L1CAM_TAKRU
ID L1CAM_TAKRU Reviewed; 1277 AA.
AC Q98902;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Neural cell adhesion molecule L1;
DE Short=N-CAM-L1;
DE Short=NCAM-L1;
DE AltName: Full=L1-CAM;
DE Flags: Precursor;
GN Name=l1cam;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain {ECO:0000269|PubMed:9479034}, and
RC Muscle {ECO:0000269|PubMed:9479034};
RX PubMed=9479034; DOI=10.1016/s0378-1119(97)00614-8;
RA Coutelle O., Nyakatura G., Taudien S., Elgar G., Brenner S., Platzer M.,
RA Drescher B., Jouet M., Kenwrick S., Rosenthal A.;
RT "The neural cell adhesion molecule L1: genomic organisation and
RT differential splicing is conserved between man and the pufferfish Fugu.";
RL Gene 208:7-15(1998).
CC -!- FUNCTION: Neural cell adhesion molecule involved in the dynamics of
CC cell adhesion and in the generation of transmembrane signals at
CC tyrosine kinase receptors. During brain development, critical in
CC multiple processes, including neuronal migration, axonal growth and
CC fasciculation, and synaptogenesis. In the mature brain, plays a role in
CC the dynamics of neuronal structure and function, including synaptic
CC plasticity. {ECO:0000250|UniProtKB:P32004}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q05695};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q05695}.
CC Cell projection, growth cone {ECO:0000250|UniProtKB:Q05695}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:9479034}; Synonyms=Brain
CC {ECO:0000269|PubMed:9479034};
CC IsoId=Q98902-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:9479034}; Synonyms=Muscle
CC {ECO:0000269|PubMed:9479034};
CC IsoId=Q98902-2; Sequence=VSP_050474, VSP_050475;
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000305}.
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DR EMBL; Z71926; CAA96469.1; -; Genomic_DNA.
DR EMBL; AF026198; AAC15580.1; -; Genomic_DNA.
DR PIR; T30532; T30532.
DR AlphaFoldDB; Q98902; -.
DR SMR; Q98902; -.
DR STRING; 31033.ENSTRUP00000036744; -.
DR PRIDE; Q98902; -.
DR eggNOG; KOG3513; Eukaryota.
DR InParanoid; Q98902; -.
DR Proteomes; UP000005226; Unplaced.
DR GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 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 Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 3: Inferred from homology;
KW Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..1277
FT /note="Neural cell adhesion molecule L1"
FT /id="PRO_0000015025"
FT TOPO_DOM 35..1135
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1136..1156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1157..1277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 51..140
FT /note="Ig-like C2-type 1"
FT DOMAIN 150..241
FT /note="Ig-like C2-type 2"
FT DOMAIN 256..344
FT /note="Ig-like C2-type 3"
FT DOMAIN 349..437
FT /note="Ig-like C2-type 4"
FT DOMAIN 443..528
FT /note="Ig-like C2-type 5"
FT DOMAIN 532..623
FT /note="Ig-like C2-type 6"
FT DOMAIN 630..725
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 730..824
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 829..931
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 935..1030
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1032..1129
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 714..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 794
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1035
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1046
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1068
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1083
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 173..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 280..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 370..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 465..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 554..607
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 42..47
FT /note="YYISDL -> F (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9479034"
FT /id="VSP_050474"
FT VAR_SEQ 1190..1193
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9479034"
FT /id="VSP_050475"
SQ SEQUENCE 1277 AA; 141955 MW; 284BB49BA9A42C27 CRC64;
MAHTQRQQGG SRGQWSRCLL LLLLLPLAAQ PGRAAIQIPS SYYISDLKIP PAITTQPESV
TVFSVEDLVM RCEASGNPSP TFHWTKDGEE FDPSSDPEMK VTEEAGSSVF YTLSNTMDTL
KQYQGKYICY ASNELGTAVS NAAVLMIDAP PVQQKEKKVT EKAEAGHSIA LSCNPPQSSM
QPIIHWMDNR LRHIRLSDRV MVGKDGNLYF ANLLTEDSRN DYTCNIQYLA TRTILAKEPI
TLTVNPSNLV PRNRRPQMMR PTGSHSTYHA LRGQTLELEC IVQGLPTPKV SWLRKDGEMS
ESRISKDMFD RRLQFTNISE SDGGEYQCTA ENVQGRTFHT YTVTVEASPY WTNAPVSQLY
APGETVKLDC QADGIPSPTI TWTVNGVPLS ATSLEPRRSL TESGSLILKD VIFGDTAIYQ
CQASNKHGTI LANTNVYVIE LPPQILTENG NTYTFVEGQK ALLECETFGS PKPKVTWESS
SISLLLADPR VNLLTNGGLE IANVSHDDEG IYTCLVQGSN ISVNAEVEVL NRTVILSPPQ
ALRLQPGKTA IFTCLYVTDP KLSSPLLQWR KNDQKIFESH SDKKYTFDGP GLIISNVEPG
DEGVYTCQII TKLDMVEASS TLTLCDRPDP PVHLQVTNAK HRVVTLNWTP GDDNNSPILE
YVVEFEDQDM KENGWEELKR VAADKKHVNL PLWPYMSYRF RVIAINDQGK SDPSKLSDLY
KTPADAPDSN PEDVRSESTD PDTLVITWEE MDKRNFNGPD FKYLVMWRRV VGSGPDWHEE
YTIAPPFIVT DVQNFSAFEI KVQAVNKKGL GPEPDPIIGY SGEDVPLEAP LNLGVLLENS
TTIRVTWSAV DKETVRGHLL GYKIYLTWGH HRNSRAQEPE NIVMVQTGAN EEKKSITNLR
PYCHYDLAIS AFNSKGEGPL SEKTSFMTPE GVPGPPMSMQ MTSPSESEIT LHWTPPSKPN
GILLGYSLQY RKMQSDDNPL QVVDIASPEI THLTLKGLDR HSHYQFLLMA RTAAGKGLSI
EILGATTLEG LPPANISLSA EERSVNLSWE ARKRHRTVGF QIHYFSKNGT KNGGKWKKTE
MVNSSLQFFQ LQGLTPGSHY RLLFTYKNNT FWETEIQTKG TSVTEVQPSF ATQGWFIGVV
SAVVLLLLVL LILCFIKRSK GGKYSVKDKE DGPMDSEARP MKDETFGEYR SLESDLEEKR
TASQPSLGED SKLCSEDNLD FNGSSAVTTE LNMDESLASQ FSRHSEGPEP FHGVPDNSPL
NPAANPPATN GAPSFLN
