ID A0A498NCX8_LABRO Unreviewed; 2343 AA.
AC A0A498NCX8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
GN ORFNames=ROHU_018088 {ECO:0000313|EMBL:RXN29944.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN29944.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN29944.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN29944.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN29944.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN29944.1}.
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DR EMBL; QBIY01011684; RXN29944.1; -; Genomic_DNA.
DR STRING; 84645.A0A498NCX8; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
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; 10.
DR CDD; cd00062; FN2; 2.
DR CDD; cd00063; FN3; 13.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 12.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR46708:SF2; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46708; TENASCIN; 1.
DR Pfam; PF00039; fn1; 10.
DR Pfam; PF00040; fn2; 2.
DR Pfam; PF00041; fn3; 14.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00058; FN1; 12.
DR SMART; SM00059; FN2; 2.
DR SMART; SM00060; FN3; 15.
DR SUPFAM; SSF49265; Fibronectin type III; 11.
DR SUPFAM; SSF57603; FnI-like domain; 12.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR PROSITE; PS01253; FN1_1; 5.
DR PROSITE; PS51091; FN1_2; 10.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 2.
DR PROSITE; PS50853; FN3; 14.
PE 1: Evidence at protein level;
KW Acute phase {ECO:0000256|ARBA:ARBA00022486};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498NCX8};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT DOMAIN 77..120
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 121..164
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 166..210
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 211..255
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 341..389
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 401..449
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 454..497
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 502..544
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 545..588
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 669..763
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 764..853
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 874..965
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 966..1054
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1115..1203
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1206..1300
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1301..1387
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1388..1478
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1485..1577
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1578..1667
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1675..1765
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1767..1858
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1861..1953
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2066..2161
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2166..2210
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2211..2253
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2255..2295
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT REGION 1948..2028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2056..2082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 346..372
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 360..387
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 406..432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 420..447
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 2343 AA; 259003 MW; 3A9A9B2510E5314C CRC64;
MPQSAGKNKR HVQEQARLDP VYEEARSLAI HESGCSDNGR FYRKNDQWER QYMDSTLVCT
CEGATGVKCK SKPAAEETCY DKFNARSYRV GQTYERPKDG MIWDCTCIGS GKGKISCTIA
NRCHEGGNSY RIGDTWTRPH DTGDYMLECV CLGNGKGEWT CKPVAERCYD DSLGSSYVVG
QTWQKPYQGW MIVDCTCLGE GNGRITCTSR NRCNDEDTRT SYRIGETWTK TDTSGNTLQC
LCTGNGRGEW KCDRHAASHS TLAIGSGSTM THRVLPVINQ VDVLTDLLEE GNCKTDSGVY
YSNGMSWIRS QGSKEMLCTC IGGGISCEEQ DGQSFVYGGN SGGQQCVFPF VFSGNTHYSC
ISEGRNDGQL WCSTTSDYDS DGMYSFCTRK NQLVTTRGGN SNGALCQFPF KYNGRNYTDC
TSDGRRDSMK WCGTTTDYDG DRKYGFCPMA AHEEVCTVND VMYRVGDEWD KRHDTLGHMM
RCTCQGNGRG EWNCISHTQL RDQCVVNGQT YDVNETFDKR HDQGYMMNCT CFGQGRGRWK
CDAIDQCQEP ETKVFYQIGE TWNKVIQGVP YRCSCYGNGI GELACEPLQS TGGSFEVSQM
GQKNTRTPWK EVTIPGHINS HTISGLKPGL TYEGQLISIL RYGPREVTRF DFTTTYGSLE
KAEGETTQPP RIVDTSESVT EITSSSFVIS WVSASETVSG FRVQYELSEE GAQQNVIDLP
RTATSVNIQD LLPGRRYNVQ VFEVNPEGDK NLILTTTQTT APDAPTNHEV SNVQETSIMI
RWSKPQAPIT GYRVVYTPTV EGSSTELILP ETQTFVTLGD LRPGLSYNVS IYSVEDNMES
QPLVLQVSTA GEQQPVEGKI VILLYITLTE EVQAPTDLQF YEVTDVKITI TWTGPPNEVS
GYRVTFAPVS TDGRAQRPLQ LPVMQNAYAE LTHLQPGTLY RFHIYAVNRG VESEPLIGEK
STKPDVPTDL RFTDITDDSA LVIWSVPRAQ VTGYRLFIST GSSSPKQLRI PGRDSQYKLT
DLQPDTEYLV TLHSEQGNTL SEGVTDAFRT SQPTGNAPRF TTEVTDTAII VTWIPLPRYS
YRMSVRPSQG GEAPRDVTSG DGTIYISGLT PGLEYTYNLQ PLFNGRKHGK PITNKVVTYI
TGYRVTCTPT NGQRGNTLEE FVRGHETSCT LENLSPGVEY NVSVYTIKNH LESEPVSTTV
TQAVPAPTNL NFGEVGADTM RVSWTPPSVQ PSEISRFVIR YHPTKNDDDT QELNIGSAIN
NFVLQNLLPN TEYLVKVVCV YDDRESEPVT GTQKTKLDSP TNLDFSDVST NSFTVHWMAP
RAVITGYRLR YQPTSGGRAK DERLPPTRNY FTLVNLAPET EYTVYIYAVS GNKESLPLTG
TQATVSDAPT DLAVTSSTPT SITISWDAPA VTVRYYKITH GESGERDVPR EFTVPGTQST
ATIQGLRPDT EYTITLYAVT GRGDSPASST PVIITHRTAG GSVPSPSDLD VTDIQDNALT
VRWSPARGPI TGYRVTGTPK DGQGPTFSEL VGPERTEMTI RGLVPTVEYT INVIALSQEG
ESAPVVQKAK TAELQHPRDL TFSDVDSTSM LVTWDVPHVP GVTSYRVLYS SPEEGEREYQ
PAISGRDKSV VLQGLRPGTT YNVKVIPMKG RTAIRTLEGI QQTTYEESQP TAVPAPTEID
FRDISPSSFV VTWQAPNARL SGYRVVVSPK NHYAQPKEMN VAPDSTQVLV PGLMVATAYE
VHVYALRGLE KSSPLTGECT TAENITPPRR VRITDVKDTS FTLSWRVVNN EPMTGFLIEA
TPKTGDYPTF RQTIPAESRT YVVTGLQPSV MYVVNMYTLN GNTRSPPFTM TVTTARPAVQ
PPTNLQFTSL TPSSMSFTWQ PPPTHFTGYY ITYEESGGSP HELTPRPTAG QNYATITGLK
PGTQYTIKIF ALLNNHRSTP LVGTATTQLT SDLPSLPHRG GPDKLDVPEP DNRVHTVGPT
GPDSPDAHGQ HVEYTEYNNQ PSQPNRGYEP HHRHTVPQPN QPRPQPYVPQ VGETLVYIPK
VGPDGGRVPR IIQVSERPGD GNPFAFPEDK TGQPQEAQTQ TTISWQPYQQ SSAYLVSCHP
VTHPNEKMFQ MRVPGTTTSA TLIGLTSGAS YNVIVEALKG ALKHKILEEM VTAGNTVTGD
GSSSKDSCYD TFTATYHDVG AEWERMSETG FKLWCKCLGL GSGHFRCDSS KWCHDSGNNY
RIGEKWERRA ENGHLMSCSC LGNGKGEFKC EPHESICYDD GKMYQVGNQW QKEYLGAICT
CTCYGGQQGW RCENCRRPGA EISSDLLKPV RLNTGQRVNI QCPIECLRPE LLADAVANAK
TGE
//
