ID A0A1U8CV92_ALLSI Unreviewed; 1193 AA.
AC A0A1U8CV92;
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 X7 {ECO:0000313|RefSeq:XP_014372952.1};
GN Name=CHL1 {ECO:0000313|RefSeq:XP_014372952.1};
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_014372952.1};
RN [1] {ECO:0000313|RefSeq:XP_014372952.1}
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_014372952.1; XM_014517466.2.
DR AlphaFoldDB; A0A1U8CV92; -.
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 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; 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: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..1193
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010560836"
FT TRANSMEM 1067..1088
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 252..343
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 370..455
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 461..548
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 553..639
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 652..747
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 752..845
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 850..952
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 953..1054
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 344..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 132233 MW; 02A64D5D5F02DD1B CRC64;
MEMLFSTKGI TICLLFFVLS LAAAIQIPLS VAQLPTITEQ SKTQVAYPFD DDFAIKCEAT
GNPQPTFNWT KDGKPFDLLS DPRIIPFNNS GTFMIQNHGI MADFQGKYRC YASNALGTAM
SEEIELIVPS IPKFPKEKIE PLDVDCGDSV VLHCNPPKGI PPLHIYWMNI DLQHIPQDAR
VSMSLKGDLY FANVEENDSR SDYCCFAAFP RLRTIVQKMP MTLRVTRFKH TNDSGSPNAA
VTKANFIKER KPKLLIPPES SGISSLVTVI KGGVLLLECI AEGLPTPLLI WNRVGRDMPE
DRAATENYGK VLKIGEVSAA DEGTYLCTAS NSVGSVKHEF RVHVEDQKTR RERSRDSTKA
SDGISVRKPP QWVKKPVSNV YSVGSNLVLF CQAIGNPEPT IKWKLNGMPI DGRTYRGQIL
PREISLINLQ LQDSAVYQCE ATNKHGTILA TANVNVINVS PVVLTPEGED YATVVGYSAF
LHCKVFASPP PVIRWVREDS TQSLEGLRYA VYENGSLEIK ETMKEDSGLY TCWVTNSVGK
GAVNANLDIR DATKIAVTPK NPQVLKSHSV LLKCLSEYDP HLKHSFKLSW RKDGDELQIN
STEDGRIIAD MDTVFISSVT MEDQGIYTCV ASTSLDRVTA ESQLIVLDIP DPPAALHLSE
KQDRSVRLSW RAGDSHNSPI NESIIEFEEN RWEPGKWQEL TRIQGNDTTA VLSLAPFINY
HFRVISVNAV GRSRASEPSA RYETPPAAPD KNPENIRVEA SQPNEMIMKW EPLKPVERNG
PGLEYKVSWR QQGVETDWNE ELVKKHSLPL GNTPTFVPYE IKVQAVNSLG SGPEPNVTTG
YSGEDIPDAA PSSVMVEVLN STLVKAMWSR IPRDRVRGRL RGYKVIWWKT RSLLDGKRHH
PEKHFLTFIG DRNHGMIPGL EPFSEFHLTV LAFNGKGDGP ESSPIMFHTP EGVPEQPHFL
RILNFDKDSV TLSWGLPKKS NGFLTGYNLQ YQIINETDEI GPLSDVNITN PSTFSWRLSN
LSSSTKYKFY VSACTMKGCG KPATEEGLTI TDGTYAGIYE GISTQGWFIG LMCAIALLTL
LLLTVCFVKR NKGGKYSVKE KEDLHPDPEA QSIKDEIFGE YSDSDEKPLK GSLQSINGDI
KATESADSLV DYGEGDHGMF NEDGSFIGAY SGSKEKGSVE STGSSTATFP LHA
//
