ID L5KGT4_PTEAL Unreviewed; 1394 AA.
AC L5KGT4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Neural cell adhesion molecule L1 {ECO:0000313|EMBL:ELK09728.1};
GN ORFNames=PAL_GLEAN10001410 {ECO:0000313|EMBL:ELK09728.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK09728.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB030794; ELK09728.1; -; Genomic_DNA.
DR STRING; 9402.L5KGT4; -.
DR InParanoid; L5KGT4; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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; cd05876; Ig3_L1-CAM; 1.
DR CDD; cd05867; Ig4_L1-CAM_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; IPR026966; Neurofascin/L1/NrCAM_C.
DR PANTHER; PTHR44170:SF44; L1 CELL ADHESION MOLECULE; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF13927; Ig_3; 2.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 5.
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:UP000010552};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1394
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003969202"
FT TRANSMEM 1262..1284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..124
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 194..282
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 339..432
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 437..525
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 530..619
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 701..802
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 858..951
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 953..1057
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1061..1156
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 1294..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1394 AA; 154002 MW; 11EB277093926800 CRC64;
MAVALRYLWP LLLCSPCLLI QIPEELMEPP VITDQSPRRL VVFPTDDISL KCEATGKPEV
QFRWTRDGVH FKPKEELGVT VHQAPRSGSF TITGNNSNFA QRFQGTYRCF ASNKLGTAMS
HEIQLMAEEI LHIKQDERVT MGQNGNLYFA NVLTSDNHSD YICHAHFPGT RTIIQKEPID
LRVKATNSMI DRKPRLLFPT NASSHLVALQ GQPLVLECIA EGFPTPTIKW LRPSGHMPAD
RVTYQNHNKT LHLLDMGEED DGEYRCLAEN SLGSDRHTYY VTVEGMVSLL GATPALLQGS
PERPPGVAIC DAHCHGGAGG IWARGESWLQ AAGSGQLPPF LAAAPYWLHK PQSHLYGPGE
TARLDCQVQG RPKPEVTWRI NGIPVEELGK DQKYRIQHGA LTLSNVQPSD TMVTQCEARN
RHGVLLANAY IYVVQLPAKI LTPDNETYLA VEGSTAYLLC KAFGAPVPGV QWLDKEGKTV
LQDERFFPYT NGTLGIRDLQ ANDTGHYYCQ AANDQNNVTI VANLQVKDAT QITQGPQNAI
EKKGSRVTFT CQASFDPSLQ RSITWRRDGR NLQELGDSDK YFIEDGRLVI HSLDYSDQGN
YSCVASTKLD VVESKAELLV VGSPGPVPQL ELSGRHLLKQ SQVHLSWSPA DDHNSPIESK
RPGHDATHLP HCPFCQPSLL PGPWLHDCHL TGAHGSSCES ENANRLGHLR ESQACTLITS
PPYHTLITPS SIHFSAEYDI EFEDKEMAPE KWYSLGKVPG NQTSTTLKLS PYVHYTFRVT
AINKYGPGEP SPASETVVTP EAGLQRELRG RVPSGLLAPG FQGQKGPFFP SSSAFTASAG
AQSIDELTIH CFPAPEKNPV DVRGEGNETN NMVITWKPLR WMDWNAPHVQ YRVQWRPQGL
RGAWQEQIVN DPFLVVSNTS TFVPYEIKVQ AINSQGKGPE PQVTIGYSGE DYPQASPQLE
DVKILNSSTV LVKWWPLDPA QVKGHLRGYN VTYWWEGSQR KHSKRHVHKG HVVVPANTTS
TILGGLRPYS SYHLEVQAFN GRGLGPASKM TFSTPEGVPG HPEALHLECQ SNTSLLLHWQ
PPLSHNGVLT GYVLSYHSLD DGVMEQLSFN LSDPELRMHN LTNLSPHLRY RFQLQATTKE
GPGEAIVQEG GTMALSGTLD FGNISAMAGE NYSVVSWVPK EGQCNFGFQI SFKARGEEKM
GAYLPPQYVS YNQRSYTQWD LQPDTDYDIC LLKNTVLLHQ MAVKTNGTGR MRLPPPGFAT
EGWFIGFISA IILLLLILLI LCFIKRSKGG KYSVKDKEDT QVDSEARPMK DETFGEYSDN
EEKAFGSSQP SLNGDIKPLG SDDSLADYGG SVDVQFNEDG SFIGQYSGKK EKEAAGGNDS
SGAASPINPA GTLE
//
