Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-01295
Entry Name
UniProt Accession
Theoretical PI
5.55
Molecular Weight
140934.52
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Neural cell adhesion molecule L1
Protein Synonyms/Alias
N-CAM-L1; NCAM-L1; Nerve-growth factor-inducible large external glycoprotein; NILE; CD171;
Gene Name
L1cam
Gene Synonyms/Alias
Caml1;
Created Date
01-FEB-1994
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
14
Canonical
YVLPLLLCSPCLLIQ
[1]
S-Palmitoylation
17
Canonical
PLLLCSPCLLIQIPD
[1]
S-Palmitoylation
1143
Canonical
LLILLILCFIKRSKG
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Predicted from GPS-Lipid
Functional Description
Cell adhesion molecule with an important role in the development of the nervous system. Involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc. Binds to axonin on neurons.
Sequence Annotation
Topological domain: 20 1122 Extracellular.
Transmembrane: 1123 1145 Helical.
Topological domain: 1146 1259 Cytoplasmic.
Domain: 35 128 Ig-like C2-type 1.
Domain: 138 225 Ig-like C2-type 2.
Domain: 239 327 Ig-like C2-type 3.
Domain: 332 419 Ig-like C2-type 4.
Domain: 424 506 Ig-like C2-type 5.
Domain: 517 600 Ig-like C2-type 6.
Domain: 613 711 Fibronectin type-III 1.
Domain: 716 809 Fibronectin type-III 2.
Domain: 811 916 Fibronectin type-III 3.
Domain: 919 1014 Fibronectin type-III 4.
Domain: 1016 1116 Fibronectin type-III 5.
Motif: 553 555 Cell attachment site.
Motif: 562 564 Cell attachment site.
Modified residue: 1165 1165 Phosphoserine.
Modified residue: 1183 1183 Phosphoserine; by CaMK2.
Modified residue: 1196 1196 Phosphoserine.
Modified residue: 1250 1250 Phosphoserine.
Protein Length
1259 AA.
Protein Sequence
(Canonical)
MVMMLWYVLP LLLCSPCLLI QIPDEYKGHH VLEPPVITEQ SPRRLVVFPT DDISLKCEAR  60
GRPQVEFRWT KDGIHFKPKE ELGVVVHEAP YSGSFTIEGN NSFAQRFQGI YRCYASNNLG  120
TAMSHEIQLV AEGAPKWPKE TVKPVEVEEG ESVVLPCNPP PSAAPLRIYW MNSKILHIKQ  180
DERVSMGQNG DLYFANVLTS DNHSDYICNA HFPGTRTIIQ KEPIDLRVKP TNSMIDRKPR  240
LLFPTNSSSH LVALQGQSLI LECIAEGFPT PTIKWLHPSD PMPTDRVIYQ NHNKTLQLLN  300
VGEEDDGEYT CLAENSLGSA RHAYYVTVEA APYWLQKPQS HLYGPGETAR LDCQVQGRPQ  360
PEVTWRINGM SIEKVNKDQK YRIEQGSLIL SNVQPSDTMV TQCEARNQHG LLLANAYIYV  420
VQLPARILTK DNQTYMAVEG STAYLLCKAF GAPVPSVQWL DEEGTTVLQD ERFFPYANGH  480
LGIRDLQAND TGRYFCQAAN DQNNVTILAN LQVKEATQIT QGPRSTIEKK GARVTFTCQA  540
SFDPSLQASI TWRGDGRDLQ ERGDSDKYFI EDGQLVIKSL DYSDQGDYSC VASTELDEVE  600
SRAQLLVVGS PGPVPHLELS DRHLLKQSQV HLSWSPAEDH NSPIEKYDIE FEDKEMAPEK  660
WFSLGKVPGN QTSTTLKLSP YVHYTFRVTA INKYGPGEPS PVSETVVTPE AAPEKNPVDV  720
RGEGNETNNM VITWKPLRWM DWNAPQIQYR VQWRPLGKQE TWKEQTVSDP FLVVSNTSTF  780
VPYEIKVQAV NNQGKGPEPQ VTIGYSGEDY PQVSPELEDI TIFNSSTVLV RWRPVDLAQV  840
KGHLRGYNVT YWWKGSQRKH SKRHVHKSHM VVPANTTSAI LSGLRPYSSY HVEVQAFNGR  900
