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Database: UniProt
Entry: A0A4W4GXF4_ELEEL
LinkDB: A0A4W4GXF4_ELEEL
Original site: A0A4W4GXF4_ELEEL 
ID   A0A4W4GXF4_ELEEL        Unreviewed;      1138 AA.
AC   A0A4W4GXF4;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2025, sequence version 2.
DT   28-JAN-2026, entry version 26.
DE   RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS   Electrophorus electricus (Electric eel) (Gymnotus electricus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC   Gymnotoidei; Gymnotidae; Electrophorus.
OX   NCBI_TaxID=8005 {ECO:0000313|Ensembl:ENSEEEP00000043562.2, ECO:0000313|Proteomes:UP000314983};
RN   [1] {ECO:0000313|Proteomes:UP000314983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24970089;
RA   Gallant J.R., Traeger L.L., Volkening J.D., Moffett H., Chen P.H.,
RA   Novina C.D., Phillips G.N.Jr., Anand R., Wells G.B., Pinch M., Guth R.,
RA   Unguez G.A., Albert J.S., Zakon H.H., Samanta M.P., Sussman M.R.;
RT   "Nonhuman genetics. Genomic basis for the convergent evolution of electric
RT   organs.";
RL   Science 344:1522-1525(2014).
RN   [2] {ECO:0000313|Proteomes:UP000314983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28695212;
RA   Traeger L.L., Sabat G., Barrett-Wilt G.A., Wells G.B., Sussman M.R.;
RT   "A tail of two voltages: Proteomic comparison of the three electric organs
RT   of the electric eel.";
RL   Sci. Adv. 3:e1700523-e1700523(2017).
RN   [3] {ECO:0000313|Ensembl:ENSEEEP00000043562.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Myers G., Meyer A., Fedrigo O., Formenti G., Rhie A., Tracey A., Sims Y.,
RA   Jarvis E.D.;
RT   "Electrophorus electricus (electric eel) genome, fEleEle1, primary
RT   haplotype.";
RL   Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Ensembl:ENSEEEP00000043562.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [5] {ECO:0000313|Ensembl:ENSEEEP00000043562.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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DR   AlphaFoldDB; A0A4W4GXF4; -.
DR   Ensembl; ENSEEET00000044061.2; ENSEEEP00000043562.2; ENSEEEG00000020577.2.
DR   GeneTree; ENSGT00940000158212; -.
DR   Proteomes; UP000314983; Chromosome 2.
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   FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR   FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.40.1620.70; -; 1.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1019; COLLAGEN ALPHA-5(IV) CHAIN ISOFORM X1; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000314983};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1138
FT                   /note="Thrombospondin-like N-terminal domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5044203441"
FT   DOMAIN          61..248
FT                   /note="Thrombospondin-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00210"
FT   REGION          329..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          678..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          884..993
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..347
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..381
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..501
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..558
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..719
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..744
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..764
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..787
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        800..811
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        932..944
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        949..963
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1138 AA;  121568 MW;  7D65B20D532696C5 CRC64;
     MFRHGLWFGL FVLTGLCVGH SCGWFWFDDS KDKDNGEGTQ MPAYVTTVDT TMSTLTTVNS
     CISLLQLVGE PLPEGVTKTS DNSPGYVFST NSKTGQLAHA YLPNPFFHDF SLLFNVKPTS
     KKAGIIFSIT DSYQKIMYVG VKLTAMQGKK QNIVLFYTEP DSQTSYEAAS FSVPSLVGSW
     TRFSISVFEE QVSLYLNCDS DPQVVRFERS PDEMELEDGA GIFIGQAGGA DPDKFVGIIG
     DLKVIGDPRA AERHCEEDED DSDAVSSKVR VTSACNHILT RFIGLPDRDD AIKIIYDFNG
     IWMLKQCTSP CTWTRNPYFL QGAAGFGFPG PKGEPGLPGP PGPPGLPGPI ASVVERGDGS
     VVQRVAGPRG PPGPQGPPGP AGPSGTDGEP VSSCKKHLNG SSLRILASYI LLERTGPPDP
     KSDIIWYFRH SHKISAQLVA ALYVELHTFA CMRLRSHSVQ DDMEGSAVNM FGGVPGVRGP
     EGIQGPPGVP GLPGKSGLPG PKGERGSEGP PGVEGRPGLD GFQGQQGPKG DHGEKGERGE
     PGRDGIGLPG PPGPPGPPGQ VISQPSDDVT TQFEGILCLQ GEKGEPGLVI GPDGSPLYLG
     GLASHKGERG PPGPIGPMGP YGHPGMKGEI GMPGRPGRPG VNGYKGEKGE PGSGAGYGYP
     VRTNFVEYAV FSPALFPTLK GEKGDRGAPG VPGPPGETTM FHELKGEHGE PGLKGDKGEP
     GGSFYDPRFR GVTSPGPPGI PGLPGPKGDS IRGPPGPQGP PGPPGIGYDG RPGNPGPPGP
     PGPPGSPSLP GAYRPTVGIP GPPGPPGPPG LPAQNSGVVI LRTRDIILTA SSRQPEGSLI
     YVVENSELYI RVRDGLRQVT LGVYKPFYRD LDNEVAAVQP PPVVHYSQGH SASSGAEHFA
     HSESASRPIE PPARQPTEKH VREPPPPAPL DPRYDPRYSS HPDTRYQPQP QPDPRYQPQP
     DPRYIPMQPD RYPVTPARRP NLPVHQPEGH MHTSGPGVSS LYRFSFCCFL SQAISADMQP
     FITHRYFHPL QDQLLFNSWE SLFGEGRMKS NTPIYSFDGR DILRDSAWPE KMIWHGSDGK
     GHRQMDNYCE TWRTADSAVL GLASSLQAGQ LLQQTPRSCS GSYIVLCIEN SYITQFKK
//
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