ID A0A087QPQ7_APTFO Unreviewed; 1255 AA.
AC A0A087QPQ7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Neurofascin {ECO:0000313|EMBL:KFM03211.1};
DE Flags: Fragment;
GN ORFNames=AS27_02011 {ECO:0000313|EMBL:KFM03211.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM03211.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM03211.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM03211.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL225799; KFM03211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QPQ7; -.
DR STRING; 9233.A0A087QPQ7; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
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 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; 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 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; PF13927; Ig_3; 2.
DR SMART; SM00060; FN3; 5.
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:UP000053286};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1126..1147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..105
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 111..198
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 229..317
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 322..409
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 415..504
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 506..593
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 600..695
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 700..793
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 798..900
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 904..1000
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 683..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM03211.1"
FT NON_TER 1255
FT /evidence="ECO:0000313|EMBL:KFM03211.1"
SQ SEQUENCE 1255 AA; 141272 MW; 5C768D6AB5717E81 CRC64;
ICFAVPQPPT ITKQSVKDYI VDPRDNIFIE CEAKGNPVPT FSWTRNGKFF NVAKDPKVSM
RRRSGTLVID FHSGGRPEDY EGEYQCFARN DYGTALSSKI HLQVSKSPLW PKEKVDVIEV
DEGAPLSLQC NPPPGLPSPV IFWMSSSMEP IHQDKRVSQG QNGDLYFSNV MLQDAQTDYS
CNARFHFTHT IQQKNPYTLK VKTKKPHNET SLRNHTDMYS ARGITETTPS FMYPYGTSSS
QMVLRGVDLL LECIASGVPA PDIVWYKKGG ELPAGKTKLE NFNKALRISN VSEEDSGEYF
CLASNKMGSI RHTISVRVKA APYWLDEPQN LILAPGEDGR LVCRANGNPK PAIQWLVNGE
PIEASPPNPS REVAGDTIVF RDTQIGSSAV YQCNASNEHG YLLANAFVSV LDVPPRILAP
RNQLIKVIQN NRTRLDCPFF GSPIPTLRWF KNGQGNTLDG GNYKAHENGS LEMNMARKED
QGIYTCVATN ILGKAEAQVR LEVKDPTRIV RGPEDQVVKR GSMPRLHCRI KHDPTLKLTV
TWLKDDAPLY IGNRMKKEDD GLTIYGVAEK DQGDYTCIAS TELDKDSAKA YLTVLERPDR
PRDLELTDLA ERSVRLTWIP GDDNNSPITD YIVQFEEDRF QPGMWHNHSR YPGSVNSAVL
SLSPYVNYQF RVIAVNDVGS SLPSVPSERY QTNGARPEIN PTGVQGAGTQ KNNMEITWTP
LNATQAYGPN LRYIVRWRRR DPRGSWYNET VKTPRHVVWN TPIYVPYEIK VQAENDFGRA
PEPDTVIGYS GEDYPKAAPT DVRIRVLNST AIALTWTRVH LDTIQGQLKE YRAYFWRDSS
LLKNLWVSKK RQYVSFPGDR NRGIVSRLFP YSNYKLEMVV TNGRGDGPRS EVKEFPTPEG
VPSSPRYLRI RQPNLESINL EWDQPEHPNG VLTGYNLRYQ AFNGSKTGRT LVENFSPNQT
RFTLQRTDPI SRYRFFLRAR TQVGEGETIV EESPALLNEG ATLRGVCVKC TFTPLLWKYS
TATNGSSIWD IRAMANSNWA NITWSHNYSA GTDFVVKYIT SNKTEKSIPV KAQTPSSVQL
ANLTPGMMYK LWVFPIWSSP SEHSYITFTT SSAYTKNHVD IATQGWFIGL MCAIALLVLI
LLIVCFIKRS RGGKYPVRDN KDEHLNPEDK NVEDGSFDYS DEDNKPLPNS QTSLDGTIKQ
QESDDSLVDY GEGGEGQFNE DGSFIGQYTV KKDKEETEGN ESSEATSPVN AIYSL
//
