ID A0A2K6BQB7_MACNE Unreviewed; 1184 AA.
AC A0A2K6BQB7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Neurofascin {ECO:0000313|Ensembl:ENSMNEP00000013611.1};
GN Name=NFASC {ECO:0000313|Ensembl:ENSMNEP00000013611.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000013611.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000013611.1}
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; A0A2K6BQB7; -.
DR Ensembl; ENSMNET00000037812.1; ENSMNEP00000013611.1; ENSMNEG00000029843.1.
DR GeneTree; ENSGT00940000157024; -.
DR OMA; NHSSYPG; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000029843; Expressed in temporal lobe and 9 other cell types or tissues.
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; cd05731; Ig3_L1-CAM_like; 1.
DR CDD; cd05845; IgI_2_L1-CAM_like; 1.
DR CDD; cd05875; IgI_hNeurofascin_like; 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; IPR013151; Immunoglobulin.
DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR InterPro; IPR026965; NFASC_Ig-like.
DR PANTHER; PTHR44170:SF12; NEUROFASCIN; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 2.
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:UP000233120};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1184
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014386793"
FT TRANSMEM 1054..1075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..131
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 137..224
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 255..343
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 348..435
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 440..528
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 532..614
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 641..736
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 741..834
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 839..941
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 945..1041
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 721..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1184 AA; 133246 MW; C40BA9FEA3C7B89C CRC64;
MARQPPPPWV HAAFLLCLLS LGGAIEIPMD LTQPPTITKQ SVKDHIVDPR DNILIECEAK
GNPAPSFHWT RNSRFFNIAK DPRVSMRRRS GTLVIDFRSG GRPEEYEGEY QCFARNKFGT
ALSNRIRLQV SKSPLWPKEN LDPVVVQEGA PLTLQCNPPP GLPSPVIFWM SSSMEPITQD
KRVSQGHNGD LYFSNVMLQD MQTDYSCNAR FHFTHTIQQK NPFTLKVLTN HPYNDSSLRN
HPDMYSARGV AERTPSFMYP QGTASSQMVL RGMDLLLECI ASGVPTPDIA WYKKGGDLPS
DKAKFENFNK ALRITNVSEE DSGEYFCLAS NKMGSIRHTI SVRVKAAPYW LDEPKNLILA
PGEDGRLVCR ANGNPKPTVQ WMVNGEPLQS APPNPNREVA GDTIIFRDTQ ISSRAVYQCN
TSNEHGYLLA NAFVSVLDVP PRMLSPRNQL IRVILYNRTR LDCPFFGSPI PTLRWFKNGQ
GSNLDGGNYH VYENGSLEIK MIRKEDQGIY TCVATNILGK AENQVRLEVK DPTRIYRMPE
DQVAKRGTTV QLECRVKHDP SLKLTVSWLK DDEPLYIGNR MKKEDDSLTI FGVAERDQGS
YTCVASTELD QDLAKAYLTV LADQATPTNR LAALPKGRPD RPRDLELTDL AERSVRLTWI
PGDDNNSPIT DYVVQFEEDQ FQPGVWHDHS KYPGSVNSAV LRLSPYVNYQ FRVIAVNEVG
SSHPSLPSER YRTSGAPPES NPGDVKGEGT RKNNMEITWT PMNATSAFGP NLRYIVKWRR
RETREAWNNV TVWGSRYVVG QTPVYVPYEI RVQAENDFGK GPEPESVIGY SGEDYPRAAP
TEVKVRVMNS TAISLQWNRV YPDTVQGQLR EYRAYYWRES SLLKNLWVSQ KRQQASFPGD
RLRGVVSRLF PYSNYKLEMV VVNGRGDGPR SETKEFTTPE GVPSAPRRFR VRQPNLETIN
LEWDHPEHPN GIMTGYTLKY VAFNGTKVGK QIVENFSPNQ TKFTVQRTDP VSRYRFTLSA
RTQVGSGEAV TEESPAPPNE AYTNNQADIA TQGWFIGLMC AIALLVLILL IVCFIKRSRG
GKYPVREKKD VPLGPEDPKE EDGSFDYSDE DNKPLQGSQT SLDGTIKQQE SDDSLVDYGE
GGEGQFNEDG SFIGQYTVKK DKEETEGNES SEATSPVNAI YSLA
//
