ID Q9XT41_CHLAE Unreviewed; 1248 AA.
AC Q9XT41;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Neural cell adhesion molecule L1 {ECO:0000313|EMBL:AAD28610.1};
GN Name=L1CAM {ECO:0000313|EMBL:AAD28610.1};
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534 {ECO:0000313|EMBL:AAD28610.1};
RN [1] {ECO:0000313|EMBL:AAD28610.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Kidney {ECO:0000313|EMBL:AAD28610.1};
RX PubMed=10797421;
RX DOI=10.1002/(SICI)1096-8628(20000501)92:1<40::AID-AJMG7>3.0.CO;2-R;
RA Finckh U., Schroeder J., Ressler B., Veske A., Gal A.;
RT "Spectrum and detection rate of L1CAM mutations in isolated and familial
RT cases with clinically suspected L1-disease.";
RL Am. J. Med. Genet. 92:40-46(2000).
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 EMBL; AF129167; AAD28610.1; -; mRNA.
DR AlphaFoldDB; Q9XT41; -.
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; cd05867; Ig4_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; 3.
DR Pfam; PF13927; Ig_3; 2.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 2: Evidence at transcript 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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|SAM:SignalP}; 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..1248
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004336684"
FT TRANSMEM 1116..1138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..120
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 134..221
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 235..323
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 328..415
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 420..502
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 513..602
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 610..707
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 712..805
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 809..911
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 915..1010
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 693..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1248 AA; 138902 MW; 2438A93A29C3BD61 CRC64;
MVVALRYVWP LLLCSPCLLI QIPEELMEPP VITEQSPRRL VVFPTDDISL KCEASGKPEV
QFRWTRDGVH FKPKEELGVT VYQSPHSGSF TITGNNSNFA QRFQGIYRCF ASNKLGTAMS
HEIRLMAEGA PKWPKETVKP VEVEEGESVV LPCHPPPSAE PLRIYWMNSK ILHIKQDERV
TMGQNGNLYF ANVLTSDNHS DYICHAHFPG TRTIIQKEPI DLRVKATNSM IDRKPRLLFP
TNSSSHLVAL QGQPLVLECI AEGFPTPTIK WLRPSGPMPA DRVTYQNHNK TLQLLKVGEE
DDGEYRCLAE NSLGSARHAY YVTVEAAPYW LHKPQSHLYG PGETARLDCQ VQGRPQPEVT
WRINGIPMEE LAKDQKYRIQ RGALILSNAQ PSDTMVTQCE ARNRHGLLLA NAYIYVVQLP
AKILTADNQT YMAVQGSTAY LLCKAFGAPV PSVQWLDEDG TTVLQDERFF PYANGTLGIR
DLRANDTGRY LCLAANDQNN VTIVAHLKVK DATQITQGPR SAIEKKGSRV TFTCQASFDP
SLQPSITWRG DGRDLQELGD SDKYFIEDGR LVIHSLDYSD QGNYSCVAST ELDVVESRAQ
LLVVGSPGPV PRLVLSDLHL LTQSQVRVSW SPAEDHNAPI EKYDIEFEDK EMAPEKWYSL
GKVPGNQTST TLKLSPYVHY TFRVTAINKY GPGEPSPVSE TVVTPEAAPE KNPVDVKGEG
NETTNMVITW KPLRWMDWNA PQVQYRVQWR PQGTRGPWQE QIVSDPFLVV SNTSTFVPYE
IKVQAVNSQG KGPEPQVTIG YSGEDYPQAI PELEGIEILN SSAVLVKWRP VDLAQVKGHL
RGYNVTYWRE GSQRKHSKRH IHKDHVVVPA NTTSVILSGL RPYSSYHLEV QAFNGRGLGP
ASEFTFSTPE GVPGHPEALH LECQSNTSLL LRWQPPLSHN GVLTGYVLSY HPLDEGGKGQ
LSFNLRDPEL RTHNLTDLSP HLRYRFQLQA TTKEGPGEAI VREGGTMALS GISDFGNISA
TAGENYSVVS WVPKEGQCNF RFHILFKALG EEKGGASLSP QYVSYNQSSY TQWDLQPDTD
YEIHLFKERM FRHQMAVKTN GTGRVRLPPA GFATEGWFIG FVSAIILLLL VLLILCFIKR
SKGGKYSVKD KEDTQVDSEA RPMKDETFGE YSDNEEKAFG SSQPSLNGDI KPLGSDDSLA
DYGGSVDVQF NEDGSFIGQY SGKNEKEAAG GNDSSGATSP INPAVALE
//
