ID G1PPL6_MYOLU Unreviewed; 1257 AA.
AC G1PPL6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=L1 cell adhesion molecule {ECO:0000313|Ensembl:ENSMLUP00000012960.2};
GN Name=L1CAM {ECO:0000313|Ensembl:ENSMLUP00000012960.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000012960.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000012960.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000012960.2}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAPE02015462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_014310351.1; XM_014454865.1.
DR RefSeq; XP_014310352.1; XM_014454866.1.
DR RefSeq; XP_014310353.1; XM_014454867.1.
DR AlphaFoldDB; G1PPL6; -.
DR STRING; 59463.ENSMLUP00000012960; -.
DR Ensembl; ENSMLUT00000014248.2; ENSMLUP00000012960.2; ENSMLUG00000014234.2.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000157506; -.
DR HOGENOM; CLU_005756_1_1_1; -.
DR InParanoid; G1PPL6; -.
DR OMA; GARTIIQ; -.
DR TreeFam; TF351098; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR CDD; cd00063; FN3; 5.
DR CDD; cd05876; Ig3_L1-CAM; 1.
DR CDD; cd05867; Ig4_L1-CAM_like; 1.
DR CDD; cd05845; IgI_2_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; 4.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF13927; Ig_3; 2.
DR SMART; SM00060; FN3; 4.
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:UP000001074};
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..1257
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003418481"
FT TRANSMEM 1122..1144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..129
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 139..226
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 240..328
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 333..421
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 426..514
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 519..608
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 615..713
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 718..811
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 813..919
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 922..1018
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 697..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1257 AA; 140138 MW; 628552B7066EA69E CRC64;
MAVALRYLWP LLLCSPCLFI QIPDEYEGQH VMEPPVITEQ SPRRLVVFPT DEISLKCEAS
GKPEVMFRWS RDGIHFNPNE ELDVTVKQAP HSGSFTIAGN NSNFAQRFQG TYRCFASNDL
GTAMSHEIQL MAEGAPKWPK ETVKPVEVEE GESVILPCHP PPSAEPLRIY WMNSKIMHIK
QDERVTMGQN GNLYFANVLT SDNHSDYICH AHFPGTRTII QKEPIDLRVK ATNSMIDRKP
RLLFPTNASS HLVALQGQPL VLECIAEGFP TPTIKWLRPS GPMPADRVTY QNHNKTLHLL
NVGEEDDGEY RCVAENSLGS DRHAYYVTVE AAPYWLHKPQ SRLYGPGETA RLDCQVQGRP
EPEVTWRING IPVEELLAKD QKYRIQHGAL ILSNVQPSDT MVTQCEARNR HGLLLANAYI
YVVQLPAKIL TPDNETYLAV EGSTAYLLCK VFGAPVPSVQ WLDKEGKTVL QDERFFPYTN
GTLGIRDLQA NDTGHYFCQA ANDQNNVTIV ANLQVKDATR ITQGPQSTIK KKGSRVTFTC
QATFDPSLQQ SITWRRDGRS LQEPGDSDKY FIEDGHLVIH SLDYSDQGNY SCVASTKLDV
VESRAELQVV GSPGPVPQLE LSDRHLLKQS QVRLSWSPAD DHNAPIEKYD IEFEDKEMAP
EKWYSLGKVP GNQTSTTLKL SPYVHYTFRV TAINKYGPGE PSPASETVVT PEAAPEKNPV
DVKGEGNETN NMVITWKPLK WMDWNAPQVQ YRVQWRPQGT RGAWQEQIVS DPFLVVSNTS
TFVPYEIKVQ TINSQGKGPE PQVTIGYSGE DYPQAKPKLE DIKILNASTV LVKWWPVDPA
QVKGHLRGYN LTYSWEGSPR RHSKRHIPES HVVVVPANTT STVLDGLRPY SSYHLELRAF
NSRGLGPPSK TTFSTPEGVP GPPEALHLEC QSDTSLLLHW QPPFSHNGVL TGYVLSCLPL
GDGGEEQLSF NLSDPELRSY NLTNLSPHLQ YRFQLQATTK QGPGEAITRE GGTKTLTGTS
DFGDVSTTVG ENYSVVSWVP KEGQCNFGFQ ILFKPLSDEK MDAIPPQYVS YNQRSYTQWD
LQPGTNYQIQ LLKEAVLLHE TFVTTNGTGR VRLPPPGFTT EGWFIGFVSA IILLLLILLI
LCFIKRSKGG KYSVKDKEDT QVDSEARPMK DETFGEYRSL ESDNEEKAFS SQPSLNGNIK
TLGSDDSLAD YGGSVDVQFN EDGSFIGQYS GKKEKEAAGG NDSSGAASPI NPTGTLE
//
