P70232 (CHL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neural cell adhesion molecule L1-like protein

Alternative name(s):
Cell adhesion molecule with homology to L1CAM
Chl1-like protein
Close homolog of L1

Cleaved into the following chain:

1. Processed neural cell adhesion molecule L1-like protein

Gene names

Name:	Chl1
Synonyms:	Call

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1209 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. Both soluble and membranous forms promote neurite outgrowth of cerebellar and hippocampal neurons and suppress neuronal cell death. Plays a role in neuronal positioning of pyramidal neurons as well as in regulation of both the number of interneurons and the efficacy of GABAergic synapses. May play a role in regulating cell migration in nerve regeneration and cortical development. Potentiates integrin-dependent cell migration towards extracellular matrix proteins. Recruits ANK3 to the plasma membrane. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Subunit structure	May interact with L1CAM. May interact with ITGB1/ITGA1 heterodimer and ITGB1/ITGA2 heterodimer as well as with ANK3.
Subcellular location	Cell membrane; Single-pass type I membrane protein. Note: Soluble forms produced by cleavage/shedding also exist. Processed neural cell adhesion molecule L1-like protein: Secreted › extracellular space › extracellular matrix.
Tissue specificity	Expressed in the brain, in the cerebellum and in the spinal cord. Detected in the retina and the optic nerve. Expressed in neurons and glial cells in the central nervous system and by Schwann cells in the peripheral nervous system. Ref.1 Ref.7 Ref.13
Developmental stage	Not detectable in the forebrain at E11, weakly detectable at E13 with highest detection at E18 to postnatal day 7. Down-regulated at postnatal day 15 and further reduced in four-week-old animals. Ref.1 Ref.7 Ref.13
Domain	The FIG[AQ]Y motif seems to be an ankyrin recruitment region. The DGEA motif seems to be a recognition site for integrin.
Post-translational modification	Cleavage by metalloprotease ADAM8 in the extracellular part generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is inhibited by metalloprotease inhibitors. In brain extracts, these two soluble forms are also present and are dramatically reduced in mice lacking ADAM8. N-glycosylated. Contains N-linked oligosaccharides with a sulfated carbohydrate structure type HNK-1 (SO4-3-GlcUABeta1,3GalBeta1,4GlcNAc). Ref.1 O-glycosylated. Ref.1
Disruption phenotype	Mice exhibit misguided axonal projections and aberrant axonal connectivity. They show alterations of hippocampal fiber organization and olfactory axon projections. Their exploratory behavior in novel environments is altered suggesting deficits in information processing and in attention. They also display signs of decreased stress and are more sociable and less aggressive. Heterozygous mice exhibit half levels of CHL1 expression in the hippocampus compared to their wild-type littermates, reflecting a gene dosage effect. Ref.6 Ref.9 Ref.10 Ref.14
Sequence similarities	Belongs to the immunoglobulin superfamily. L1/neurofascin/NgCAM family. Contains 4 fibronectin type-III domains. Contains 6 Ig-like C2-type (immunoglobulin-like) domains.
Sequence caution	The sequence BAC30699.1 differs from that shown. Reason: Frameshift at positions 616, 624, 631, 632, 642 and 645.

Ontologies

Keywords
Biological process	Cell adhesion Differentiation Neurogenesis
Cellular component	Cell membrane Extracellular matrix Membrane Secreted
Coding sequence diversity	Alternative splicing
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult locomotory behavior Inferred from mutant phenotype Ref.9. Source: MGI axon guidance Inferred from mutant phenotype Ref.6. Source: MGI cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cognition Inferred from mutant phenotype Ref.9. Source: MGI negative regulation of neuron apoptotic process Inferred from direct assay Ref.12. Source: BHF-UCL neuron migration Inferred from mutant phenotype Ref.13. Source: MGI
Cellular_component	apical part of cell Inferred from direct assay Ref.13. Source: MGI dendrite Inferred from direct assay Ref.13. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement. Source: Reactome proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P70232-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P70232-2)

The sequence of this isoform differs from the canonical sequence as follows:
     227-227: S → LKHASDSSSSTEICSQA
     1016-1070: SKGIRKITEGVNVTQKIHPVEVLVPGAEHIVHLMTKNWGDNDSIFQDVIETRGRE → K
     1138-1209: SDSDEKPLKG...SSTATFPLRA → RKMVLKQKLL...LRYFSSNKHT

