FINC_CANLF
ID FINC_CANLF Reviewed; 2208 AA.
AC Q28275; Q28276;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Fibronectin {ECO:0000250|UniProtKB:P02751};
DE Short=FN;
DE Flags: Fragment;
GN Name=FN1 {ECO:0000250|UniProtKB:P02751};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1737-2131 (ISOFORM 2), FUNCTION, AND
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1737-2132 (ISOFORM 1).
RC TISSUE=Cartilage;
RX PubMed=8702559; DOI=10.1074/jbc.271.31.18954;
RA Macleod J.N., Burton-Wurster N., Gu D.N., Lust G.;
RT "Fibronectin mRNA splice variant in articular cartilage lacks bases
RT encoding the V, III-15, and I-10 protein segments.";
RL J. Biol. Chem. 271:18954-18960(1996).
CC -!- FUNCTION: Fibronectins bind cell surfaces and various compounds
CC including collagen, fibrin, heparin, DNA, and actin. Fibronectins are
CC involved in cell adhesion, cell motility, opsonization, wound healing,
CC and maintenance of cell shape (By similarity). Involved in osteoblast
CC compaction through the fibronectin fibrillogenesis cell-mediated matrix
CC assembly process, essential for osteoblast mineralization. Participates
CC in the regulation of type I collagen deposition by osteoblasts (By
CC similarity). {ECO:0000250|UniProtKB:P02751,
CC ECO:0000250|UniProtKB:P11276}.
CC -!- FUNCTION: [Isoform 2]: Probably involved in matrix organization of
CC cartilage. {ECO:0000269|PubMed:8702559}.
CC -!- SUBUNIT: Mostly heterodimers or multimers of alternatively spliced
CC variants, connected by 2 disulfide bonds near the carboxyl ends; to a
CC lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and
CC COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP.
CC Interacts (via type III repeats 9-14) with TNFAIP6 (via CUB domain);
CC this interaction enhances fibronectin fibril assembly. TNFAIP6 may act
CC as a bridging molecule between FN1 and THBS1 (By similarity). Interacts
CC with TNR; the interaction inhibits cell adhesion and neurite outgrowth
CC (By similarity). Interacts with FST3 and MYOC (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P02751}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=A number of isoforms are produced. The diversity of isoforms
CC depends on the V region and either of the two extra domains which can
CC be either included or excluded (partially or completely for the V
CC region). {ECO:0000305};
CC Name=3;
CC IsoId=Q28275-4; Sequence=Displayed;
CC Name=1;
CC IsoId=Q28275-1; Sequence=VSP_060854, VSP_060855, VSP_060857;
CC Name=2; Synonyms=(V+C)-;
CC IsoId=Q28275-3; Sequence=VSP_060854, VSP_060856;
CC -!- TISSUE SPECIFICITY: Plasma FN (soluble dimeric form) is secreted by
CC hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms),
CC made by fibroblasts, epithelial and other cell types, is deposited as
CC fibrils in the extracellular matrix. Isoform 2 is the major transcript
CC in articular cartilage, but it is absent from liver.
CC -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P02751}.
CC -!- PTM: Forms covalent cross-links mediated by a transglutaminase, such as
CC F13A or TGM2, between a glutamine and the epsilon-amino group of a
CC lysine residue, forming homopolymers and heteropolymers (e.g.
CC fibrinogen-fibronectin, collagen-fibronectin heteropolymers).
CC {ECO:0000250|UniProtKB:P11276}.
CC -!- PTM: Some lysine residues are oxidized to allysine by LOXL3, promoting
CC fibronectin activation and matrix formation.
CC {ECO:0000250|UniProtKB:P11276}.
CC -!- PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia.
CC {ECO:0000250|UniProtKB:P07589}.
CC -!- MISCELLANEOUS: [Isoform 2]: Lacks repeat 15 of fibronectin type-III,
CC repeat 10 of fibronectin type-I, and the connecting strand 3.
CC {ECO:0000305}.
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DR EMBL; AAEX00000000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U52105; AAC48611.1; -; mRNA.
DR EMBL; U52106; AAC48612.1; -; mRNA.
DR AlphaFoldDB; Q28275; -.
DR SMR; Q28275; -.
DR CORUM; Q28275; -.
DR STRING; 9615.ENSCAFP00000066679; -.
DR PaxDb; Q28275; -.
DR PRIDE; Q28275; -.
DR Ensembl; ENSCAFT00030032444; ENSCAFP00030028299; ENSCAFG00030010199. [Q28275-4]
DR eggNOG; ENOG502QPTS; Eukaryota.
DR InParanoid; Q28275; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd00061; FN1; 11.
DR CDD; cd00062; FN2; 2.
DR CDD; cd00063; FN3; 15.
DR Gene3D; 2.10.10.10; -; 2.
DR Gene3D; 2.60.40.10; -; 16.
DR InterPro; IPR000083; Fibronectin_type1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013806; Kringle-like.
