L1CAM_HUMAN » Neural cell adhesion molecule L1

L1CAM_HUMAN » Neural cell adhesion molecule L1
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
L1CAM_HUMAN » Neural cell adhesion molecule L1 » N-CAM-L1; NCAM-L1;
Hydrophobic Thickness 33.2 ± 1.8 Å
Tilt Angle 3 ± 1°
ΔGtransfer -42.3 kcal/mol
ΔGfold -26.8 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology Out
TM Segments 1119-1144 (1118-1147)
Pathways

Axon guidance (KEGG)

Cell adhesion molecules (KEGG)

Developmental Biology (Reactome)

Hemostasis (Reactome)

PDB none
OPM none
Complexes none
Interactions

APRIO, Complex: L1CAM:APRIO.PRIO, PubMed

CALX, Complex: CALX:L1CAM, PubMed

ITA5, Complex: ITA5:L1CAM, PubMed

ITAV, Complex: ITAV:L1CAM, PubMed

NCAM1, Complex: NCAM1:L1CAM, PubMed

NRP1, Complex: NRP1:L1CAM, PubMed

Domains

AA: 34-118, PDBID: 3P3Y, Subunit A, Seq Identity:34%, Immunoglobulin domain

AA: 239-316, PDBID: 3P3Y, Subunit A, Seq Identity:38%, Immunoglobulin domain

AA: 333-421, PDBID: 3LAF, Subunit A, Seq Identity:33%, Immunoglobulin I-set domain

AA: 428-514, PDBID: 2EDJ, Subunit A, Seq Identity:36%, Immunoglobulin I-set domain

AA: 519-595, PDBID: 1CS6, Subunit A, Seq Identity:32%, Immunoglobulin domain

AA: 613-701, PDBID: 1UEY, Subunit A, Seq Identity:33%, Fibronectin type III domain

AA: 716-800, PDBID: 1UEY, Subunit A, Seq Identity:48%, Fibronectin type III domain

AA: 813-907, PDBID: 1UEN, Subunit A, Seq Identity:38%, Fibronectin type III domain

AA: 919-1004, PDBID: 2X10, Subunit A, Seq Identity:31%, Fibronectin type III domain

AA: 1144-1233, Bravo-like intracellular region

UniProt annotation for L1CAM_HUMAN » Neural cell adhesion molecule L1
FUNCTION: 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.

DISEASE: Hydrocephalus due to stenosis of the aqueduct of Sylvius (HSAS) OMIM: Hydrocephalus is a condition in which abnormal accumulation of cerebrospinal fluid in the brain causes increased intracranial pressure inside the skull. This is usually due to blockage of cerebrospinal fluid outflow in the brain ventricles or in the subarachnoid space at the base of the brain. In children is typically characterized by enlargement of the head, prominence of the forehead, brain atrophy, mental deterioration, and convulsions. In adults the syndrome includes incontinence, imbalance, and dementia. HSAS is characterized by mental retardation and enlarged brain ventricles. disease is caused by mutations affecting the gene represented in this entry. L1CAM mutations have also been found in few patients affected by hydrocephalus with Hirschsprung disease, suggesting a role of this gene acting either in a direct or indirect way in the pathogenesis of Hirschsprung disease (PubMed).

DISEASE: Mental retardation, aphasia, shuffling gait, and adducted thumbs syndrome (MASA) OMIM: An X-linked recessive syndrome with a highly variable clinical spectrum. Main clinical features include spasticity and hyperreflexia of lower limbs, shuffling gait, mental retardation, aphasia and adducted thumbs. The features of spasticity have been referred to as complicated spastic paraplegia type 1 (SPG1). Some patients manifest corpus callosum hypoplasia and hydrocephalus. Inter- and intrafamilial variability is very wide, such that patients with hydrocephalus, MASA, SPG1, and agenesis of corpus callosum can be present within the same family. disease is caused by mutations affecting the gene represented in this entry.

DISEASE: Spastic paraplegia 1, X-linked (SPG1) OMIM: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. Note=The disease is caused by mutations affecting the gene represented in this entry.

DISEASE: Note=Defects in L1CAM may contribute to Hirschsprung disease by modifying the effects of Hirschsprung disease- associated genes to cause intestinal aganglionosis.

DISEASE: Agenesis of the corpus callosum, X-linked, partial (ACCPX) OMIM: A syndrome characterized by partial corpus callosum agenesis, hypoplasia of inferior vermis and cerebellum, mental retardation, seizures and spasticity. Other features include microcephaly, unusual facies, and Hirschsprung disease in some patients. caused by mutations affecting the gene represented in this entry.