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 1209	1184	Neural cell adhesion molecule L1-like protein		PRO_0000247897
	Chain	26 – ?		Processed neural cell adhesion molecule L1-like protein Potential		PRO_0000314778
Regions
	Topological domain	26 – 1083	1058	Extracellular Potential
	Transmembrane	1084 – 1104	21	Helical; Potential
	Topological domain	1105 – 1209	105	Cytoplasmic Potential
	Domain	35 – 124	90	Ig-like C2-type 1
	Domain	128 – 223	96	Ig-like C2-type 2
	Domain	235 – 328	94	Ig-like C2-type 3
	Domain	331 – 417	87	Ig-like C2-type 4
	Domain	423 – 510	88	Ig-like C2-type 5
	Domain	515 – 607	93	Ig-like C2-type 6
	Domain	611 – 707	97	Fibronectin type-III 1
	Domain	711 – 804	94	Fibronectin type-III 2
	Domain	809 – 911	103	Fibronectin type-III 3
	Domain	916 – 1011	96	Fibronectin type-III 4
	Motif	555 – 558	4	DGEA
	Motif	1182 – 1186	5	FIG[AQ]Y
Sites
	Site	753 – 754	2	Cleavage; by ADAM8
	Site	1040 – 1041	2	Cleavage; by ADAM8
Amino acid modifications
	Modified residue	1128	1	Phosphoserine Ref.15
	Modified residue	1148	1	Phosphoserine Ref.15
	Glycosylation	87	1	N-linked (GlcNAc...) Potential
	Glycosylation	225	1	N-linked (GlcNAc...) Potential
	Glycosylation	299	1	N-linked (GlcNAc...) Potential
	Glycosylation	476	1	N-linked (GlcNAc...) Potential
	Glycosylation	562	1	N-linked (GlcNAc...) Potential
	Glycosylation	580	1	N-linked (GlcNAc...) Potential
	Glycosylation	767	1	N-linked (GlcNAc...) Potential
	Glycosylation	822	1	N-linked (GlcNAc...) Potential
	Glycosylation	945	1	N-linked (GlcNAc...) Potential
	Glycosylation	1027	1	N-linked (GlcNAc...) Potential
	Disulfide bond	57 ↔ 109		By similarity
	Disulfide bond	153 ↔ 204		By similarity
	Disulfide bond	262 ↔ 310		By similarity
	Disulfide bond	352 ↔ 401		By similarity
	Disulfide bond	445 ↔ 494		By similarity
	Disulfide bond	536 ↔ 591		By similarity
Natural variations
	Alternative sequence	227	1	S → LKHASDSSSSTEICSQA in isoform 2.		VSP_020083
	Alternative sequence	1016 – 1070	55	SKGIR…TRGRE → K in isoform 2.		VSP_020084
	Alternative sequence	1138 – 1209	72	SDSDE…FPLRA → RKMVLKQKLLSWSSSRGRTF YSCTKNTLFDGSSVDMKTLQ PLRYFSSNKHT in isoform 2.		VSP_020085
Experimental info
	Mutagenesis	555 – 558	4	DGEA → AGEV: Inhibition of migration potentiation. Ref.11
	Mutagenesis	1186	1	Y → A: Inhibition of migration potentiation. Ref.11
	Sequence conflict	50	1	D → G in BAC35247. Ref.2
	Sequence conflict	77	1	D → E in CAC88131. Ref.6
	Sequence conflict	425	1	I → V in BAC35247. Ref.2
	Sequence conflict	602	1	E → K in CAA63972. Ref.1
	Sequence conflict	612	1	P → G in CAA63972. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 3, 2012. Version 2. Checksum: 2C689475920AB84C	FASTA	1,209	135,074