DR Pfam; PF00039; fn1; 12.
DR Pfam; PF00040; fn2; 2.
DR Pfam; PF00041; fn3; 15.
DR SMART; SM00058; FN1; 12.
DR SMART; SM00059; FN2; 2.
DR SMART; SM00060; FN3; 16.
DR SUPFAM; SSF49265; SSF49265; 10.
DR SUPFAM; SSF57440; SSF57440; 2.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01253; FN1_1; 10.
DR PROSITE; PS51091; FN1_2; 12.
DR PROSITE; PS00023; FN2_1; 2.
DR PROSITE; PS51092; FN2_2; 2.
DR PROSITE; PS50853; FN3; 15.
PE 2: Evidence at transcript level;
KW Acute phase; Alternative splicing; Cell adhesion; Cell shape;
KW Disulfide bond; DNA-binding; Extracellular matrix; Glycoprotein;
KW Heparin-binding; Isopeptide bond; Oxidation; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted;
KW Sulfation.
FT CHAIN <1..2208
FT /note="Fibronectin"
FT /id="PRO_0000158528"
FT DOMAIN 27..67
FT /note="Fibronectin type-I 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 72..115
FT /note="Fibronectin type-I 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 116..159
FT /note="Fibronectin type-I 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 161..205
FT /note="Fibronectin type-I 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 206..250
FT /note="Fibronectin type-I 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 283..322
FT /note="Fibronectin type-I 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 332..380
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 392..440
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 421..475
FT /note="Fibronectin type-I 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 480..522
FT /note="Fibronectin type-I 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 523..566
FT /note="Fibronectin type-I 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 574..669
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 681..776
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 777..866
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 873..964
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 965..1052
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1053..1139
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1140..1234
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1235..1323
FT /note="Fibronectin type-III 8; extra domain B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1324..1414
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1415..1505
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1506..1581
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1583..1673
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1674..1766
FT /note="Fibronectin type-III 13; extra domain A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1767..1856
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1857..1949
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2025..2071
FT /note="Fibronectin type-I 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2072..2114
FT /note="Fibronectin type-I 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2116..2156
FT /note="Fibronectin type-I 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DNA_BIND 871..1136
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..249
FT /note="Fibrin- and heparin-binding 1"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 285..572
FT /note="Collagen-binding"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 662..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1581
FT /note="Cell-attachment"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 1447..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2040..2160
FT /note="Fibrin-binding 2"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOTIF 1565..1567
FT /note="Cell attachment site"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT COMPBIAS 1447..1462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 627
FT /note="Important for superfibronectin formation"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT SITE 630
FT /note="Important for superfibronectin formation"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOD_RES 840
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 845
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 2185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOD_RES 2206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 841
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 971
