ID A0A2Y9PW20_DELLE Unreviewed; 1235 AA.
AC A0A2Y9PW20;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Neurofascin isoform X12 {ECO:0000313|RefSeq:XP_022449386.1};
GN Name=NFASC {ECO:0000313|RefSeq:XP_022449386.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022449386.1};
RN [1] {ECO:0000313|RefSeq:XP_022449386.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022449386.1};
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_022449386.1; XM_022593678.2.
DR AlphaFoldDB; A0A2Y9PW20; -.
DR Proteomes; UP000248483; 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; cd05731; Ig3_L1-CAM_like; 1.
DR CDD; cd05845; IgI_2_L1-CAM_like; 1.
DR CDD; cd05875; IgI_hNeurofascin_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 InterPro; IPR026965; NFASC_Ig-like.
DR PANTHER; PTHR44170:SF12; NEUROFASCIN; 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; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 2.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
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:UP000248483};
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..1235
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016030023"
FT TRANSMEM 1105..1126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..137
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 143..224
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 244..332
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 337..424
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 429..517
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 521..603
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 630..725
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 727..823
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 827..923
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1002..1094
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 713..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1235 AA; 137316 MW; E39CDA0235D5FD17 CRC64;
MARQQPPPWV HTAFLFCLLS LTGAIEIPMD PSIQNELSQP PTITKQSVKE HIVDPRDNIL
IECEAKGNPA PSFHWTRNSR FFNIAKDPRV SMRRRSGTLV IDFRSGGRPE EYEGEYQCFA
RNKFGTALSN RIRLQVSKSP LWPKENLDPV VVQEGAPLTL QCNPPPGLPS PVIFWMSSSM
EPITQDKRVS QGHNGDLYFS NVMLQDMQTD YSCNARFHFT HTIQQKNPFN LKVLTTRGVA
ERTPSFMYPQ GTASSQMVLR GMDLLLECIA SGVPTPDIAW YKKGGDLPSD KAKFENFNKA
LRITNVSEED SGEYFCLASN KMGSIRHTIS VRVKAAPYWL DEPKNLILAP GEDGRLVCRA
NGNPKPTVQW MVNGEPLQSA PPNPNREVAG DTIIFRDTQI SSRAVYQCNT SNEHGYLLAN
AFVSVLDVPP RMLSPRNQLI RVILYNRTRL DCPFFGSPIP TLRWFKNGQG SNLDGGNYHV
YENGSLEIKM IRKEDQGIYT CVATNILGKA ENQVRLEVKD PTRIYRMPED QVAKRGTTVQ
LECRVKHDPS LKLTVYWLKD DEPLYVGNRM KKEEDSLTIF GVAERDQGSY TCVASTELDQ
DLAKAYLTVL ADQATPTNRL AALPKGRPDR PRDLELTDLA ERSVRLTWIP GDDNNSPITD
YVVQFEEDQF QPGVWHDHSK FPGSVNSAIL QLSPYVNYQF RVIAINEVGS SHPSLPSERY
RTSGAPPESN PSDVKGEGTR KNNMEITWTP MNATSAFGPN LRYIVKWRRR ETRETWNNVT
VWGSRYVVGQ TPVYVPYEIR VQAENDFGKG PEPDTVIGYS GEDLPSAPRR FRVRQPNLET
INLEWDHPEH PNGILIGYTL KYVAFNGTKV GKQIAENFSP NQTKFTMQRA DPVSRYRFSL
SARTQVGSGE AVTEESPAPP NEAAPTAAPP TSPPTTVGVT GTVGSTDATA ATTEATTVPT
IPTVAPSTVA TTTVATTTTT TAAATATEGP PTTTRTEIQE SAPDEQSIWN VTVLPNSKWA
NITWKHNFGP GTDFVVEYID SNHTKKTVPV KAQAQPIQLT DLYPGMTYTL RVYSRDNEGI
SSTVITFMTS TAYTNNQADI ATQGWFIGLM CAVALLVLTL LIVCFIKRSR GGKYPVREKK
DVPLGPEDPK EEDGSFDYSD EDNKPLQGSQ TSLDGTIKQQ ESDDSLVDYG EGGEGQFNED
GSFIGQYTVK KDKEETEGNE SSEATSPVNA IYSLA
//