	10 20 30 40 50 60 MMELPLCGRG LILSLIFLLL KLSAAEIPLS VQQVPTIVKQ SYVQVAFPFD EYFQIECEAK 70 80 90 100 110 120 GNPEPIFSWT KDDKPFDLSD PRIIAANNSG TFKIPNEGHI SHFQGKYRCF ASNRLGTAVS 130 140 150 160 170 180 EEIEFIVPGV PKFPKEKIEP IDVEEGDSIV LPCNPPKGLP PLHIYWMNIE LEHIEQDERV 190 200 210 220 230 240 YMSQRGDLYF ANVEENDSRN DYCCFAAFPK LRTIVQKMPM KLTVNSSNSI KQRKPKLLLP 250 260 270 280 290 300 PAQMGSLSAK TVLKGDTLLL ECFAEGLPTP HIQWSKPGSE LPEGRATIEV HEKTLKIENI 310 320 330 340 350 360 SYQDRGNYRC TANNLLGKAS HDFHVTVEEP PRWKKKPQSA VYSTGSSGIL LCEAEGEPQP 370 380 390 400 410 420 TIKWRLNGLP IEKHPFPGDF MFPREISFTN LLPNHTGVYQ CEASNIHGTI LANANIDVID 430 440 450 460 470 480 VIPLIKTKNE ENYATVVGYS AFLHCEYFAS PKATVVWEVA DETHPLEGDR YHTHENGTLE 490 500 510 520 530 540 IYRTTEEDAG SYSCWVDNAM GKAVITANLD IRNATKLRVS PKNPRIPKSH VLELYCESQC 550 560 570 580 590 600 DSHLKHSLKL SWSKDGEAFE MNGTEDGRIV IDGAYLTISN ITAEDQGVYS CSAQTSLDST 610 620 630 640 650 660 SEKTQVTVLG VPDPPGNLHL SERQNRSVRL SWEAGDDHNS KISEYIVEFE GNREEPGKWE 670 680 690 700 710 720 ELTRVQGEET DVVLSLAPYV RYQFRVTAVN EVGRSHASLP SDHHETPPAA PDKNPQNIRV 730 740 750 760 770 780 QASQPKEMII KWEPLKSMEQ NGPGLEYKVS WKPQGAPEEW EEEIVTNHTL RVMTPTVYAP 790 800 810 820 830 840 YDVKVQAINQ LGSSPDPQPV TLYSGEDYPS TAPVIQRVDV MNSTLVKVTW SSIPKETVHG 850 860 870 880 890 900 LLRGYQINWW KTKSLLDGRT HPKEVNILRF SGQRNSGMVP SLDPFSEFHL TVLAYNSKGA 910 920 930 940 950 960 GPESEPYIFQ TPEGVPEQPS FLKVIKVDKD TATLSWGLPK KLNGNLTGYL LQYQIINDTY 970 980 990 1000 1010 1020 ELGELNEINV TTPSKSSWHL SNLNSTTKYK FYLRACTSRG CGKPISEEGA TLGEGSKGIR 1030 1040 1050 1060 1070 1080 KITEGVNVTQ KIHPVEVLVP GAEHIVHLMT KNWGDNDSIF QDVIETRGRE YAGLYDDIST 1090 1100 1110 1120 1130 1140 QGWFIGLMCA IALLTLILLT ICFVKRNRGG KYSVKEKEDL HPDPEVQSAK DETFGEYSDS 1150 1160 1170 1180 1190 1200 DEKPLKGSLR SLNRNMQPTE SADSLVEYGE GDQSIFNEDG SFIGAYTGAK EKGSVESNGS STATFPLRA
	Isoform 2 [UniParc]. Checksum: 6CF6C082529C7A99	FASTA	1,150	129,001
	10 20 30 40 50 60 MMELPLCGRG LILSLIFLLL KLSAAEIPLS VQQVPTIVKQ SYVQVAFPFD EYFQIECEAK 70 80 90 100 110 120 GNPEPIFSWT KDDKPFDLSD PRIIAANNSG TFKIPNEGHI SHFQGKYRCF ASNRLGTAVS 130 140 150 160 170 180 EEIEFIVPGV PKFPKEKIEP IDVEEGDSIV LPCNPPKGLP PLHIYWMNIE LEHIEQDERV 190 200 210 220 230 240 YMSQRGDLYF ANVEENDSRN DYCCFAAFPK LRTIVQKMPM KLTVNSLKHA SDSSSSTEIC 250 260 270 280 290 300 SQANSIKQRK PKLLLPPAQM GSLSAKTVLK GDTLLLECFA EGLPTPHIQW SKPGSELPEG 310 320 330 340 350 360 RATIEVHEKT LKIENISYQD RGNYRCTANN LLGKASHDFH VTVEEPPRWK KKPQSAVYST 370 380 390 400 410 420 GSSGILLCEA EGEPQPTIKW RLNGLPIEKH PFPGDFMFPR EISFTNLLPN HTGVYQCEAS 430 440 450 460 470 480 NIHGTILANA NIDVIDVIPL IKTKNEENYA TVVGYSAFLH CEYFASPKAT VVWEVADETH 490 500 510 520 530 540 PLEGDRYHTH ENGTLEIYRT TEEDAGSYSC WVDNAMGKAV ITANLDIRNA TKLRVSPKNP 550 560 570 580 590 600 RIPKSHVLEL YCESQCDSHL KHSLKLSWSK DGEAFEMNGT EDGRIVIDGA YLTISNITAE 610 620 630 640 650 660 DQGVYSCSAQ TSLDSTSEKT QVTVLGVPDP PGNLHLSERQ NRSVRLSWEA GDDHNSKISE 670 680 690 700 710 720 YIVEFEGNRE EPGKWEELTR VQGEETDVVL SLAPYVRYQF RVTAVNEVGR SHASLPSDHH 730 740 750 760 770 780 ETPPAAPDKN PQNIRVQASQ PKEMIIKWEP LKSMEQNGPG LEYKVSWKPQ GAPEEWEEEI 790 800 810 820 830 840 VTNHTLRVMT PTVYAPYDVK VQAINQLGSS PDPQPVTLYS GEDYPSTAPV IQRVDVMNST 850 860 870 880 890 900 LVKVTWSSIP KETVHGLLRG YQINWWKTKS LLDGRTHPKE VNILRFSGQR NSGMVPSLDP 910 920 930 940 950 960 FSEFHLTVLA YNSKGAGPES EPYIFQTPEG VPEQPSFLKV IKVDKDTATL SWGLPKKLNG 970 980 