P97685 (NFASC_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neurofascin

Gene names

Name:

Nfasc

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1240 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions. Isoform 2/isoform 3 may be responsible for mediating and signaling axon-glial interaction during the early stages of myelination. Ref.3 Ref.4 Ref.6
Subunit structure	Horseshoe-shaped homodimer By similarity. Probable constituent of a neurofascin/NRCAM/ankyrin G complex. Associates with the sodium channel beta-1 (SCN1B) and beta-3 (SCN3B) subunits. Associates to subunit beta-1 in developing axons as early as postanatal day 5, during the period that nodes of Ranvier are forming. Isoform 2/isoform 3 is likely to interact with axonal proteins in close association with CNTNAP1. Interacts with GLDN/gliomedin. Ref.2 Ref.5 Ref.6
Subcellular location	Cell membrane; Single-pass type I membrane protein. Note: Isoform 1 colocalizes with ankyrin G at the nodes of Ranvier. Isoform 2/ isoform 3 is a glial component of the paranodal axo-glial junction.
Tissue specificity	Isoform 1 is expressed at Nodes of Ranvier while isoform 2/isoform 3 is expressed in unmyelinated axons. Ref.4
Developmental stage	Strongly but transiently up-regulated in oligodendrocytes at the onset of myelinogenesis. Once these last have engaged their target exons, expression declines precipitously.
Domain	Homophilic adhesion is primarily mediated by the interaction of the second Ig-like domains By similarity.
Post-translational modification	Isoform 2/isoform 3 is phosphorylated at P12. Dephosphorylation is required for ankyrin binding. Ref.4
Sequence similarities	Belongs to the immunoglobulin superfamily. L1/neurofascin/NgCAM family. Contains 4 fibronectin type-III domains. Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Inferred from electronic annotation. Source: Compara cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW myelination Inferred from expression pattern PubMed 16652168PubMed 16652168. Source: BHF-UCL paranodal junction assembly Inferred from electronic annotation. Source: Compara peripheral nervous system development Inferred from expression pattern PubMed 16652168. Source: BHF-UCL protein localization to juxtaparanode region of axon Inferred from electronic annotation. Source: Compara protein localization to paranode region of axon Inferred from electronic annotation. Source: Compara protein targeting to plasma membrane Inferred from direct assay PubMed 16525039. Source: BHF-UCL synapse organization Inferred from electronic annotation. Source: Compara
Cellular_component	Schwann cell microvillus Inferred from direct assay PubMed 17045809. Source: RGD axon initial segment Inferred from direct assay PubMed 11724816. Source: BHF-UCL integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intracellular Inferred from direct assay PubMed 16525039. Source: BHF-UCL node of Ranvier Inferred from direct assay PubMed 16652168. Source: BHF-UCL paranodal junction Inferred from electronic annotation. Source: Compara paranode region of axon Inferred from electronic annotation. Source: Compara plasma membrane Traceable author statement. Source: Reactome
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P97685-1)

Also known as: NF186; 186 kDa isoform;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P97685-2)

Also known as: NF155; 155 kDa isoform;

The sequence of this isoform differs from the canonical sequence as follows:
     31-36: Missing.
     236-236: T → NNPYNDSSLRNHPDIYSA
     824-824: L → YPRAAPTEVK...TKEFTTPEGV
     928-1096: Missing.

Isoform 3 (identifier: P97685-3)

Also known as: NF155; 155 kDa isoform;

