ID A0A2K6SXW8_SAIBB Unreviewed; 1174 AA.
AC A0A2K6SXW8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Neurofascin {ECO:0000313|Ensembl:ENSSBOP00000012205.1};
GN Name=NFASC {ECO:0000313|Ensembl:ENSSBOP00000012205.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000012205.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000012205.1}
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; A0A2K6SXW8; -.
DR Ensembl; ENSSBOT00000028994.1; ENSSBOP00000012205.1; ENSSBOG00000022869.1.
DR GeneTree; ENSGT00940000157024; -.
DR Proteomes; UP000233220; 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; 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:UP000233220};
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..1174
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014412177"
FT TRANSMEM 1044..1065
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 626..721
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 726..819
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 824..926
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 930..1026
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 709..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 132124 MW; 79EA9731C5373082 CRC64;
MARQPAPPWV HTAFLLCLLS LGGAIEIPMD LTQPPTITKQ SVKDHIVDPR DNILIECEAK
GNPAPSFHWT RNSRFFNIAK DPRVSMRRRS GTLVIDFRSG GRPEEYEGEY QCFARNKFGT
ALSNRIRLQV SKSPLWPKEN LDPVVVQEGA PLTLQCNPPP GLPSPVIFWM SSSMEPIAQD
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 HLECRVKHDP SLKLTVSWLK DDEPLYIGNR MKKEDDSLTI FGVAERDQGS
YTCVASTELD QDLAKAYLTV LGRPDRPRDL ELTDLAERSV RLTWIPGDDN NSPITDYVVQ
FEEDQFQPGV WHDHSKYPGS VNSAVLRLSP YVNYQFRVIA INEVGSSHPS LPSERYRTSG
APPESNPGDV KGEGTRKNNM EITWTPMNAT SAFGPNLRYI VKWRRRETRE AWNNVTVWGS
RYVVGQTPVY VPYEIRVQAE NDFGKGPEPE SVIGYSGEDY PRAAPTEVKV RVMNSTAISL
QWNRVYSDTV QGQLREYRAY YWRESSLLKN LWVSQKRQQA SFPGDRLRGV VSRLFPYSNY
KLEMVVVNGR GDGPRSETKE FTTPEGVPSA PRRFRVRQPN LETINLEWDH PEHPNGIMLG
YTLKYVAFNG TKVGKQIVEN FSPNQTKFTV QRTDPVSRYR FTLSARTQVG SGEAVTEESP
APPNEATPTA AYTNNQADIA TQGWFIGLMC AIALLVLILL IVCFIKRSRG GKYPVREKKD
VPLGPEDPKE EDGSFDYSDE DNKPLQGSQT SLDGTIKQQE SDDSLVDYGE GGEGQFNEDG
SFIGQYTVKK DKDETEGNES SEATSPVNAI YSLA
//
