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Database: UniProt
Entry: W5N2A4_LEPOC
LinkDB: W5N2A4_LEPOC
Original site: W5N2A4_LEPOC 
ID   W5N2A4_LEPOC            Unreviewed;      1377 AA.
AC   W5N2A4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Neurofascin homolog (chicken) a {ECO:0000313|Ensembl:ENSLOCP00000014763.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000014763.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000014763.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   EMBL; AHAT01016688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7918.ENSLOCP00000014763; -.
DR   Ensembl; ENSLOCT00000014792.1; ENSLOCP00000014763.1; ENSLOCG00000011984.1.
DR   eggNOG; KOG3513; Eukaryota.
DR   GeneTree; ENSGT00940000157024; -.
DR   InParanoid; W5N2A4; -.
DR   OMA; NHSSYPG; -.
DR   Proteomes; UP000018468; Linkage group LG3.
DR   Bgee; ENSLOCG00000011984; Expressed in ovary and 11 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0007420; P:brain development; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   CDD; cd00063; FN3; 5.
DR   CDD; cd00096; Ig; 1.
DR   CDD; cd05731; Ig3_L1-CAM_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 11.
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:SF12; NEUROFASCIN; 1.
DR   PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR   Pfam; PF13882; Bravo_FIGEY; 1.
DR   Pfam; PF00041; fn3; 5.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF13927; Ig_3; 2.
DR   SMART; SM00060; FN3; 5.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
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:UP000018468};
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..1377
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004866893"
FT   TRANSMEM        1239..1260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          41..129
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          143..230
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          264..352
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          357..444
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          455..537
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          542..648
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          669..764
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          769..862
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          867..971
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          972..1071
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          652..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          751..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1271..1377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1271..1304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1305..1320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1348..1362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1363..1377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1377 AA;  154119 MW;  5E0FD08F385CD1D0 CRC64;
     MLTRGRRLSP TGLALLFLWT EVSTIEVPLD PKIQQDLKQP PTIIKQSVKD YIVDPRDNII
     IECEAKGNPL PVFSWRRNGR FFNVGKDPRV SMRKRSGTLE IGFRSGGRPE DYEGEYQCLA
     TNDYGTALSN KILLRVSKSP LWPKEVLEPV VVNEGSSLIL ACNPPPGLPP PSTFWMNSSM
     MPIVQDRRVS MGLNGDLYFS NVLAKDAQTD YSCNARFLFT HTIQQKNPFT LKVLTKEPYN
     DTSVFSSLNH TDFYSARGVA ETTPTFLSPT GTSSFKMVLR GQDLLLECIA AGVPTPSIKW
     FKKGGDLPAQ KAKFDNFNKT LRISGVSEED SGEYFCMANN KIGSIRHTVS VQVKAAPYWL
     DKPSNLVLAP DESGRLVCRA NGSPKPTIQW LVNGEPIQSA PPNPSREVVG DTIIFRSVQI
     GSSAVYQCNA SNGHGYLLAN AFVSILDMQP RMLGPKNQLI KVIENNRTFL DCPFFGSPLP
     ELRWFKNGQG SNLDGGQYRV YSNGTLEIRR TRPEDQGTYT CVATNILGNA ENQVRLEVKE
     STRIVRAPEH LTAVRGTVAR FDCRINYDPS LRLTISWLKD DVPVSLGWRN FIQIIGNWFK
     DVVAMFYPRM KKDEDSLAIH NVNEGDEGTY TCTASTELDS DSASARLTVL DDPLSPTNRS
     AVVPDRPDPP TDLELSDPSE RSVRLTWIPG DDNHSPITNF LVQFEEDRWE PNKWKNLSIY
     PGNLNSVLLQ LSPFINYQFR VIAINAIGAS RPSRPSQRYQ TSGAPPDAIP GQLRGAGTKK
     TNMEITWEAL LDTQRNGPNL RYVVWWRRQG SREEWKNITT KWLKHVIYDT DTYTPYDIKI
     QAVNDFGPGP ESPVITGYSG EDRPLAAPTN LRVSKIESMR VHLMWNSVPP STVQGEMKEY
     KVYYWRESSV LKWLTVNREK KTRSFQGTMS RPSGWLPNLI PYSNYKAYVV MANNRYEGPQ
     SNVVDFQTKE GVPSAPKYFR IQQRHMDTIY LDWDKPAEPN GILTGYTLKY QTVNGTRMGR
     MVTENFSPNV TSFSMRRPDR YTRYKFQLNA RTQAGAGEVY IEESPHSANE EDFAITVVTP
     TPSPADLVPT PTAATPTTSI SATPETTTVT APTAAPTTVV STVAATRPVP DRPVLVAPGR
     RIWNLTVEPN SNYANVSWEH NFPPDSTAFV IEFIDSNGTR KSVTVNHQTP VKLAGLTEGA
     KYELRVYSRE YETVSSKTVT FETSAAYTKD QVDIATQGWF IGLMCAIALL VLILLIVCFI
     KRSRGGKYPV RDKKDLPLDP VDQKDQDGSF DYRNENRSLE SDEDNKPLQG SQTSLDGMVK
     MQESDDSLVD YGEGGDGQFN EDGSFIGQYT VKKDKDETEG NESSEATSPV NAIYSLA
//
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