ID A0A498P4N0_LABRO Unreviewed; 1134 AA.
AC A0A498P4N0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 08-OCT-2025, entry version 19.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X2 {ECO:0000313|EMBL:RXN38998.1};
GN ORFNames=ROHU_000648 {ECO:0000313|EMBL:RXN38998.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN38998.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN38998.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN38998.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN38998.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN38998.1}.
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DR EMBL; QBIY01003913; RXN38998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498P4N0; -.
DR STRING; 84645.A0A498P4N0; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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 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:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 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 1: Evidence at protein level;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:RXN38998.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498P4N0};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1134
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019730887"
FT DOMAIN 91..282
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 40..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..58
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..418
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..492
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..538
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..672
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..712
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..731
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..814
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..834
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..854
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..925
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1134 AA; 116250 MW; DCE79BE33C839820 CRC64;
MVAPVLPLTC LVLLSLVSVS SQIQWLKFLW VPETTSPAAA VTTPAPTTTA PEESTAPVFP
AFPPQPTEGS SKARTKRPLK MWKSERGSKG HLVLTELVGV PLPPSVSFIT GYEGFPAYHF
GSKANVGRLT QTFVPEPFFL DFAIIVTVKP SSSRGGVLFA ITDPSQKIIH LGLALTPVED
KTQKIVFYYS EPGLADSMEV ASFKVPDMTQ QWNRFTLTVE AEEVRLYMDC EKYHSTPLKR
SQQPLSFKPG SGIFVANAGG TDLERFVGLT KQMKQGRVQG MVLARGKKGS VENLDLLAPQ
DPLALLDRLS LQHIQGQRGY PGPTGLPGES GVKGEKGDPG VGQPGLPGPP GPPGLPGPSK
PIKVPYGFDA LGSGFGDVDV DTELLRGPPG PPGPPGKPGP PGPNSSSGGL LPGPAGAPGK
DGKNGQPGLP GVPGQDGLTG QQGLKGAKGE QGIRGPPGPK GENGDPGPIG PMGPRGVPGP
PGIPGPPGPP GPSSNNFMKD TLKGLPGADG APGLSVKGEP GSPGKDGIPG LAGLPGARGP
KGDKGSPGQK GERGRDGLSI TGPPGPPGPP GTIINLEDLL LNDTAAELNL TKIRGPPGPM
GPRGPKGEIG FPGIQGPPGL KGDRGEPGVS IAADGSLITG LRGPKGPKGM KGDIGPSGQP
GIVGPIGPPG QKGEYGLPGR PGRSGIAGRK GDKGDSSGPP GPPGPPGPPG PPGRVIGLNG
VNNNNSQPGN GRVSYGVKGD KGDVGNPGLP GTSVPMFPDG SVGEKGDNGY KGQKGEKGDP
GLSGLPGRTG LVGPKGDSIV GPPGDAGPPG PPGRPGYGSP GPQGPPGPPG PPGTPSGSAV
SLPGPPGPPG PPGAPGHGNS VRSYENSQTL IRETSQTAEG TLAYVIDKSE LFIRVRGGWK
KVELGELIPV PQDSSSSALS QGLSRPSDRS VPRVHSQELN SFLPDYHVFP QNGHSVPALH
LVALNAPFSG DMHGIRGADY QCYQQARARG LTSTYRAFLS SHLQDISSIV KKGDRFSLPV
VNLKGDVLFS SWMAMFSGNG AVFDPLTPIY SFDGRNVMTD QAWSQKLVWH GSSTAGIRMT
TSYCEAWRTG DMAVTGQASL LQTGRLLGQH TRSCSNHFIV LCIENSYIQN PGRN
//
