ID A0A3P8Z043_ESOLU Unreviewed; 1219 AA.
AC A0A3P8Z043;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Neural cell adhesion molecule L1.1-like {ECO:0000313|Ensembl:ENSELUP00000022179.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000022179.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000022179.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000022179.2}
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; A0A3P8Z043; -.
DR Ensembl; ENSELUT00000033060.2; ENSELUP00000022179.2; ENSELUG00000021621.2.
DR GeneTree; ENSGT00940000157506; -.
DR Proteomes; UP000265140; LG12.
DR Bgee; ENSELUG00000021621; Expressed in brain and 10 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; Immunoglobulins; 11.
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:SF48; MYOPALLADIN; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 4.
DR SMART; SM00060; FN3; 5.
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; 5.
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:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1087..1108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..133
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 137..221
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 242..330
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 335..410
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 427..510
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 518..610
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 596..690
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 692..789
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 791..895
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 899..990
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 992..1079
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 672..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1219 AA; 135985 MW; 1A8FD2C4A5F1A7E3 CRC64;
MQHPNFFGNR VVYILCSVFL SVILLFCMYM SCIYVYLYYM MCSVLQPPVL TELPKSLTAF
SLDDVTLPCE ATGTPTPSFR WTRDGLELKT KYEGSGTFTP HDDQPLSSYQ GNYRCYANND
LGTAMTHTIR LITELTPTLP KQKRIRLKVD EGAHVVLHCN PPQSSTPPEI HWMDRKLNHI
MQSERVIRGL DGNLYFANVL KGDSRDDYTC NAHYSEARTI LPKEPISLTV ISSNDEVRGR
KPQLMQPQGQ HSSHLALRGH HLVLECIPRG LPTPLVKWRH KDVALAESGA EEKHHGRWLE
FKSITQKADG EYECVSSNTH GSIKHSYTVT VEAEPYWVKE PQSLLYAPGE TVRLDCQAEG
VPTPTVTWSM NGEPIKDLDS DFRRNVSRGV LILTDVTFTD TAVYQCEATN RHGTILINTF
IYVIELPAQI LSSDGVVYRI TEGGVVRMHC DAFGSPRPQV TWDTADPQNV LLSDSRVSQL
TNGTIELFNA SREDVGIYTC SITQSNISIT AHLEVLNRTV MLIGPQDVKV KRGGDSWLDC
YVSHDLQINH LKITWKKDNL NIVESSPDDK YTIFKNGTLR VTDIHSGDGG RYSCEVITEL
DRVSASGSIT VFINVKFMVL PVEFVVEMWE KKNSSETVKW EEFHRVNGDI HHLELSLLPD
LTYQFRVSGV NDLGKSNPSE PSESYRHPPA VPDRNPEDVR SVSNETGKLL ITWKEMDDRY
FYGSGFLYKV SWRQAHGREP HWHHAFVRKP PHSVNGVGTF SSYDIKVQAV NSLGEGPHPV
TTTGHSGEDK PLDSVSNISI SVVNNSAKVR WQPVDPHMVQ GHLLGHKVTR TTMGGVERGT
EREEDRRVLV VNGSMTEVEL TGLTLYSVYE LSITVFNSMG EGPHSPKHSF STPEGAPGPP
ASLDFESPSE TELILRWTPP TQPNGQILEY ILQYQQNSPL KILMIPDWAV TQILVAGLEP
HSSYVFYLSG RTAAGRGPAI KREGATLLDG VPPSDISTVP GETSVNLSWV PEKRHRNHGF
HIRYLPKTGG SRWEESEQVN STQGFYSLTG LQAGTEYHLL ITHNNKTKWE TRILTTGPVG
DFATQGWFIG LISAVVLLML LLLILCFIKR SRGGKYAVKD KEVGQADSDV RPIKDETFGE
YSDGEEKRSG SQPSLCVESK LGSDDSLAEY GDSVDIQFNE DGSFIGQYSG RGPVPTGNES
SGPTSPCTRD EHSQPKTAG
//
