ID A2AFG7_MOUSE Unreviewed; 1250 AA.
AC A2AFG7;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE SubName: Full=L1 cell adhesion molecule {ECO:0000313|Ensembl:ENSMUSP00000068135.6};
GN Name=L1cam {ECO:0000313|Ensembl:ENSMUSP00000068135.6,
GN ECO:0000313|MGI:MGI:96721};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000068135.6, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000068135.6, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000068135.6,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000068135.6}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000068135.6};
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}.
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DR RefSeq; XP_006527924.1; XM_006527861.3.
DR AlphaFoldDB; A2AFG7; -.
DR SMR; A2AFG7; -.
DR EPD; A2AFG7; -.
DR MaxQB; A2AFG7; -.
DR PeptideAtlas; A2AFG7; -.
DR ProteomicsDB; 318408; -.
DR Antibodypedia; 449; 1405 antibodies from 46 providers.
DR DNASU; 16728; -.
DR Ensembl; ENSMUST00000066576.12; ENSMUSP00000068135.6; ENSMUSG00000031391.19.
DR AGR; MGI:96721; -.
DR MGI; MGI:96721; L1cam.
DR VEuPathDB; HostDB:ENSMUSG00000031391; -.
DR GeneTree; ENSGT00940000157506; -.
DR OrthoDB; 2912783at2759; -.
DR BioGRID-ORCS; 16728; 2 hits in 78 CRISPR screens.
DR ChiTaRS; L1cam; mouse.
DR Proteomes; UP000000589; Chromosome X.
DR Bgee; ENSMUSG00000031391; Expressed in cortical plate and 253 other cell types or tissues.
DR ExpressionAtlas; A2AFG7; baseline and differential.
DR GO; GO:0030424; C:axon; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 4.
DR CDD; cd05876; Ig3_L1-CAM; 1.
DR CDD; cd05733; IgI_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; 4.
DR Pfam; PF13927; Ig_3; 1.
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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|EPD:A2AFG7,
KW ECO:0007829|MaxQB:A2AFG7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
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..1250
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002642252"
FT TRANSMEM 1119..1140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..125
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 133..220
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 234..322
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 327..414
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 419..501
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 512..595
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 608..706
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 711..804
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 806..911
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 914..1009
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 692..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1219..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1250 AA; 139822 MW; A7AD1EF63DA7B38D CRC64;
MVVMLRYVWP LLLCSPCLLI QIPDELLEPP VITEQSPRRL VVFPTDDISL KCEARGRPQV
EFRWTKDGIH FKPKEELGVV VHEAPYSGSF TIEGNNSFAQ RFQGIYRCYA SNKLGTAMSH
EIQLVAEGAP KWPKETVKPV EVEEGESVVL PCNPPPSAAP LRIYWMNSKI LHIKQDERVS
MGQNGDLYFA NVLTSDNHSD YICNAHFPGT RTIIQKEPID LRVKPTNSMI DRKPRLLFPT
NSSSRLVALQ GQSLILECIA EGFPTPTIKW LHPSDPMPTD RVIYQNHNKT LQLLNVGEED
DGEYTCLAEN SLGSARHAYY VTVEAAPYWL QKPQSHLYGP GETARLDCQV QGRPQPEITW
RINGMSMETV NKDQKYRIEQ GSLILSNVQP SDTMVTQCEA RNQHGLLLAN AYIYVVQLPA
RILTKDNQTY MAVEGSTAYL LCKAFGAPVP SVQWLDEEGT TVLQDERFFP YANGTLSIRD
LQANDTGRYF CQAANDQNNV TILANLQVKE ATQITQGPRS AIEKKGARVT FTCQASFDPS
LQASITWRGD GRDLQERGDS DKYFIEDGKL VIQSLDYSDQ GNYSCVASTE LDEVESRAQL
LVVGSPGPVP HLELSDRHLL KQSQVHLSWS PAEDHNSPIE KYDIEFEDKE MAPEKWFSLG
KVPGNQTSTT LKLSPYVHYT FRVTAINKYG PGEPSPVSET VVTPEAAPEK NPVDVRGEGN
ETNNMVITWK PLRWMDWNAP QIQYRVQWRP QGKQETWREQ TVSDPFLVVS NTSTFVPYEI
KVQAVNNQGK GPEPQVTIGY SGEDYPQVSP ELEDITIFNS STVLVRWRPV DLAQVKGHLK
GYNVTYWWKG SQRKHSKRHI HKSHIVVPAN TTSAILSGLR PYSSYHVEVQ AFNGRGLGPA
SEWTFSTPEG VPGHPEALHL ECQSDTSLLL HWQPPLSHNG VLTGYLLSYH PVEGESKEQL
FFNLSDPELR THNLTNLNPD LQYRFQLQAT TQQGPGEAIV REGGTMALFG KPDFGNISAT
AGENYSVVSW VPRKGQCNFR FHILFKALPE GKVSPDHQPQ PQYVSYNQSS YTQWNLQPDT
KYEIHLIKEK VLLHHLDVKT NGTGPVRVST TGSFASEGWF IAFVSAIILL LLILLILCFI
KRSKGGKYSV KDKEDTQVDS EARPMKDETF GEYSDNEEKA FGSSQPSLNG DIKPLGSDDS
LADYGGSVDV QFNEDGSFIG QYSGKKEKEA AGGNDSSGAT SPINPAVALE
//