The sequence of this isoform differs from the canonical sequence as follows:
     31-36: Missing.
     236-236: T → NNPYNDSSLRNHPDIYSA
     611-625: Missing.
     824-824: L → YPRAAPTEVK...TKEFTTPEGV
     928-1096: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 1240	1216	Neurofascin		PRO_0000015051
Regions
	Topological domain	25 – 1110	1086	Extracellular Potential
	Transmembrane	1111 – 1131	21	Helical; Potential
	Topological domain	1132 – 1240	109	Cytoplasmic Potential
	Domain	41 – 137	97	Ig-like C2-type 1
	Domain	143 – 230	88	Ig-like C2-type 2
	Domain	244 – 332	89	Ig-like C2-type 3
	Domain	337 – 424	88	Ig-like C2-type 4
	Domain	429 – 517	89	Ig-like C2-type 5
	Domain	521 – 603	83	Ig-like C2-type 6
	Domain	628 – 720	93	Fibronectin type-III 1
	Domain	727 – 820	94	Fibronectin type-III 2
	Domain	825 – 918	94	Fibronectin type-III 3
	Domain	1008 – 1094	87	Fibronectin type-III 4
	Compositional bias	913 – 1006	94	Thr-rich
Amino acid modifications
	Modified residue	481	1	Phosphotyrosine By similarity
	Modified residue	485	1	Phosphoserine By similarity
	Modified residue	1226	1	Phosphoserine By similarity
	Modified residue	1227	1	Phosphoserine By similarity
	Glycosylation	305	1	N-linked (GlcNAc...) Potential
	Glycosylation	409	1	N-linked (GlcNAc...) Potential
	Glycosylation	446	1	N-linked (GlcNAc...) Potential
	Glycosylation	483	1	N-linked (GlcNAc...) Potential
	Glycosylation	752	1	N-linked (GlcNAc...) Potential
	Glycosylation	778	1	N-linked (GlcNAc...) Potential
	Glycosylation	866	1	N-linked (GlcNAc...) Potential
	Glycosylation	881	1	N-linked (GlcNAc...) Potential
	Glycosylation	1015	1	N-linked (GlcNAc...) Potential
	Glycosylation	1026	1	N-linked (GlcNAc...) Potential
	Glycosylation	1047	1	N-linked (GlcNAc...) Potential
	Glycosylation	1101	1	N-linked (GlcNAc...) Potential
	Disulfide bond	63 ↔ 118		By similarity
	Disulfide bond	162 ↔ 213		By similarity
	Disulfide bond	268 ↔ 316		By similarity
	Disulfide bond	358 ↔ 408		By similarity
	Disulfide bond	452 ↔ 501		Potential
	Disulfide bond	543 ↔ 592		Potential
Natural variations
	Alternative sequence	31 – 36	6	Missing in isoform 2 and isoform 3.		VSP_050416
	Alternative sequence	236	1	T → NNPYNDSSLRNHPDIYSA in isoform 2 and isoform 3.		VSP_050417
	Alternative sequence	611 – 625	15	Missing in isoform 3.		VSP_008941
	Alternative sequence	824	1	L → YPRAAPTEVKIRVLNSTAIS LQWNRVYPDTVQGQLREYRA YYWRESSLLKNLWVSQKRQQ ASFPGDRPRGVVGRLFPYSN YKLEMVVVNGRGDGPRSETK EFTTPEGV in isoform 2 and isoform 3.		VSP_050418
	Alternative sequence	928 – 1096	169	Missing in isoform 2 and isoform 3.		VSP_050419
Experimental info
	Sequence conflict	482	1	E → Q in AAB47753. Ref.2
	Sequence conflict	482	1	E → Q in AAB47754. Ref.2
	Sequence conflict	675	1	W → L in AAB47753. Ref.2
	Sequence conflict	675	1	W → L in AAB47754. Ref.2
	Sequence conflict	699	1	Q → D in AAB47753. Ref.2
	Sequence conflict	699	1	Q → D in AAB47754. Ref.2
	Sequence conflict	763	1	Y → YY in AAB47753. Ref.2
