ID H2MHG7_ORYLA Unreviewed; 1233 AA.
AC H2MHG7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Collagen type XVIII alpha 1 chain a {ECO:0000313|Ensembl:ENSORLP00000018074.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000018074.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000018074.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000018074.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000018074.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000018074.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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 AlphaFoldDB; H2MHG7; -.
DR STRING; 8090.ENSORLP00000018074; -.
DR Ensembl; ENSORLT00000018075.2; ENSORLP00000018074.2; ENSORLG00000014422.2.
DR eggNOG; KOG3544; Eukaryota.
DR eggNOG; KOG3546; Eukaryota.
DR GeneTree; ENSGT00940000158212; -.
DR HOGENOM; CLU_004003_1_0_1; -.
DR InParanoid; H2MHG7; -.
DR TreeFam; TF315821; -.
DR Proteomes; UP000001038; Chromosome 21.
DR Bgee; ENSORLG00000014422; Expressed in sexually immature organism and 14 other cell types or tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR CDD; cd00247; Endostatin-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 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; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR PANTHER; PTHR24637:SF422; GENE, 37797-RELATED; 1.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1233
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017274190"
FT DOMAIN 238..356
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 98..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..604
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..766
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..869
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..895
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 253..299
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 290..328
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1233 AA; 133414 MW; D3034615E4850956 CRC64;
MPATKTKFGL LLFLTQWVVY SEAWFWSWSG TTTRLPQTLE YEGSGSPTGS GELPSEITTK
AEGDMVHEGH GTPNIKQTWV LTTEDPQMST VTPATLRETD DASESVTARI PPQSTSGNGT
STLTALGSDP SRILKNASKI ESEVELAVEL DSKHGGFSSS GLLPVAENMA SLVYEDGAVK
QADRRGLDNA SGAAFHVKKV GLRLSERVST IASKQEFSKA SVRAVGIGKG IHAQTENASS
ISCLVLDAAL PFCSSKFGET FAVPNYFNHS SLEEVQALLK EWAWLLESRC HHSLEWFFCL
LLVPKCDPAT PMLTLPCRSF CEVLLDSCWA LLEGQHLPVE CHTLPDASHG YQCLSVCNQN
EDNGVSLLQL IGDPPPSEIS QVYGPDNAIG YVFGPDAKMG QLAVAHFPTP FYRDFSLNFH
LKPTSNEGGV VFSITDSSQQ VIVVGVKLST VERQTQDVIF YYSETGSEQS YEAARFQVTS
MTDTWTRFSI SVRDDKVAFY FNCDLSPVVK RFERSPDDME LERGSGVFVG QTGGPDPERF
LVCICFHPTQ PNVVFYTQCH RTTDFSKWNL GDGELLAGFG YQGKKGDPGQ PGPPGPPGPP
GPSTEYVPSS DGTVVSKVQG PRGPPGPPGP QGQPGEDGEP VCRWFHCQHT FFLKKHHIFN
KVFRSFSIIS LFQVLILIHA VTFFSHLLLC VQGEKGEPGL IIGPDGNPLY LGGLTGQKGD
IGPQGPGPPG LKGEIGMPGR PVSIHQNGVP GPPGPPGPPG PPGPPFAIDR FNVRTASDFD
IYTLKNQWKG ERGDPGVKGE KGEPGAGHDP QYGALQGPLG PPGLPGPKGD SIMGPPGPQG
PPGSPGIGYD GRPGPPGPPG PPGPPWSQTL PESYKPNYPV SVPGPPGPPG PPGHPGHSSG
VMVLRSYDTL IATARSQEEG SLIYILDKAD LYLRVRDGLR QVMLGEYNPF FRDFDNEVAE
AQPPPVVLYP HSPDHSQNNG ASQYSQGGSV IRPIETPPPV ERRYPPQYEP RFPDQQRPSQ
TDGRLINQPS DGKYAVTPQR RPNPPVPGPV ETSTLGVSGL RLIALNTPQS GNMKGIRGPD
YLCFEQARAA GLRGTFRAFL SSKVQDLHTI VRHSDREKPP IVNLKNQVLF DSWQSIFGES
VSKMRKNVPI YSFDGRDILR DSAWPEKMVW HGSSKKGHRQ TDQYCEAWRA GDQAVTGLAS
SLQSSHLLQQ TPTSCSRACI VLCIENAMVS PSK
//
