ID A0A2K6UR41_SAIBB Unreviewed; 1248 AA.
AC A0A2K6UR41;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=L1 cell adhesion molecule {ECO:0000313|Ensembl:ENSSBOP00000034379.1};
GN Name=L1CAM {ECO:0000313|Ensembl:ENSSBOP00000034379.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000034379.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000034379.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6UR41; -.
DR Ensembl; ENSSBOT00000051301.1; ENSSBOP00000034379.1; ENSSBOG00000033301.1.
DR GeneTree; ENSGT00940000157506; -.
DR Proteomes; UP000233220; Unplaced.
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 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:UP000233220};
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..1248
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014394552"
FT TRANSMEM 1116..1138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..125
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 139..226
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 240..328
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 333..420
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 425..513
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 518..607
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 612..712
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 717..810
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 815..916
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 920..1015
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 698..725
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; 138992 MW; 5B2CB447B0300D35 CRC64;
MVVALRYVWP LLLCSPCLLI QIPEEYEGHH VMEPPVITEQ SPRRLVVFPT DDISLKCEAS
GKPEVQFRWT RDGVHFKPKD ELGVTVYQAP HSGSFTITGN NSNFAQRFQG VYRCFASNKL
GTAMSHEIRL MAEGAPKWPK ETVKPVEVEE GESVVLPCHP PPSAEPLRIY WMNSKILHIK
QDERVTMGQN GNLYFANVLT SDNHSDYICH AHFPGTRTII QKEPIDLRVK ATNSMIDRKP
RLLFPTNSSS HLVALQGQPL VLECIAEGFP TPTIKWLRPS GPMPADRVTY QNHNKTLQLL
NVGEEDDGEY RCLAENSLGS ARHDYYVTVE AAPYWLHKPQ SHLYGPGETA RLDCQVQGRP
QPEITWRING IPVEELAKDQ KYRIQRGALI LSNVQPSDTM VTQCEAGNRH GLLLANAYIY
VVQLPAKILT ADNQTYMAVR GSTAYLLCKA FGAPVPSVQW LDEDGTTVLQ DERFFPYANG
TLGIRDLQAN DTGRYFCQAA NDQNNVTIVA NLQIKDATQI TQGPRSTIEK KGSRVTFTCQ
ASFDPSLQPS ITWRGDGRDL QELGDSDKYF IEDGRLVIHS LDYSDQGNYS CVASTELDVV
ESRAQLLVVG SPGSVPWLAV SDLHLLKQSQ VRLSWSPAED HNAPIEKYDI EFEDKEMAPE
KWYSLGKVPG NQTSTTLKLS PYVHYTFRVT AINKYGPGEP SPVSETVVTP EAAPEKNPVN
VKGEGNETTN MVITWKPLRW MDWNAPQVQY RVQWRPQGTR GPWQEQIVSD PFLVVSNTST
FVPYEIKVQA VNRQGKGPEP QVTIGYSGED YPQAVPELEG IEILNSSAVL VKWRPVDLAQ
VKGHLRGYNV TYWREGSQRK HSKRHTHRDH VVVPANTTSV ILSGLRPYSS YHLEVQAFNG
RGLGPASEFT FSTPEGVPGH PEALHVECQS NTSLRLHWQP PLSHNGVLTG YVLSYRPLDE
GGKVPLSFNL RDPELRAHNL TDLSPHLRYR FQLQATTKEG PGEAIVREGG TMALSGISDF
GNISATAGEN YSVVSWVPRE GQCNFRFHIL FKALGEEKGG AYVSYNQSSY TQGDLQPDTD
YEIHLFKERM FQHRMAVKTN GTGRVRLPPA GFATEGWFIG FVSAIILLLL LLLILCFIKR
SKGGKYSVKD KEDTQVDSEA RPMKDETFGE YSDNEEKAFG SSQPSLNGDI KPLGSDDSLA
DYGGSVDVQF NEDGSFIGQY SGKKEKEAAG GNDSSGATSP INPAVALE
//