	Sequence conflict	763	1	Y → YY in AAB47754. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (NF186) (186 kDa isoform) [UniParc]. Last modified November 14, 2003. Version 2. Checksum: 636A187BC3772513	FASTA	1,240	138,004
	10 20 30 40 50 60 MARQQAPPWV HVALILFLLS LGGAIEIPMD PSIQNELTQP PTITKQSVKD HIVDPRDNIL 70 80 90 100 110 120 IECEAKGNPA PSFHWTRNSR FFNIAKDPRV SMRRRSGTLV IDFRSGGRPE EYEGEYQCFA 130 140 150 160 170 180 RNKFGTALSN RIRLQVSKSP LWPKENLDPV VVQEGAPLTL QCNPPPGLPS PVIFWMSSSM 190 200 210 220 230 240 EPITQDKRVS QGHNGDLYFS NVMLQDMQTD YSCNARFHFT HTIQQKNPFT LKVLTTRGVA 250 260 270 280 290 300 ERTPSFMYPQ GTSSSQMVLR GMDLLLECIA SGVPTPDIAW YKKGGDLPSD KAKFENFNKA 310 320 330 340 350 360 LRITNVSEED SGEYFCLASN KMGSIRHTIS VRVKAAPYWL DEPKNLILAP GEDGRLVCRA 370 380 390 400 410 420 NGNPKPTVQW LVNGDPLQSA PPNPNREVAG DTIIFRDTQI SSRAVYQCNT SNEHGYLLAN 430 440 450 460 470 480 AFVSVLDVPP RMLSPRNQLI RVILYNRTRL DCPFFGSPIP TLRWFKNGQG SNLDGGNYHV 490 500 510 520 530 540 YENGSLEIKM IRKEDQGIYT CVATNILGKA ENQVRLEVKD PTRIYRMPED QVAKRGTTVQ 550 560 570 580 590 600 LECRVKHDPS LKLTVSWLKD DEPLYIGNRM KKEDDSLTIF GVAERDQGSY TCMASTELDQ 610 620 630 640 650 660 DLAKAYLTVL ADQATPTNRL AALPKGRPDR PRDLELTDLA ERSVRLTWIP GDDNNSPITD 670 680 690 700 710 720 YVVQFEEDQF QPGVWHDHSK FPGSVNSAVL HLSPYVNYQF RVIAVNEVGS SHPSLPSERY 730 740 750 760 770 780 RTSGAPPESN PSDVKGEGTR KNNMEITWTP MNATSAFGPN LRYIVKWRRR ETRETWNNVT 790 800 810 820 830 840 VWGSRYVVGQ TPVYVPYEIR VQAENDFGKG PEPETVIGYS GEDLPSAPRR FRVRQPNLET 850 860 870 880 890 900 INLEWDHPEH PNGILIGYTL RYVPFNGTKL GKQMVENFSP NQTKFSVQRA DPVSRYRFSL 910 920 930 940 950 960 SARTQVGSGE AATEESPTPP NEATPTAAPP TLPPTTVGTT GLVSSTDATA LAATSEATTV 970 980 990 1000 1010 1020 PIIPTVVPTT VATTIATTTT TTAAATTTTT TESPPTTTTG TKIHETAPDE QSIWNVTVLP 1030 1040 1050 1060 1070 1080 NSKWANITWK HNFRPGTDFV VEYIDSNHTK KTVPVKAQAQ PIQLTDLFPG MTYTLRVYSR 1090 1100 1110 1120 1130 1140 DNEGISSTVI TFMTSTAYTN NQTDIATQGW FIGLMCAIAL LVLILLIVCF IKRSRGGKYP 1150 1160 1170 1180 1190 1200 VREKKDVPLG PEDPKEEDGS FDYSDEDNKP LQGSQTSLDG TIKQQESDDS LVDYGEGGEG 1210 1220 1230 1240 QFNEDGSFIG QYTVRKDKEE TEGNESSEAT SPVNAIYSLA
	Isoform 2 (NF155) (155 kDa isoform) [UniParc]. Checksum: C63224BE3EE83B1B	FASTA	1,189	133,776
	10 20 30 40 50 60 MARQQAPPWV HVALILFLLS LGGAIEIPMD LTQPPTITKQ SVKDHIVDPR DNILIECEAK 70 80 90 100 110 120 GNPAPSFHWT RNSRFFNIAK DPRVSMRRRS GTLVIDFRSG GRPEEYEGEY QCFARNKFGT 130 140 150 160 170 180 ALSNRIRLQV SKSPLWPKEN LDPVVVQEGA PLTLQCNPPP GLPSPVIFWM SSSMEPITQD 190 200 210 220 230 240 KRVSQGHNGD LYFSNVMLQD MQTDYSCNAR FHFTHTIQQK NPFTLKVLTN NPYNDSSLRN 250 260 270 280 290 300 HPDIYSARGV AERTPSFMYP QGTSSSQMVL RGMDLLLECI ASGVPTPDIA WYKKGGDLPS 310 320 330 340 350 360 DKAKFENFNK ALRITNVSEE DSGEYFCLAS NKMGSIRHTI SVRVKAAPYW LDEPKNLILA 370 380 390 400 410 420 PGEDGRLVCR ANGNPKPTVQ WLVNGDPLQS APPNPNREVA GDTIIFRDTQ ISSRAVYQCN 430 440 450 460 470 480 TSNEHGYLLA NAFVSVLDVP PRMLSPRNQL IRVILYNRTR LDCPFFGSPI PTLRWFKNGQ 490 500 510 520 