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 29..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 53..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 74..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 100..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 118..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 144..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 163..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 190..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 208..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 235..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 285..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 310..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 337..363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 351..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 397..423
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 411..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 423..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 460..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 482..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 507..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 525..553
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 551..563
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2056..2068
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2074..2101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2099..2111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2118..2144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2142..2153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT CROSSLNK 18
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P11276"
FT CROSSLNK 19
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P11276"
FT VAR_SEQ 1848..1864
FT /note="RLTFVFFQPLMHHPTCV -> ASTAIDAPSNLR (in isoform 2 and
FT isoform 1)"
FT /id="VSP_060854"
FT VAR_SEQ 1944
FT /note="K -> KTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFITNPGYDTGNGIQL
FT PGTSGQQPSVGQQMIFEEHGFRRTTPPTTATPVRHRPRPYPPNVNEEIQVGHVPRGDVD
FT HHLYPHVMGLNPNAS (in isoform 1)"
FT /id="VSP_060855"
FT VAR_SEQ 1945..2072
FT /note="TGQEALSQTTISWTPFQESSEYIISCHPVGIDEEPLQFRVPGTSASATLTGL
FT TRGATYNIIVEALKDQKRHKVREEVVTVGNSVDQGLNQPTDDSCFDPYTRLSESGFKLS
FT CQCLGFGSGHFRCDSSK -> TE (in isoform 2)"
FT /id="VSP_060856"
FT VAR_SEQ 2045
FT /note="T -> TVSHYAIGEEWE (in isoform 1)"
FT /id="VSP_060857"
FT CONFLICT 2130
FT /note="Q -> H (in Ref. 2; AAC48612)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 2208 AA; 243226 MW; 1F5380A3D7921513 CRC64;
LGAALRSAGA ARGRRQAQQI VQPPGPPGCY DNGKHYQINQ QWERTYLGNA LVCTCYGGSR
GFNCESKPEP EETCFDKYTG NTYRVGDTYE RPKDSMIWDC TCIGAGRGRI SCTIANRCHE
GGQSYKIGDT WRRPHETGGY MLECVCLGNG KGEWTCKPIA EKCFDHAAGT SYVVGETWEK
PYQGWMMVDC TCLGEGSGRI TCTSRNRCND QDTRTSYRIG DTWSKKDNRG NLLQCICTGN
GRGEWKCERH ASLQTTSTGS GPFTDVRTAI YQPQPHPQPA PYGHCVTDSG VVYSVGMQWL
KTQGNKQMLC TCLGNGVSCQ ETAVTQTYGG NSNGEPCVLP FTYNGRTFYS CTTEGRQDGH
LWCSTTSNYE QDQKYSFCTD HTVLVQTRGG NSNGALCHFP FLYNNHNYTD CTSEGRRDNM
KWCGTTPNYD ADQKFGFCPH AHEEICTTNE GHDMGHMMRC TCVGNGRGEW TCVAYSQLRD
QCIVDDITYN VNDTFHKRHE EGHMLNCTCF GQGRGRWKCD PIDQCQDSET RTFYQIGDSW
EKYVHGVRYQ CYCYGRGIGE WHCQPLQTYP GTTGPVQVII TETPSQPNSH PIQWNAPEPS
HISKYILRWK PKNSPGRWKE ATIPGHLNSY TIKGLTPGVV YEGQLISVQH YGHREVTRFD
FTTTSTSPPV TSNTVTGETT PLSPVVATSE SVTEITASSF VVSWVSASDT VSGFRVEYEL
SEEGDEPQYL DLPSTATSVN IPDLLPGRKY IVNVYQISEE GEQSLILSTS QTTAPDAPPD
PAVDRVDDTS IVVRWSRPQA PITGYRIVYS PSVEGSSTEL NLPETANSVT LSDLQPGVQY
NITIYAVEEN QESTPVFIQQ ETTGVPRSDK VPPPRDLQFV EVTDVKITIM WTPPESTVTG
YRVDVIPVNL PGEHGQRLPI NRNTFAEVTG LSPGVTYHFK VFAVNQGRES RPLTAEQTTK
LDAPTNLRFA NETDSTVLVI WTPPRARIAG YRLTVGPTRG GHPKQYNVGP SASQYPLRNL
QPATEYTVSL VAVKGNQQSP KATGVFTTLQ PLSSIPPYNT EVTETTIVIT WTPAPRIGFK
LGVRPSQGGE APREVTSDSG SIVVSGLTPG VEYVYTISVL RDGQERDTPI VKKVVTPLSP
PTNLHLEANP DTGVLTVSWE RSTTPDITGY RITTTPTNGQ QGYSLEEVVH ADQSSCTFEN
LSPGLEYNVS VYTVKDDKES VPISDTIIPE VPQLTDLSFV DITDSSIGLR WTPLNSSTII
GYRITVVAAG EGIPIFEDFV DSSVGYYTVT GLEPGIDYDI SVITLINGGE SAPTTLTQQT
AVPPPTDLRF TNIGPDTMRV TWAPPPSIEL TNFLVRYSPV KNEEDVAELS ISPSDNVVVL
TNLLPGTEYL VSVSSVYEQH ESTPLRGRQK TGLDSPSGID FSDITANSFT VHWIAPRATI
TGYRIRHHPE HTSGRPREDR VPPSRNSITL TNLNPGTEYV VSIIALNGRE ESPPLIGQQS
SLQPPTSLLI SWDAPAVTVR YYRITYGENS PVQEFTVPGS KSTATISGLK PGADYTITVY
AVTGRGDSPA SSKPVSIDYR TGTDSSMQVT DVQDNSISVR WLPSSSPVTG YRVTTTPKNG
PGPSKTKTAG PDQTEMTIEG LQPTVEYVVS VYAQNRNGES QPLVQTAVTT IPAPADLKFT
QVTPTSLTAQ WTAPNVQLTG YRVRVTPKEK TGPMKEINLA PDSSSVVVSG LMVATKYEVS
VYALKDTLTS RPAQGVVTTL ENVSPPRRAR VTDATETTIT ISWRTKTETI TGFQVDAIPA
NGQNPIQRTI RPDVRSYTIT GLQPGTDYKI YLYTLNDNAR SSPVVIDRLT FVFFQPLMHH
PTCVFLATTP NSLLVSWQPP RARITGYIIK YEKPGSPPRE VVPRPRPGVT EATITGLEPG
TEYTIQVIAL KNNQKSEPLI GRKKTGQEAL SQTTISWTPF QESSEYIISC HPVGIDEEPL
QFRVPGTSAS ATLTGLTRGA TYNIIVEALK DQKRHKVREE VVTVGNSVDQ GLNQPTDDSC
FDPYTRLSES GFKLSCQCLG FGSGHFRCDS SKWCHDNGVN YKIGEKWDRQ GENGQMMSCT
CLGNGKGEFK CDPHEATCYD DGKTYHVGEQ WQKEYLGAIC SCTCFGGQRG WRCDNCRRPG
AEPGHEGSTG HYNQYSQRYH QRTNTNVNCP IECFMPLDVQ ADREDSRE