990 1000 1010 1020 NLTGYLLQYQ IINDTYELGE LNEINVTTPS KSSWHLSNLN STTKYKFYLR ACTSRGCGKP 1030 1040 1050 1060 1070 1080 ISEEGATLGE GKYAGLYDDI STQGWFIGLM CAIALLTLIL LTICFVKRNR GGKYSVKEKE 1090 1100 1110 1120 1130 1140 DLHPDPEVQS AKDETFGEYR KMVLKQKLLS WSSSRGRTFY SCTKNTLFDG SSVDMKTLQP 1150 LRYFSSNKHT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural features of a close homologue of L1 (CHL1) in the mouse: a new member of the L1 family of neural recognition molecules." Holm J., Hillenbrand R., Steuber V., Bartsch U., Moos M., Luebbert H., Montag D., Schachner M. Eur. J. Neurosci. 8:1613-1629(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, GLYCOSYLATION, DEVELOPMENTAL STAGE.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-425 AND 666-1209 (ISOFORM 1). Strain: C57BL/6J. Tissue: Aorta, Head and Vein.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Misguided axonal projections, neural cell adhesion molecule 180 mRNA upregulation, and altered behavior in mice deficient for the close homolog of L1." Montag-Sallaz M., Schachner M., Montag D. Mol. Cell. Biol. 22:7967-7981(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129, FUNCTION, DISRUPTION PHENOTYPE. Strain: 129/Sv.
[7]	"The close homologue of the neural adhesion molecule L1 (CHL1): patterns of expression and promotion of neurite outgrowth by heterophilic interactions." Hillenbrand R., Molthagen M., Montag D., Schachner M. Eur. J. Neurosci. 11:813-826(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH L1CAM, TISSUE SPECIFICITY.
[8]	"Prevention of neuronal cell death by neural adhesion molecules L1 and CHL1." Chen S., Mantei N., Dong L., Schachner M. J. Neurobiol. 38:428-439(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Mice deficient for the close homologue of the neural adhesion cell L1 (CHL1) display alterations in emotional reactivity and motor coordination." Pratte M., Rougon G., Schachner M., Jamon M. Behav. Brain Res. 147:31-39(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[10]	"CALL interrupted in a patient with non-specific mental retardation: gene dosage-dependent alteration of murine brain development and behavior." Frints S.G.M., Marynen P., Hartmann D., Fryns J.-P., Steyaert J., Schachner M., Rolf B., Craessaerts K., Snellinx A., Hollanders K., D'Hooge R., De Deyn P.P., Froyen G. Hum. Mol. Genet. 12:1463-1474(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[11]	"Close homolog of L1 is an enhancer of integrin-mediated cell migration." Buhusi M., Midkiff B.R., Gates A.M., Richter M., Schachner M., Maness P.F. J. Biol. Chem. 278:25024-25031(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ANK3; ITGB1/ITGA1 HETERODIMER AND ITGB1/ITGA2 HETERODIMER, MOTIFS, MUTAGENESIS OF 555-ASP--ALA-558 AND TYR-1186.
[12]	"Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death." Naus S., Richter M., Wildeboer D., Moss M., Schachner M., Bartsch J.W. J. Biol. Chem. 279:16083-16090(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CLEAVAGE BY ADAM8.