530 540 GSNLDGGNYH VYENGSLEIK MIRKEDQGIY TCVATNILGK AENQVRLEVK DPTRIYRMPE 550 560 570 580 590 600 DQVAKRGTTV QLECRVKHDP SLKLTVSWLK DDEPLYIGNR MKKEDDSLTI FGVAERDQGS 610 620 630 640 650 660 YTCMASTELD QDLAKAYLTV LADQATPTNR LAALPKGRPD RPRDLELTDL AERSVRLTWI 670 680 690 700 710 720 PGDDNNSPIT DYVVQFEEDQ FQPGVWHDHS KFPGSVNSAV LHLSPYVNYQ FRVIAVNEVG 730 740 750 760 770 780 SSHPSLPSER YRTSGAPPES NPSDVKGEGT RKNNMEITWT PMNATSAFGP NLRYIVKWRR 790 800 810 820 830 840 RETRETWNNV TVWGSRYVVG QTPVYVPYEI RVQAENDFGK GPEPETVIGY SGEDYPRAAP 850 860 870 880 890 900 TEVKIRVLNS TAISLQWNRV YPDTVQGQLR EYRAYYWRES SLLKNLWVSQ KRQQASFPGD 910 920 930 940 950 960 RPRGVVGRLF PYSNYKLEMV VVNGRGDGPR SETKEFTTPE GVPSAPRRFR VRQPNLETIN 970 980 990 1000 1010 1020 LEWDHPEHPN GILIGYTLRY VPFNGTKLGK QMVENFSPNQ TKFSVQRADP VSRYRFSLSA 1030 1040 1050 1060 1070 1080 RTQVGSGEAA TEESPTPPNE ATPTAAYTNN QTDIATQGWF IGLMCAIALL VLILLIVCFI 1090 1100 1110 1120 1130 1140 KRSRGGKYPV REKKDVPLGP EDPKEEDGSF DYSDEDNKPL QGSQTSLDGT IKQQESDDSL 1150 1160 1170 1180 VDYGEGGEGQ FNEDGSFIGQ YTVRKDKEET EGNESSEATS PVNAIYSLA
	Isoform 3 (NF155) (155 kDa isoform) [UniParc]. Checksum: B9FF83D9A2C20F30	FASTA	1,174	132,228
	10 20 30 40 50 60 MARQQAPPWV HVALILFLLS LGGAIEIPMD LTQPPTITKQ SVKDHIVDPR DNILIECEAK 70 80 90 100 110 120 GNPAPSFHWT RNSRFFNIAK DPRVSMRRRS GTLVIDFRSG GRPEEYEGEY QCFARNKFGT 130 140 150 160 170 180 ALSNRIRLQV SKSPLWPKEN LDPVVVQEGA PLTLQCNPPP GLPSPVIFWM SSSMEPITQD 190 200 210 220 230 240 KRVSQGHNGD LYFSNVMLQD MQTDYSCNAR FHFTHTIQQK NPFTLKVLTN NPYNDSSLRN 250 260 270 280 290 300 HPDIYSARGV AERTPSFMYP QGTSSSQMVL RGMDLLLECI ASGVPTPDIA WYKKGGDLPS 310 320 330 340 350 360 DKAKFENFNK ALRITNVSEE DSGEYFCLAS NKMGSIRHTI SVRVKAAPYW LDEPKNLILA 370 380 390 400 410 420 PGEDGRLVCR ANGNPKPTVQ WLVNGDPLQS APPNPNREVA GDTIIFRDTQ ISSRAVYQCN 430 440 450 460 470 480 TSNEHGYLLA NAFVSVLDVP PRMLSPRNQL IRVILYNRTR LDCPFFGSPI PTLRWFKNGQ 490 500 510 520 530 540 GSNLDGGNYH VYENGSLEIK MIRKEDQGIY TCVATNILGK AENQVRLEVK DPTRIYRMPE 550 560 570 580 590 600 DQVAKRGTTV QLECRVKHDP SLKLTVSWLK DDEPLYIGNR MKKEDDSLTI FGVAERDQGS 610 620 630 640 650 660 YTCMASTELD QDLAKAYLTV LGRPDRPRDL ELTDLAERSV RLTWIPGDDN NSPITDYVVQ 670 680 690 700 710 720 FEEDQFQPGV WHDHSKFPGS VNSAVLHLSP YVNYQFRVIA VNEVGSSHPS LPSERYRTSG 730 740 750 760 770 780 APPESNPSDV KGEGTRKNNM EITWTPMNAT SAFGPNLRYI VKWRRRETRE TWNNVTVWGS 790 800 810 820 830 840 RYVVGQTPVY VPYEIRVQAE NDFGKGPEPE TVIGYSGEDY PRAAPTEVKI RVLNSTAISL 850 860 870 880 890 900 QWNRVYPDTV QGQLREYRAY YWRESSLLKN LWVSQKRQQA SFPGDRPRGV VGRLFPYSNY 910 920 930 940 950 960 KLEMVVVNGR GDGPRSETKE FTTPEGVPSA PRRFRVRQPN LETINLEWDH PEHPNGILIG 970 980 990 1000 1010 1020 YTLRYVPFNG TKLGKQMVEN FSPNQTKFSV QRADPVSRYR FSLSARTQVG SGEAATEESP 1030 1040 1050 1060 1070 1080 TPPNEATPTA AYTNNQTDIA TQGWFIGLMC AIALLVLILL IVCFIKRSRG GKYPVREKKD 1090 1100 1110 1120 1130 1140 VPLGPEDPKE EDGSFDYSDE DNKPLQGSQT SLDGTIKQQE SDDSLVDYGE GGEGQFNEDG 1150 1160 1170 SFIGQYTVRK DKEETEGNES SEATSPVNAI YSLA

