ID A0A913ZDA8_PATMI Unreviewed; 1685 AA.
AC A0A913ZDA8;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:XP_038048925.1};
OS Patiria miniata (Bat star) (Asterina miniata).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC Valvatacea; Valvatida; Asterinidae; Patiria.
OX NCBI_TaxID=46514 {ECO:0000313|EnsemblMetazoa:XP_038048925.1, ECO:0000313|Proteomes:UP000887568};
RN [1] {ECO:0000313|EnsemblMetazoa:XP_038048925.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (NOV-2022) 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 RefSeq; XP_038048925.1; XM_038192997.1.
DR EnsemblMetazoa; XM_038192997.1; XP_038048925.1; LOC119722725.
DR GeneID; 119722725; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000887568; Unplaced.
DR GO; GO:0005594; C:collagen type IX trimer; 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 Gene3D; 2.60.120.200; -; 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; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1116; MACROPHAGE RECEPTOR WITH COLLAGENOUS STRUCTURE; 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.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000887568}.
FT DOMAIN 1420..1463
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 1516..1681
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 247..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..509
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..550
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..575
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..622
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..649
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..734
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..788
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..836
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..852
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..878
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..945
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1086
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1212
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1306
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1403
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1490
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1685 AA; 170416 MW; 76FBE9CD57D1E840 CRC64;
MRRGDPAFHL DRDTNIGRLA DYIFPLDFTE RFSDFTLLVT FKPESEDVGP LLVVTDNLQT
TVILALNVTR AEEGRHRVTL LMTDVSAGTP SKASFVVPSL TGHWSQFSLS VINDMATLFF
NCSTYTSTSL MRPEGWKLAI PQQAAVFVGS QGFALDNTAT FAGTIQTLEM SNDPDEAELG
CDDGDQELRK QRLYKRETSS SNLADALITN KDIPTLPTNS KQNGIVFGSA EGSGLKATEE
TEMFSGMFDS TSAPSSETVK PTMTSTGEGI NPNSVSPDFI HGMGSTTEAP TEMRTASVSP
SGITKAASDS PSEMGRTTKT PAEMRTPSSS PSGMETASKA SLEASSKTPD DMGVSSKVTS
GMETASKSSP VAATTSETLV EKPATKKPVT LPRPEPESNT SPITPSVTDS VASASPTMQP
ATLPTMAPTE SPTTQSPSRG PMVTVQDVLS PGMVSDGQDR MTVTPTTPLV RVMSETPVPT
EKDMSTPAGK ATPAPDKATP APDKATPAPV DKVATTVTIA TVAPVTLATP TPIVKVISGS
PGVPGVAGEP GPKGDPGVDG NDGLPGEDGG QGPAGVAGDK GEKGMKGEAG KAGPKGDLGD
PGLSGPTGPE GLPGAAGPPG DKGVQGDTGP IGPGGTKGVK GEPGIGLPGP SGLFVTPDPE
TIRGPKGDQG EKGEAGPKGD KGDQGDIGPV GPEGESGPQG DKGEKGEAGV GLPGPQGSVG
PQGPEGPQGE TGPLAELPEF FDLFEGSGFE DFRGQLGQKG KDGQPGPVGP EGPMGLTGPQ
GPQGIQGAPG PPGMPGVPGT PGRPGTVAMN YTGPDGPCSC RDGLNGSQGP PGIQGPAGPP
GTPGRNGTAG TPGENGKPGV PGIEGPAGMQ GDPGMAGPQG PPGPPGKVYI MPSEMTPTAI
SKMLTDGDAL TGSGFMPLTK SPIDGGGELI TGEPGPPGPQ GPPGPAGERG DRGEIGLLGE
RGPKGDVGPA GPKGMQGIQG DTGPPGPSGK HGKDGREGPQ GKQGEPGIGV RGPKGDVGPE
GPAGTPGKNG SMGSLGLQGP PGPPGPPGEM MIDMDGHMAE RGEKGDRGEV GPPGPTGQKG
DGGLNGIPGF HGDKGDAGER GPAGIDGIDG LKGEMGLKGD TGSEGTPGRD GLNGLPGPRG
PQGPKGDPYV PDDTTMLLYK GMRGPRGPRG PKGHFGIPGR PGSHGDSGPP GLQGPPGING
RPGIGLQGGK GEQGMKGEKG EPAIYGTDGT DTPIALGIKG EKGDSGERGL SGKRGPAGPQ
GVPGFPGVNG LHGPKGLMGD KGEEGRPGAM GHPGVDGVPG GEGPQGLKGE KGDPGIGVQG
DQGRSGSPGP PGFGVPGIDG PEGPRGPPGP PGPPGAQSFP ESPDGSYIPI EGPPGPQGFP
GLDGQQGRPG QTGPQGPQGL QGERGPRGYP GTGSAGQLTS FRSINDMIHQ GASLLPGTIA
FVADVQELYV RKDNGMTQIL LGATFNLDPV QPPLPTTTST PSQQTHSTTE KVVTVPTTKP
NLPGPEIPLG DQPMLYMYAL NKPMTGDRRE GLPGADHHCY QQAQQAGLHG TYRAFLSSKV
QDVRSVVNRD YHHLPVANAK GEIMFESWSG IFNGSEASFD SDKHIYSFNG KDVMTSEEWD
QKYVWHGSYV DGSRMMDSYC EEWRTQDYDA NGQASPLTSH KLLGQETQLC SNALVVLCVQ
VSPDT
//