GLGPASEWTF STPEGVPGHP EALHLECQSD TSLLLHWQPP LSHNGVLTGY LLSYHPLDGE  960
SKEQLFFNLS DPELRTHNLT NLNPDLQYRF QLQATTHQGP GEAIVREGGT MALFGKPDFG  1020
NISVTAGENY SVVSWVPREG QCNFRFHILF KALPEGKVSP DHQPQPQYVS YNQSSYTQWD  1080
LQPDTKYEIH LMREKVLLHH LAVKTNGTGP VRVSTTGSFA SEGWFIAFVS AIILLLLILL  1140
ILCFIKRSKG GKYSVKDKED TQVDSEARPM KDETFGEYRS LESDNEEKAF GSSQPSLNGD  1200
IKPLGSDDSL ADYGGSVDVQ FNEDGSFIGQ YSGKKEKEAA GGNDSSGATS PINPAVALE   1259
FASTA
(Canonical)
>LipidDB-10116-01295|Q05695
MVMMLWYVLPLLLCSPCLLIQIPDEYKGHHVLEPPVITEQSPRRLVVFPTDDISLKCEAR
GRPQVEFRWTKDGIHFKPKEELGVVVHEAPYSGSFTIEGNNSFAQRFQGIYRCYASNNLG
TAMSHEIQLVAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAAPLRIYWMNSKILHIKQ
DERVSMGQNGDLYFANVLTSDNHSDYICNAHFPGTRTIIQKEPIDLRVKPTNSMIDRKPR
LLFPTNSSSHLVALQGQSLILECIAEGFPTPTIKWLHPSDPMPTDRVIYQNHNKTLQLLN
VGEEDDGEYTCLAENSLGSARHAYYVTVEAAPYWLQKPQSHLYGPGETARLDCQVQGRPQ
PEVTWRINGMSIEKVNKDQKYRIEQGSLILSNVQPSDTMVTQCEARNQHGLLLANAYIYV
VQLPARILTKDNQTYMAVEGSTAYLLCKAFGAPVPSVQWLDEEGTTVLQDERFFPYANGH
LGIRDLQANDTGRYFCQAANDQNNVTILANLQVKEATQITQGPRSTIEKKGARVTFTCQA
SFDPSLQASITWRGDGRDLQERGDSDKYFIEDGQLVIKSLDYSDQGDYSCVASTELDEVE
SRAQLLVVGSPGPVPHLELSDRHLLKQSQVHLSWSPAEDHNSPIEKYDIEFEDKEMAPEK
WFSLGKVPGNQTSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETVVTPEAAPEKNPVDV
RGEGNETNNMVITWKPLRWMDWNAPQIQYRVQWRPLGKQETWKEQTVSDPFLVVSNTSTF
VPYEIKVQAVNNQGKGPEPQVTIGYSGEDYPQVSPELEDITIFNSSTVLVRWRPVDLAQV
KGHLRGYNVTYWWKGSQRKHSKRHVHKSHMVVPANTTSAILSGLRPYSSYHVEVQAFNGR
GLGPASEWTFSTPEGVPGHPEALHLECQSDTSLLLHWQPPLSHNGVLTGYLLSYHPLDGE
SKEQLFFNLSDPELRTHNLTNLNPDLQYRFQLQATTHQGPGEAIVREGGTMALFGKPDFG
NISVTAGENYSVVSWVPREGQCNFRFHILFKALPEGKVSPDHQPQPQYVSYNQSSYTQWD
LQPDTKYEIHLMREKVLLHHLAVKTNGTGPVRVSTTGSFASEGWFIAFVSAIILLLLILL
ILCFIKRSKGGKYSVKDKEDTQVDSEARPMKDETFGEYRSLESDNEEKAFGSSQPSLNGD
IKPLGSDDSLADYGGSVDVQFNEDGSFIGQYSGKKEKEAAGGNDSSGATSPINPAVALE
Gene Ontology
GO:0005768; C:endosome; TAS:Reactome
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0045121; C:membrane raft; IDA:RGD
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0030165; F:PDZ domain binding; IPI:RGD
GO:0007155; P:cell adhesion; IEA:UniProtKB-KW
GO:0030154; P:cell differentiation; IEA:UniProtKB-KW
GO:0071361; P:cellular response to ethanol; IEP:RGD
GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD
GO:0007399; P:nervous system development; IEA:UniProtKB-KW
Interpro
InterPro; IPR003961; Fibronectin_type3
InterPro; IPR007110; Ig-like_dom
InterPro; IPR013783; Ig-like_fold
InterPro; IPR013098; Ig_I-set
InterPro; IPR003599; Ig_sub
InterPro; IPR003598; Ig_sub2
InterPro; IPR026966; Neurofascin/L1/NrCAM_C
Pfam
Pfam; PF13882; Bravo_FIGEY;
Pfam; PF00041; fn3;
Pfam; PF07679; I-set;
SMART
SMART; SM00060; FN3;
SMART; SM00409; IG;
SMART; SM00408; IGc2;
PROSITE
PROSITE; PS50853; FN3;
PROSITE; PS50835; IG_LIKE;
PRINTS