[13]	"Close homolog of L1 modulates area-specific neuronal positioning and dendrite orientation in the cerebral cortex." Demyanenko G.P., Schachner M., Anton E., Schmid R., Feng G., Sanes J., Maness P.F. Neuron 44:423-437(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[14]	"Enhanced perisomatic inhibition and impaired long-term potentiation in the CA1 region of juvenile CHL1-deficient mice." Nikonenko A.G., Sun M., Lepsveridze E., Apostolova I., Petrova I., Irintchev A., Dityatev A., Schachner M. Eur. J. Neurosci. 23:1839-1852(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[15]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1128 AND SER-1148, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X94310 mRNA. Translation: CAA63972.1. AK040765 mRNA. Translation: BAC30699.1. Frameshift. AK048639 mRNA. Translation: BAC33405.1. AK053039 mRNA. Translation: BAC35247.2. AC153595 Genomic DNA. No translation available. AC153598 Genomic DNA. No translation available. AC161824 Genomic DNA. No translation available. CH466523 Genomic DNA. Translation: EDK99388.1. BC131670 mRNA. Translation: AAI31671.1. BC131671 mRNA. Translation: AAI31672.1. AJ319655, AJ319656, AJ319657 Genomic DNA. Translation: CAC88131.1.
IPI	IPI00222149. IPI00404529. IPI00831546.
PIR	T42718.
RefSeq	NP_031723.2. NM_007697.2.
UniGene	Mm.251288.
3D structure databases
ProteinModelPortal	P70232.
SMR	P70232. Positions 31-1002.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4106227.
PTM databases
PhosphoSite	P70232.
Proteomic databases
PaxDb	P70232.
PRIDE	P70232.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000066905; ENSMUSP00000063933; ENSMUSG00000030077.
GeneID	12661.
KEGG	mmu:12661.
Organism-specific databases
CTD	10752.
MGI	MGI:1098266. Chl1.
Phylogenomic databases
eggNOG	NOG256023.
GeneTree	ENSGT00690000101868.
HOGENOM	HOG000231380.
HOVERGEN	HBG000144.
KO	K06758.
OMA	WEAGDDH.
OrthoDB	EOG4RFKRR.
Enzyme and pathway databases
Reactome	REACT_127416. Developmental Biology.
Gene expression databases
CleanEx	MM_CHL1.
Genevestigator	P70232.
GermOnline	ENSMUSG00000030077. Mus musculus.
Family and domain databases
Gene3D	2.60.40.10. 10 hits.
InterPro	IPR026966. Fibronectin_III_C. IPR003961. Fibronectin_type3. IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. IPR013098. Ig_I-set. IPR003599. Ig_sub. IPR003598. Ig_sub2. [Graphical view]
Pfam	PF13882. Bravo_FIGEY. 1 hit. PF00041. fn3. 4 hits. PF07679. I-set. 4 hits. [Graphical view]
SMART	SM00060. FN3. 4 hits. SM00409. IG. 2 hits. SM00408. IGc2. 3 hits. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 4 hits.
PROSITE	PS50853. FN3. 4 hits. PS50835. IG_LIKE. 6 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	281890.
SOURCE	Search...

Entry information

Entry name

CHL1_MOUSE

Accession

Primary (citable) accession number: P70232
Secondary accession number(s): A2RRK1 , Q8BS24, Q8C6W0, Q8C823, Q8VBY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	October 3, 2012
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program