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Database: UniProt
Entry: A0A3Q1MLS9_BOVIN
LinkDB: A0A3Q1MLS9_BOVIN
Original site: A0A3Q1MLS9_BOVIN 
ID   A0A3Q1MLS9_BOVIN        Unreviewed;      1391 AA.
AC   A0A3Q1MLS9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=L1 cell adhesion molecule {ECO:0000313|Ensembl:ENSBTAP00000072651.1};
GN   Name=L1CAM {ECO:0000313|Ensembl:ENSBTAP00000072651.1,
GN   ECO:0000313|VGNC:VGNC:30760};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000072651.1, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000072651.1, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000072651.1,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000072651.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000072651.1};
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_015317002.1; XM_015461516.1.
DR   Ensembl; ENSBTAT00000071285.1; ENSBTAP00000072651.1; ENSBTAG00000013462.6.
DR   GeneID; 516017; -.
DR   CTD; 3897; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013462; -.
DR   VGNC; VGNC:30760; L1CAM.
DR   GeneTree; ENSGT00940000157506; -.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000013462; Expressed in retina and 92 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q1MLS9; baseline.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR   GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR   CDD; cd00063; FN3; 4.
DR   CDD; cd05876; Ig3_L1-CAM; 1.
DR   CDD; cd05867; Ig4_L1-CAM_like; 1.
DR   CDD; cd05845; IgI_2_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; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 6.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 6.
PE   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1259..1281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          172..267
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          277..364
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          378..466
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          471..558
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          563..651
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          656..745
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          752..850
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          855..948
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          951..1054
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1058..1153
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          834..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1291..1341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1364..1391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1291..1316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1375..1391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1391 AA;  154615 MW;  470CF80B3AA73975 CRC64;
     MFPRRPCMPC ASCKLQSFLL PGSCGTWWRG EGGRLCSVSS RWVSSLAFHL SLVVHPSLWS
     SSLPVRGLPS LVLLPLASPV SLFFLSHALS FCLASSLSSG FFLCDFWCHL LSVLVPSTFA
     QLLWAQLAPP RPTTQWPCGL SGSRPGFCPH GTRVRAEVLT MSVPPPAPVM EPPIITEQSP
     RRVVVFPTDD VSLKCEASGK PEVQFRWTRD GILFKPREEL GMIVNQVPHS GSFSITGNSS
     NFAQSFQGTY RCFASNKLGT AMSHEIQLMA EGTPKWPKET VKPVEVEEGE SVILPCHPPP
     SAEPLRIYWM NSKILHIKQD ERVTMGQNGN LYFANVLTSD NHSDYICHAH FPGTRTIIQK
     EPIDLRVKAT NSMMDRKPHL LFPTNSSSHL VALQGQPLIL ECIAEGFPTP TIKWLRPSGP
     MPADRVTYQN HNKTLQLLNV GEEDDGEYRC LAENSLGSDR HAYYVTVEAA PYWLHKPQSH
     LYGPGETARL DCQVQGRPQP EVTWRINGIP VEELGKDQKY RIHHGALVLS NLQPSDTMVT
     QCEARNRHGL LLANAYIYVV ELPAKILTPD NETYMAVQGS TAYLLCKAFG APVPSVQWLD
     REGKTVLQDE RFFPYTNGTL GIRDLQTNDT GHYFCQAAND QSNVTIVANL QVKDATRIMQ
     GPRSAIEKRG SRVMFTCQAS FDPSLQHSTT WRRDALDLQE LGDSDKYFIE DERLVIHSLD
     YSDQGNYSCV ASTKLDVVES RAELLVVGSP GPVPQLELSD HHLLKQSQVR LSWSPADDHN
     APIEKYDIEF EDKEMAPEKW YSLGKVPGNQ TSTTLKLSPY VHYTFRVTAI NKYGPGEPSP
     DSETVVTPEA APEKNPVDVK GEGNETNNMV ITWKPLRWMD WNAPQVQYRV QWRPQKMQGA
     WQEQIVSDPF LVVSNTSTFV PYEIKVQTVN SQGKGPEPQI TIGYSGEDYP QASPLLEPVK
     ALNSSTVLVR WQSVDPAQVK GHLRGYNVTY WWEGSQRKHN KRHVHKGHVV VPANATSTIL
     GGLRPYSSYW VEVQAFNGRG LGPASGMTFN TPEGVPGHPE ALHLECQSDT SLLLHWQPPL
     SHNGVLTGYV LSYQPLNDGS KEQLSFDLPD PELRTHNLTN LSPRLRYRFQ LQATTREGPG
     EAIVREGGTM ALSGMPDFGN ISAMAGENYS VVSWVPKEGQ CNFGFQIWFK ALGDEKLVAR
     LPPQYVSYNQ SSYTQWDLQP DTDYEIQLLK EQVLLHQMAV KTNGTGRVRL PPAGFATEGW
     FIGFISAIVV LLLVLLILCF IKRSKGGKYS VKDKEDTQVD SEARPMKDET FGEYSDNEEK
     AFGSSQPSLN GDIKPLGSDD SLADYGGSVD VQFNEDGSFI GQYSGKKEKE VAGGNDSSGA
     TSPINPAGTL E
//
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