References

[1]	Tait S., Collinson J.M., Brophy P.J. Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Strain: Wistar.
[2]	"Molecular composition of the node of Ranvier: identification of ankyrin-binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-) and NrCAM at nodal axon segments." Davis J.Q., Lambert S., Bennett V. J. Cell Biol. 135:1355-1367(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-1240 (ISOFORMS 1; 2 AND 3), SUBUNIT. Tissue: Brain.
[3]	"Transient expression of neurofascin by oligodendrocytes at the onset of myelinogenesis: implications for mechanisms of axon-glial interaction." Collinson J.M., Marshall D., Gillespie C.S., Brophy P.J. Glia 23:11-23(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF ISOFORMS 2/3.
[4]	"An oligodendrocyte cell adhesion molecule at the site of assembly of the paranodal axo-glial junction." Tait S., Gunn-Moore F., Collinson J.M., Huang J., Lubetzki C., Pedraza L., Sherman D.L., Colman D.R., Brophy P.J. J. Cell Biol. 150:657-666(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF ISOFORMS 1 AND 2/3, INDIRECT ASSOCIATION WITH CNTNAP1, PHOSPHORYLATION, TISSUE SPECIFICITY.
[5]	"Sodium channel beta1 and beta3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain." Ratcliffe C.F., Westenbroek R.E., Curtis R., Catterall W.A. J. Cell Biol. 154:427-434(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCN1B AND SCN3B.
[6]	"Gliomedin mediates Schwann cell-axon interaction and the molecular assembly of the nodes of Ranvier." Eshed Y., Feinberg K., Poliak S., Sabanay H., Sarig-Nadir O., Spiegel I., Bermingham J.R. Jr., Peles E. Neuron 47:215-229(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH GLDN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY061639 mRNA. Translation: AAL27854.1. U81035 mRNA. Translation: AAB47753.1. U81036 mRNA. Translation: AAB47754.1.
IPI	IPI00206666. IPI00209287. IPI00231463.
RefSeq	NP_001153785.1. NM_001160313.1. NP_001153786.1. NM_001160314.1. NP_446361.1. NM_053909.2.
UniGene	Rn.3048.
3D structure databases
ProteinModelPortal	P97685.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-205368.
PTM databases
PhosphoSite	P97685.
Proteomic databases
PaxDb	P97685.
PRIDE	P97685.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	116690.
KEGG	rno:116690.
UCSC	RGD:620911. rat.
Organism-specific databases
CTD	23114.
RGD	620911. Nfasc.
Phylogenomic databases
eggNOG	NOG293951.
HOGENOM	HOG000231380.
HOVERGEN	HBG000144.
InParanoid	P97685.
KO	K06757.
OrthoDB	EOG418BMK.
Enzyme and pathway databases
Reactome	REACT_96538. Developmental Biology.
Gene expression databases
ArrayExpress	P97685.
Genevestigator	P97685.
GermOnline	ENSRNOG00000030515. Rattus norvegicus.
Family and domain databases
Gene3D	2.60.40.10. 10 hits.
InterPro	IPR026966. Fibronectin_III_C. IPR003961. Fibronectin_type3. IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. IPR013098. Ig_I-set. IPR003599. Ig_sub. IPR003598. Ig_sub2. IPR026965. NFASC. [Graphical view]
PANTHER	PTHR10489:SF41. PTHR10489:SF41. 1 hit.
Pfam	PF13882. Bravo_FIGEY. 1 hit. PF00041. fn3. 4 hits. PF07679. I-set. 4 hits. [Graphical view]
SMART	SM00060. FN3. 4 hits. SM00409. IG. 2 hits. SM00408. IGc2. 4 hits. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 4 hits.
PROSITE	PS50853. FN3. 4 hits. PS50835. IG_LIKE. 6 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	619556.

Entry information

Entry name

NFASC_RAT

Accession

Primary (citable) accession number: P97685
Secondary accession number(s): P97684, Q91Z60

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	November 14, 2003
Last modified:	May 29, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program