ID U3EKF8_CALJA Unreviewed; 1209 AA.
AC U3EKF8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Neural cell adhesion molecule L1-like protein isoform 2 {ECO:0000313|EMBL:JAB26051.1};
GN Name=CHL1 {ECO:0000313|EMBL:JAB26051.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB26051.1};
RN [1] {ECO:0000313|EMBL:JAB26051.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebral cortex {ECO:0000313|EMBL:JAB26051.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GAMR01007881; JAB26051.1; -; mRNA.
DR AlphaFoldDB; U3EKF8; -.
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; cd00096; Ig; 1.
DR CDD; cd05731; Ig3_L1-CAM_like; 1.
DR CDD; cd04978; Ig4_L1-NrCAM_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: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; PF13927; Ig_3; 3.
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1209
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004640360"
FT TRANSMEM 1083..1104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..124
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 128..223
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 235..328
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 331..417
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 423..510
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 515..607
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 614..709
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 714..807
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 809..914
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 918..1015
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 693..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1209 AA; 135525 MW; 5795CB4ADDBA19CF CRC64;
METLLPRRGV IISLIFFLLK FSTAIEIPPS VQQVPTIIKQ SKVQVAFPFD EYFQIECEAK
GNPEPIFTWT KDDNPFYFTD PRIITSNNSG TFRIPNEGHI SHFQGKYRCF ASNKLGIAMS
EEIEFIVPSV PKFPKENIDP LEVEEGDPIV LPCNPPKGLP PLHIYWMNIE LEHIEQDERV
YMSQKGDLYF ANVEEKDSRN DYCCFAAFPR LRTIVQKMPM KLTVNSSNSI KQRKPRLLLP
PTESGSESSI TILKGETLLL ECFAEGLPTP QVDWNKIGGD LPKGRETKEN YGKTLKIENV
SYQDKGNYRC TASNFLGMAT HDFHVIVEEP PRWTKKPQSA VYSTGSNGIL LCEAEGEPQP
TIKWRVNGSP IDNHPFAGDV VFPREVSFTN LQPNHTAVYQ CEASNVHGTI LANANINIVD
VRPLIQTEDE ENYATVVGYS AFLHCEFFAS PEAIVSWQKV EEAKPLEGRR YHIYENGTLQ
INRTTEEDAG SYSCWVENSI GKTAVTANLD IRNATKLRVS PKNPRIPKLH MLELHCESKC
DAHLKHSLKL SWSKDGEAFE INGTEDGRII IDGANLTISN ITLEDQGIYC CSAHTDLDSA
ADITQVTVLD VPDPPENLHL SERQNRSVRL TWEAGDDHNS NISEYIVEFE GNKEEPGRWE
ELTRVQGKKT TVILPLAPFV RYQFRVIAMN EVGRSQPSQP SDHHETPPAA PDRNPQNIRV
QASQPKEMII KWEPLKSMEQ NGPGLEYRVT WKPQGAPVEW EEETVTNHTL RVMTPAVYAP
YDVEVQAINQ LGSGPDPQSV TLYSGEDYPD TAPVIHGVDV INSTLVKVTW STIPKDRVHG
RLKGYQINWW KTKSLLDGRT HPKEVNVLKF SGQRNSGMVP SLDAFSEFHL TVLAYNSKGA
GPESEPYIFQ TPEGVPEQPT FLKVIKVDKD TATLSWGLPK KLNGKLTGYL LQYQIINDTY
EIGELNDINI TTPSKPSWHL SNLNATTRYK FYLRACTSKG CGKPITEESS TLGEGSKGIG
KISEGVNLTQ KTHPIEVFEP GAEHIVRLMT KNWGDNDSIF QDVIETRGRE YAGLYDDIST
QGWFIGLMCA IALLTLVLLT VCFVKRNRGG KYSVKEKEDL HPDPEIQSVK DETFGEYSDS
DEKPLKGSLR SINRDMQPTE SADSLVEYGE GDHGLFNEDG SFIGAYAGSK EKGSVESNGS
STATFPLRA
//
