ID A0A6J2UTV0_CHACN Unreviewed; 1268 AA.
AC A0A6J2UTV0;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|RefSeq:XP_030623489.1};
GN Name=col15a1a {ECO:0000313|RefSeq:XP_030623489.1};
OS Chanos chanos (Milkfish) (Mugil chanos).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gonorynchiformes;
OC Chanidae; Chanos.
OX NCBI_TaxID=29144 {ECO:0000313|Proteomes:UP000504632, ECO:0000313|RefSeq:XP_030623489.1};
RN [1] {ECO:0000313|RefSeq:XP_030623489.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_030623489.1; XM_030767629.1.
DR AlphaFoldDB; A0A6J2UTV0; -.
DR GeneID; 115806765; -.
DR CTD; 792366; -.
DR InParanoid; A0A6J2UTV0; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000504632; Chromosome 3.
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 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; 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:SF372; COLLAGEN ALPHA-1(XVI) CHAIN; 1.
DR Pfam; PF01391; Collagen; 3.
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 ECO:0000313|RefSeq:XP_030623489.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000504632};
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..1268
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026709280"
FT DOMAIN 30..218
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 216..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..289
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..388
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..587
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..629
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..699
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..819
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..832
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..970
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..992
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1268 AA; 130473 MW; ADC405AFB3DEC082 CRC64;
MAFNSLSLSL SFCPSLSLSV SLPERGSSGQ LDLTELIGVP LPPSVSFITG FEGFPAYSFG
PDANVGRLTR SFIPDPFYRD FAIIVTAKPT SRRGGVLFAI TDAPQKIVHL GVALSPVEDG
AQRVVLYYTE PGKSQTREAA SFKMGELTGR WARFTLAVQG EEVKLYMDCE EHHRVAFYRG
QERLTFQPSS GIFVGNAGGT RMERFVGSIQ QLVLSPDPTT VDEQCEEDDP YASGYSSGDD
ILDDTETMDE VKKIVEEMEY TMPEDLQTTP VRAPPTEASL DDEDMEESSG QDLVLPTEKA
PSRTEEAAHR EKTEQTKNVS PSQKGDRGDP GPPGPPGPPG PPGPSSPAGE GSGTGEPGAR
GPQGPPGAPG TPGKDGEPGV RGGDGDPGQA GPPGFPGLPG EPGLKGDKGD PGVGVPGPPG
PPGPPGRPGT SKFLDAIDGS GFEDFDSDTE VIRGPPGPPG PPGQPGPPGP AQDPIPGPTG
PPGAPGKDGK DGEMGKPGLP VFEDWFSGSG FEFGSGYEFG SGLDSVEGVD GHNGEPGKQG
ERGEKGDPGL PGPAGPKGDP GQPGPDGPQG PRGPVGPPGP PGPPGPPALG FRFNLEVSDT
EGSGGASGFG AAMPTGPPGP PGIPGPPGPK GKDGKDGLPG VSVKGEPGAK GADGQPGIPG
LPGKNGEKGE KGDMGLKGER GQDGLSLPGP PGPPGPPGPV INLPDLLLND TEGIFNFSGT
LGPQGPMGPR GPKGDMGTPG VKGQKGEPGI TISADGALMS GLIGPQGPKG TKGDCGVPGP
PGQIGQMGPP GAKGEFGLPG RPGRPGLIGP KGAKGEPSGL PGPPGPPGPP GRPGIFNCPK
GTVFPIPPRP HCKQPINSNS TQGGANCPLT GAKGEKGDRG LPGLPGISTV PMWTKGASGD
QGFKGEKGEK GEAGMPGPPG VPGRSGLVGP KGDSVVGPPG HPGLRGPPGT PGIGRPGPAG
PPGPPGPPGQ PGHYGAAVTI PGPPGPPGPP GRPAENSNQL KTYSSLQVMK RQAYLDTDGT
LSYVTDTGKL YIRVPGGWKE IQLGGLIEIQ SSTFLSQDEA QPLVFSPQFS STPRIHTRNV
LRLVALNTPY TGNMGSIHTV NKACRAQAQA MGIRDEYRAF LSHHLQDLID LVHPAYRTNM
PVVNLRGEIL FKNWESIFIN HLLPPGIPLF SFDGRDVMSD PFWPQKAIWH GSSERGKRLD
EQNCESWRAG DMAIVGQASF LYSGLLNQQS RSCSNQFIVL CIETSPEDQS AQGLKRAQYR
YQYWHYRN
//
