ID A0A060YA09_ONCMY Unreviewed; 1505 AA.
AC A0A060YA09;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Stabilin 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSONMT00059013001 {ECO:0000313|EMBL:CDQ88362.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ88362.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ88362.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ88362.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; FR908566; CDQ88362.1; -; Genomic_DNA.
DR STRING; 8022.A0A060YA09; -.
DR PaxDb; 8022-A0A060YA09; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR Gene3D; 2.30.180.10; FAS1 domain; 3.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 3.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR24038; STABILIN; 1.
DR PANTHER; PTHR24038:SF0; STABILIN-2; 1.
DR Pfam; PF12947; EGF_3; 4.
DR Pfam; PF02469; Fasciclin; 4.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00554; FAS1; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF82153; FAS1 domain; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 9.
DR PROSITE; PS50026; EGF_3; 8.
DR PROSITE; PS50213; FAS1; 4.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Reference proteome {ECO:0000313|Proteomes:UP000193380};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1505
FT /note="Stabilin 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001591917"
FT DOMAIN 108..148
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 194..234
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 235..274
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 320..359
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 362..516
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 528..662
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 747..787
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 837..877
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 921..963
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1004..1137
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1144..1272
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1355..1393
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 138..147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 203..220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 777..786
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1383..1392
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1505 AA; 162139 MW; 660894E762CFBA74 CRC64;
MAPVTGPLAL MLLLLGLDRY TSSAAAAKNR CDKTTLVMTK TECHSCSVSS NVGCPAGFNK
KIPGKGNPDC KYRVSPMASL VLNIKGCSHE CYKEVVEPHC CPGYWGPDCI ECPEDADRPC
SNNGLCSEGM GGNGSCSCKP GFVGTACEDC ADNLYGSTCS SACTCGHGLC NAGIHGDGIC
TCFSGYKGPK CDLELPECSS LLCPQNTRCM QGSLDGSLRC QCLPGYRTSG DQCISINPCL
QQVCHIHATC AHVGPNKQLC TCAQGYSGDG HVCVPIDPCQ THLGGCSADS ARCVYDGPGK
SHCECQDGFD HLTGGVSCSL KDLCRPNSCS KHANCSTVEP NIVECTCHEG YVGNGKICYG
NIMQRLNDLN SEPGGQWTGQ LSNAITLFGA ITWPLSNFGP FTIFVPINKG FKGTPTKELS
KDTRNKIVDL HQAGMTESAI GKQLGLKKST VGAIIRKWKT YKSTDNLPRS GAPRKISPRG
DKQLKIRIHG SRKKGGVLQS DVIASNGIIH IINKLMDSVS PTVESDKKEN LMKILSDYGK
FSKFKDLLMK ANVDSVLEEA GPSTIFAPTN TAFDAMKEGQ LDYLTSSEGS TKLLELLRNH
VIPSFNLECY NAVSNQRIRT IANQILSFNV TENGQILVNG MAVLEADVEA KNGRLYSMDG
VLIPPSIEPV LPHRCDITEN KLLKGDCVSC SKVTKSGCAS GVSTNTFLRG CVFRNILSFN
ILTFGCAPIC NRTLTTPLCC KGFYGPDCTP CPGGFNTPCS RHGQCSEGIE GNGTCVCETN
FKGSRCHYCS NPNKYGPACD KTCDCIHGVC DNRPEADGRC KVDSCQPGYT GQYCERHTQA
CGPQVTFCHA HAECNFNGGA VRCVCKPGFQ GDGITCVYTE PCALPHRGGC DVNAKCIKTG
PVSHTCQCLA GWRMDEDGCQ PINDCLGPDR GGCHPNATCI YVGPGQSGCA CKSGFRGNGR
ECEASNPCVA QNGGCHYLAS CLYVSGAWKC VCEDGYTGDG EVCYGNVGQE LMALPDVTEF
AKWVTDIGIS QLPLMNSQNI TLLVPSTAAT DKMTKEDKDF WTTQGNLPSI IKNHMIQGVY
SLDDLRDASS NLQLTSVLKK ALPVTMTNES TVIGGATVTT ANVASTNGLI HIIDTVLVPE
RSLSEGLLEL LARRPEFSLF KSYLVHHNLT AEIEQASAYT VFAPTDGAVL EYLKNIASDT
MDLNTTRYHI VLSDRLMKVD LLGGAYKETM LGFSYQLGIL PRDDKLFVNE AQVNVSDILG
GKGVIHGLSA VLDITKNRCD IQQFKTFPGL CQDCFYPQLN SCPTGATTIA LVRKKCMFSR
VYQGERLLSI GCRTICKNTT IVRRCCGGFY GEHCEPCPGP KGQPCYGNGM CQDRTNGTGV
CQCNKSFNGT ACETCQEGKY GIHCDQDCRC KNGRCNDGIH GDGTCECDAY WRGVTCDDKF
TREENCGDRK CHTSAICVVG RCECLAGFQG NGTDCKGILP VTFQHALLYW YLNCYYTIHD
YHTGN
//