UniProt features for L1CAM_HUMAN » Neural cell adhesion molecule L1
SIGNAL 1 19
CHAIN 20 1257 Neural cell adhesion molecule L1.
DOMAIN 35 125 Ig-like C2-type 1.
DOMAIN 139 226 Ig-like C2-type 2.
DOMAIN 240 328 Ig-like C2-type 3.
DOMAIN 333 420 Ig-like C2-type 4.
DOMAIN 425 507 Ig-like C2-type 5.
DOMAIN 518 607 Ig-like C2-type 6.
DOMAIN 612 707 Fibronectin type-III 1.
DOMAIN 714 807 Fibronectin type-III 2.
DOMAIN 812 913 Fibronectin type-III 3.
DOMAIN 914 1011 Fibronectin type-III 4.
DOMAIN 1016 1108 Fibronectin type-III 5.
MOTIF 554 556 Cell attachment site (Potential).
DISULFID 57 114 By similarity.
DISULFID 158 209 By similarity.
DISULFID 264 312 By similarity.
DISULFID 354 404 By similarity.
DISULFID 448 497 By similarity.
DISULFID 539 591 By similarity.
Amino Acid Sequence for L1CAM_HUMAN » Neural cell adhesion molecule L1
MVVALRYVWP LLLCSPCLLI QIPEEYEGHH VMEPPVITEQ SPRRLVVFPT DDISLKCEAS GKPEVQFRWT RDGVHFKPKE ELGVTVYQSP HSGSFTITGN NSNFAQRFQG IYRCFASNKL GTAMSHEIRL MAEGAPKWPK ETVKPVEVEE GESVVLPCNP PPSAEPLRIY WMNSKILHIK QDERVTMGQN GNLYFANVLT SDNHSDYICH AHFPGTRTII QKEPIDLRVK ATNSMIDRKP RLLFPTNSSS HLVALQGQPL VLECIAEGFP TPTIKWLRPS GPMPADRVTY QNHNKTLQLL KVGEEDDGEY RCLAENSLGS ARHAYYVTVE AAPYWLHKPQ SHLYGPGETA RLDCQVQGRP QPEVTWRING IPVEELAKDQ KYRIQRGALI LSNVQPSDTM VTQCEARNRH GLLLANAYIY VVQLPAKILT ADNQTYMAVQ GSTAYLLCKA FGAPVPSVQW LDEDGTTVLQ DERFFPYANG TLGIRDLQAN DTGRYFCLAA NDQNNVTIMA NLKVKDATQI TQGPRSTIEK KGSRVTFTCQ ASFDPSLQPS ITWRGDGRDL QELGDSDKYF IEDGRLVIHS LDYSDQGNYS CVASTELDVV ESRAQLLVVG SPGPVPRLVL SDLHLLTQSQ VRVSWSPAED HNAPIEKYDI EFEDKEMAPE KWYSLGKVPG NQTSTTLKLS PYVHYTFRVT AINKYGPGEP SPVSETVVTP EAAPEKNPVD VKGEGNETTN MVITWKPLRW MDWNAPQVQY RVQWRPQGTR GPWQEQIVSD PFLVVSNTST FVPYEIKVQA VNSQGKGPEP QVTIGYSGED YPQAIPELEG IEILNSSAVL VKWRPVDLAQ VKGHLRGYNV TYWREGSQRK HSKRHIHKDH VVVPANTTSV ILSGLRPYSS YHLEVQAFNG RGSGPASEFT FSTPEGVPGH PEALHLECQS NTSLLLRWQP PLSHNGVLTG YVLSYHPLDE GGKGQLSFNL RDPELRTHNL TDLSPHLRYR FQLQATTKEG PGEAIVREGG TMALSGISDF GNISATAGEN YSVVSWVPKE GQCNFRFHIL FKALGEEKGG ASLSPQYVSY NQSSYTQWDL QPDTDYEIHL FKERMFRHQM AVKTNGTGRV RLPPAGFATE GWFIGFVSAI ILLLLVLLIL CFIKRSKGGK YSVKDKEDTQ VDSEARPMKD ETFGEYRSLE SDNEEKAFGS SQPSLNGDIK PLGSDDSLAD YGGSVDVQFN EDGSFIGQYS GKKEKEAAGG NDSSGATSPI NPAVALE