEELRGNV LLLECIAEGL PTPLIYWAKE DGILPTNRTS
YKNFKKTLQI THVSEADSGN YQCIAKNALG AIHHTISVRV KAAPYWIMAP QNLVLSPGED
GTLICRANGN PKPRISWLTN GVPIEIAPDD PSRKIDGDTI IFSNVQERSS AVYQCNASNE
YGYLLANAFV NVLAEPPRIL TPANTLYQVI ANRPALLDCA FFGSPLPTIE WFKGAKGSAL
HEDIYVLHEN GTLEIPVAQK DSTGTYTCVA RNKLGMAKND VHLEIKDPTW IIKQPEYAVV
QRGGMVSFEC KVKHDHTLVL TVLWLKDNEE LPNDERFTVD KDHLVVADVS DDDSGTYTCV
ANTTLDSVSA SAVLSVVDVP NPPFDLELTD QLDKSVQLSW TPGDDNNSPI SKFIIEYEDA
MHEPGLWHHQ TEVSGTQTTA QLKLSPYVNY SFRVTAVNSI GQSLPSEASE QYLTKASEPD
KNPTAVEGLG SEPDNLVITW KPLNGFESNG PGLQYKVSWR QKDGDDEWTS VVVANVSKYI
VSGTPTFVPY LIKVQALNDV GFAPEPAVVM GHSGEDLPMV APGNVRVNVV NSTLAEVHWD
PVPLKSIRGH LQGYRIYYWK TQNSPKRNRR HIEKKILTFQ GSKTHGMLPG LEPFSHYTLN
VRVVNGKGEG PASPDRVFNT PEGVPSAPSS LKIVNPTLDS LTLEWDPPSH PNGILTEYTL
KYQPINSTHE LGPLVDLKIP ANKTRWTLKN LNFSTRYKFY FYAQTSAGSG SQITEEAVTT
VDEAGILPPD VGAGKAMASR QVDIATQGWF IGLMCAVALL ILILLIVCFI RRNKGGKYPV
KEKEDAHADP EIQPMKEDDG TFGEYSDAED HKPLKKGSRT PSDRTVKKED SDDSLVDYGE
GVNGQFNEDG SFIGQYSGKK EKEPAEGNES SEAPSPVNAM NSFV
//
