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Database: UniProt
Entry: A0A913X7K4_EXADI
LinkDB: A0A913X7K4_EXADI
Original site: A0A913X7K4_EXADI 
ID   A0A913X7K4_EXADI        Unreviewed;      1599 AA.
AC   A0A913X7K4;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   28-JAN-2026, entry version 12.
DE   RecName: Full=Fibronectin type-III domain-containing protein {ECO:0000259|PROSITE:PS50853};
OS   Exaiptasia diaphana (Tropical sea anemone) (Aiptasia pulchella).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Aiptasiidae; Exaiptasia.
OX   NCBI_TaxID=2652724 {ECO:0000313|EnsemblMetazoa:XP_020899697.1, ECO:0000313|Proteomes:UP000887567};
RN   [1] {ECO:0000313|EnsemblMetazoa:XP_020899697.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (NOV-2022) to UniProtKB.
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DR   RefSeq; XP_020899697.1; XM_021044038.2.
DR   EnsemblMetazoa; XM_021044038.2; XP_020899697.1; LOC110238366.
DR   GeneID; 110238366; -.
DR   KEGG; epa:110238366; -.
DR   OMA; KEINCDK; -.
DR   OrthoDB; 10060752at2759; -.
DR   Proteomes; UP000887567; Unplaced.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR   CDD; cd00063; FN3; 1.
DR   FunFam; 2.60.40.10:FF:000028; Neuronal cell adhesion molecule; 1.
DR   Gene3D; 3.40.1620.70; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR050149; Collagen_superfamily.
DR   InterPro; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR   Pfam; PF01391; Collagen; 5.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   Pfam; PF00041; fn3; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000887567};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          251..343
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..1340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..441
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..464
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..561
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..651
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..743
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..794
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..815
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..920
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..949
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        983..1010
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1049..1062
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1085
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1088..1110
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1177..1190
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1255..1273
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1297..1323
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1599 AA;  159007 MW;  66D186CA6B82B100 CRC64;
     MSTSVPDVTT GDISTSAPGV TTGDISTGAA SVTTGDMTPS AAGVTTGDMS TASPAVTTGD
     LSSSALGVTT GDISTGAASV TTGVMTPSAA GVTTGDMSSV SPAVSTGNMT RASTFASIPP
     TPSSITTEEK TIKTTIYTKD WSVTITLSVV LPDLKXIHEN LSPSSELYRL LSKPILTNVE
     KFASNFESFV YAKLISVSRR SGSAVATVEL RFSSLKKNEL IDLVEVLEDN RAIEELAVGS
     SNITADKVPS APIGVQVHSI SPTVAKVLWE PIALNSRHXS LLGYKVYYRA ANSKKWNTAS
     CNCTNVSVKN LKPNVKYRIR VFALTTNGNG IPSPALEVIT GQGIGAAATT VKPISTAPSC
     AVTCPKGEKG DRGSIGLPGL PGQTVYLSSN NGTVHLVKGS KGEPGSCSTN CSSMLKIRGP
     KGEPGKSIVG PPGKPGNPGP PGVSGQPGAS GLPGTPGAPG LPATYINMTT GEVIRILQGQ
     KGQQGFNGSK GETGFKGDKG ITGSDGXKGE KGQDGRPGPQ GKRGLIGLPG KSLPGPQGKP
     GPVGIKGEKG DPGAPKGEKG SEGPPGSIGI KGDKGESVTG PPGPPGPPGD GSITNGHSTC
     SCPPGPKGVT GLTGQSGRDG LKGESGEKGQ KGEIGEPGIP APISPPFPGP PGLKGVKGEP
     GDPGYPGLRG EIGLQGPPGF KGESGQVGIK GTPGIPGTKG DRGNAGRIGF PGIKGSPGEP
     GPVGPTGAAG KSGGKGEKGE RGIKGATGTN GLKGEPGVPG IQGEQGVIGS AGEKGAKGDR
     GLAGIKGEKG DEGIGIKGAQ GSPGTSGTQG PRGRQGPPGP PGLVAFVKGA KGEIGLTGKP
     GTPGEKGNEG DEGQKGSQGI KGEQGSKGEV GATGPRGKPG LVIPGPSGPQ GPPGSKGSSG
     EKGSTGEAGL KGPIGPPGLK GSKGEIGPVG PKGKSIQGXP GPPGPPGPPG LITEVLIPGQ
     GQQKGGVSKG QKGNPGRPGF PGQPGTDGEP GEPGLXGPPG DLGPQGLEGP IGQKGRKGEI
     GSPGKQGLQG IAGRPGQKGA VGPQGDRGLS GPPGIPGQSG PSGDKGTRGA VGPAGERGEK
     GDKGESGQPG PAGAQGQKGT AGKQGPQGPV GLPGPQGPPG LDGEAGRKGE KGNQGFGVKG
     IKGEKGSMGP RGANGFPGRK GAKGDFGQSG LPGPAGEPGV SGLPGSVGPP GRKGERGDTG
     PIGIRGEKGE VGSPGVPGKD GLVGIPGQTG VKGEAGDRGN DGANGAKGDK GTKGQDGQPG
     VKGSPGDVTT VVGPPGPPGP PGLSTIKNEN GTIIRGPPGP PGPKSLIPGP PGPPGPPGSP
     GPPGDSKRSV GKTPVDIPGM KTMEHGVVTF DSLNNMIQSA PAVFAGTIAF VLSEQRLYVK
     TSTGWRLVLV GPLVIGQTPT DQIYVTQEPS NGMLILPQPG IRLTGRYLRL IALNYPITGQ
     MGTLAGIDGQ CWKQSRKAGF IGGFRAFLSN TLQHIYTVVP RGERDLPVAN LKGEQIFSSW
     RKLFAKHLAF NPKTPIYSFD GEDVNKSKRW STKYFWHGSK NDGRKAEENC GSWQSRSGKD
     LSTASALDGS SAILDEQYYT CDNRFAVLCI QTSHNTFRK
//
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