ID A0A1U8CY48_ALLSI Unreviewed; 1231 AA.
AC A0A1U8CY48;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Neural cell adhesion molecule L1-like protein isoform X2 {ECO:0000313|RefSeq:XP_014372951.1};
GN Name=CHL1 {ECO:0000313|RefSeq:XP_014372951.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014372951.1};
RN [1] {ECO:0000313|RefSeq:XP_014372951.1}
RP IDENTIFICATION.
RG RefSeq;
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_014372951.1; XM_014517465.2.
DR AlphaFoldDB; A0A1U8CY48; -.
DR GeneID; 102378844; -.
DR CTD; 10752; -.
DR OrthoDB; 2912783at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 4.
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; IPR013151; Immunoglobulin.
DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR PANTHER; PTHR44170:SF51; NEURAL CELL ADHESION MOLECULE L1-LIKE PROTEIN ISOFORM X1; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 2.
DR SMART; SM00060; FN3; 5.
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:UP000189705};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1231
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010537584"
FT TRANSMEM 1105..1126
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 129..222
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 236..327
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 354..439
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 445..532
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 537..623
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 636..731
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 736..829
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 834..936
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 937..1038
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 328..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1211..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1231 AA; 136559 MW; 92D23806F09038F9 CRC64;
MEMLFSTKGI TICLLFFVLS LAAAIQIPLS VAQLPTITEQ SKTQVAYPFD DDFAIKCEAT
GNPQPTFNWT KDGKPFDLLS DPRIIPFNNS GTFMIQNHGI MADFQGKYRC YASNALGTAM
SEEIELIVPS IPKFPKEKIE PLDVDCGDSV VLHCNPPKGI PPLHIYWMNI DLQHIPQDAR
VSMSLKGDLY FANVEENDSR SDYCCFAAFP RLRTIVQKMP MTLRVTRSNF IKERKPKLLI
PPESSGISSL VTVIKGGVLL LECIAEGLPT PLLIWNRVGR DMPEDRAATE NYGKVLKIGE
VSAADEGTYL CTASNSVGSV KHEFRVHVED QKTRRERSRD STKASDGISV RKPPQWVKKP
VSNVYSVGSN LVLFCQAIGN PEPTIKWKLN GMPIDGRTYR GQILPREISL INLQLQDSAV
YQCEATNKHG TILATANVNV INVSPVVLTP EGEDYATVVG YSAFLHCKVF ASPPPVIRWV
REDSTQSLEG LRYAVYENGS LEIKETMKED SGLYTCWVTN SVGKGAVNAN LDIRDATKIA
VTPKNPQVLK SHSVLLKCLS EYDPHLKHSF KLSWRKDGDE LQINSTEDGR IIADMDTVFI
SSVTMEDQGI YTCVASTSLD RVTAESQLIV LDIPDPPAAL HLSEKQDRSV RLSWRAGDSH
NSPINESIIE FEENRWEPGK WQELTRIQGN DTTAVLSLAP FINYHFRVIS VNAVGRSRAS
EPSARYETPP AAPDKNPENI RVEASQPNEM IMKWEPLKPV ERNGPGLEYK VSWRQQGVET
DWNEELVKKH SLPLGNTPTF VPYEIKVQAV NSLGSGPEPN VTTGYSGEDI PDAAPSSVMV
EVLNSTLVKA MWSRIPRDRV RGRLRGYKVI WWKTRSLLDG KRHHPEKHFL TFIGDRNHGM
IPGLEPFSEF HLTVLAFNGK GDGPESSPIM FHTPEGVPEQ PHFLRILNFD KDSVTLSWGL
PKKSNGFLTG YNLQYQIINE TDEIGPLSDV NITNPSTFSW RLSNLSSSTK YKFYVSACTM
KGCGKPATEE GLTITDGSKG IGKISGAVNP TQKFHPIEAL EPGTEYTVRL VTKNWVDNNS
IFEDVIETRG RAYAGIYEGI STQGWFIGLM CAIALLTLLL LTVCFVKRNK GGKYSVKEKE
DLHPDPEAQS IKDEIFGEYS DSDEKPLKGS LQSINGDIKA TESADSLVDY GEGDHGMFNE
DGSFIGAYSG SKEKGSVEST GSSTATFPLH A
//
