ID F7ADD9_CIOIN Unreviewed; 950 AA.
AC F7ADD9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 28-JAN-2026, entry version 81.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCINP00000019538.3};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000019538.3, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000019538.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wild type {ECO:0000313|Ensembl:ENSCINP00000019538.3};
RX PubMed=18854010; DOI=10.1186/gb-2008-9-10-r152;
RA Satou Y., Mineta K., Ogasawara M., Sasakura Y., Shoguchi E., Ueno K.,
RA Yamada L., Matsumoto J., Wasserscheid J., Dewar K., Wiley G.B.,
RA Macmil S.L., Roe B.A., Zeller R.W., Hastings K.E., Lemaire P.,
RA Lindquist E., Endo T., Hotta K., Inaba K.;
RT "Improved genome assembly and evidence-based global gene model set for the
RT chordate Ciona intestinalis: new insight into intron and operon
RT populations.";
RL Genome Biol. 9:R152-R152(2008).
RN [3] {ECO:0000313|Ensembl:ENSCINP00000019538.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSCINP00000019538.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EAAA01002980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F7ADD9; -.
DR STRING; 7719.ENSCINP00000019538; -.
DR Ensembl; ENSCINT00000019538.3; ENSCINP00000019538.3; ENSCING00000009609.3.
DR GeneTree; ENSGT00980000198702; -.
DR HOGENOM; CLU_014222_0_0_1; -.
DR InParanoid; F7ADD9; -.
DR OMA; YSHERPY; -.
DR Proteomes; UP000008144; Chromosome 9.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR Gene3D; 3.40.1620.70; -; 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; 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 SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000008144}.
FT DOMAIN 678..723
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 776..942
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 57..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..187
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..223
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..294
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..449
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..480
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..583
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..647
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..657
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 94794 MW; 10609186A8DAC767 CRC64;
MPASLPVTTN SPIDPKTLAL TVASFEPTTS KSMPLVGSVD HRASDRIIQP GLFPVSAVKG
EKGEPGRNGE NGIGVPGAAG EVGQKGEAGA DSVVAGSPGE RGPKGEPGIP GKDGVSLGAG
GVGEKGEKGD QGPMGEQGVG IAGQKGEAGE IGKDGLPGDV GLPGADGVAG PAGAKGEKGV
PGVPGVDGSQ GVGLPGADGA KGEKGEVGKA VSVTGPAGAA GPPGVQGEKG EPGEDGDDGE
DGEDGEKGDR GPPGVGIRGP AGPPGTFSAA FADMEGSCFS SMPGEPGPPG PMGPQGPAGV
DGVGKDGEKG DKGDKGDIGP QGPAGKDGVS GPEGQMGIPG PVGAAGPKGE PGEDGRAGLP
GPPGLPGVCE KSDAKMPTDD EDLMEGSGNV EFKKKFSARF TAGLPGVPGV PGPEGRAGLP
GPHGPAGPQG PQGPQGLQGA QGPSGLQGPK GMTGASGEHG AEGPAGVPGA VGPQGNPGVN
GRDGAAGTPG LDGEPGIQGM KGDTGSQGPP GPPGPSAVAT TNAEPLTSVV KGEKGEPGAV
IGPDGNVLSA GQKGEPGTPG PMGPPGLSGS AGSKGDMGMP GRRGTPGRHG RDGAEGPPGP
PGSSSGIFGG SSGEKGDKGE RGFDGSKGAP GVAGEAGIPG RTGRSGPSGP PGPPGPPGRS
NQHDTRSAAL IENTMMTSFP SVAEMQANYQ TTAEGTLAFV VNREEMFVKT TLGWRQVMLS
RPIPPPRVEV ATLEPETVAT TTRAPIVPEV TTTTTTRRTT TTPAATPVVS TSQKSLHMIA
LNFPLRGNTR GIVGADARCF QQARRAGLKG TYRAFLSSRD QNVRSIVRRE DRRNVPIVNI
RGEQLFSSWE ELFRTEGRMD NPNMIYSFEN RQVSTDARWP VKFVWHGSYT DGRLNPMHYC
ASWYTDHKAV TGQASPLSTR RLLAQKPYSC ESGFVVLCVE NSTRTLRYKR
//