ID A0A093ITD5_FULGA Unreviewed; 1918 AA.
AC A0A093ITD5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Stabilin-1 {ECO:0000313|EMBL:KFW05980.1};
DE Flags: Fragment;
GN ORFNames=N327_10600 {ECO:0000313|EMBL:KFW05980.1};
OS Fulmarus glacialis (Northern fulmar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC Fulmarus.
OX NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW05980.1, ECO:0000313|Proteomes:UP000053806};
RN [1] {ECO:0000313|EMBL:KFW05980.1, ECO:0000313|Proteomes:UP000053806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW05980.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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 EMBL; KK600798; KFW05980.1; -; Genomic_DNA.
DR Proteomes; UP000053806; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.30.180.10; FAS1 domain; 6.
DR Gene3D; 2.10.25.10; Laminin; 10.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR000538; Link_dom.
DR PANTHER; PTHR24038; STABILIN; 1.
DR PANTHER; PTHR24038:SF8; STABILIN-1; 1.
DR Pfam; PF12947; EGF_3; 7.
DR Pfam; PF02469; Fasciclin; 5.
DR Pfam; PF00193; Xlink; 1.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00554; FAS1; 6.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF82153; FAS1 domain; 6.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 10.
DR PROSITE; PS50026; EGF_3; 14.
DR PROSITE; PS50213; FAS1; 6.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292};
KW Reference proteome {ECO:0000313|Proteomes:UP000053806}.
FT DOMAIN 1..130
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 210..250
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 342..384
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 385..427
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 428..469
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 469..599
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 610..738
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 821..853
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 860..897
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 901..940
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 941..982
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 983..1025
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1067..1195
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1210..1350
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1422..1462
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1472..1506
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1511..1545
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1546..1586
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1587..1629
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1663..1756
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 1776..1914
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DISULFID 240..249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 843..852
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 868..885
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 887..896
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 905..915
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 909..926
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1452..1461
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1496..1505
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1515..1525
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1685..1754
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 1709..1730
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW05980.1"
FT NON_TER 1918
FT /evidence="ECO:0000313|EMBL:KFW05980.1"
SQ SEQUENCE 1918 AA; 208554 MW; E4EEC10701C88271 CRC64;
ILASMEIFSR FETILENCGL PAILDGPGPF TVFVPSNDGV DKLRDGRLIY LFTEGINKLQ
ELVKHHIYTS AAVTVEKLIM MPHIVTMANQ ILTINISADG RILMDESGIP LNMRDIVASN
GIIHTLDGIF IPPSIIPILP HRCNEEQHKI VLGSCVDCEA LNNSICPPGS REMVNICGYF
GLNVLKKGCA RYCNQTVTKP ECCKGFFGPD CMPCPGGFSS PCYGRGNCSD GIQGNGNCHC
FEGFKGIACH ICSNPNKHGE NCDEDCGCVH GVCDNRPGSG GVCQSWSCKE GYTGKFCDKT
SKNCGPSGLS QYCHQNAVCS LNDTARCICM DGYEGDGFSC QPINLCSQPE RGGCSQNALC
TSTGPGTATC QCNTGWTGDG KACVAIDSCM LESRGNCHIN ADCVYIGPGQ SNCVCKRGYA
GDGHNCDAIN PCLMDNGGCH DLAMCVPLGG GERSCACPQG YMGDGMTCYG DILKELARNS
HFAGFYDWLQ KSLFSIPAGA NVTVLVPSEA AIKNLSKTEK DFWLTPYMLP FLVRAHFLEG
IFTGEKLKKY DRPELPTLNP QTRWQINTRS GVLTIQNASI VVSDIPASNG IIHVLSKVLL
PPSGDIPPSP PGLQKQLETV ASFSTFRELL QQYQLIGKIE SSEKYTVFVP GNNSIEEYCH
TANVTQLDNE TVQYHVVLGE KLLPTDLRSG IHKNSMLGLS YWLMFYQNST QKFVNNILLD
GKFLETKNGM LIGVSQVLQV QKNRCTANTT TIQKSRCGKC EKGIKCPPGS VLVVSRVASP
VKLYFVLHET AHPDLFLLVP QRSVCCPGYY GHMCEMCPGK PGQWCSGNGE CQDGIEGSGE
CRCLEGFHGT ACEMCEVGRY GADCKSECAC DNGICNDGLQ GDGSCKCFPG WKGPTCRERI
EIDLCNNTCH QMANCLNSSA DSPPTCFCSA GYTGNGTHCT EIDPCTIDHG GCSVHAVCTK
VSPGERTCVC KEGYAGDGTL CMEIDLCLES NGGCHTNAEC IKTGPRKVAC NCLPGYSGDG
VSQCNPINLC EQNNGGCSLF GLCKYTGPGT RNCSCPWHSI GDGFTCRGKV YQELGRIEDA
SVFFKMTLAE NIKELSGAGP FTLFVPQTDF IGNTTTFEEW RSRGLLRDLL RYHMVGCQKL
LSSDLEAQES LTSLSGHKIK ITVKENSIYL NEEAKVVVSD IIGMNGVIHF INKILIPSDL
VGRNISSKIS QQNVTEVAEA FGYTIYSKLL QDAELLPLVS DPLHRPFTML WPTDAAFNAL
SEKRQKWLYR REHRDMLASY LKAHMIRDTK IVAGNMPQVE SIRTMHGSTV SFSCSKTHMG
ELLVGNGDAT IIQRHMEFNG GIAYGIDRLL EPPDLGSRCD EFIFVELQVS TCDEANEDLC
HLKPLLLVIK LNEWHKKSQG CRRSCVSTQW VPQCCANHYG RDCRACPGGL EVPCSNRGTC
DDKIGGSGRC NCSQAFIGTS CELCAPGRYG PDCRECNCTE NGVCNGGLHG DGFCFCAEGW
TGDHCEIRLV MTPTCSPPCH PQAICRSGNL CECNLHYEGD GRTCSVIDMC SQDNGGCARH
AQCTQVGVNI SCACAPGYGG DGYVCDPIDR CADGRNGDCS QHANCISTGP NERRCECKRG
YVGDGIQCLE EAVPPTDRCL EDNGQCHREA ICTDLHFHDK TMGVFHLQSP RKKYDFTYEQ
AQKACAAEGA SLATFRQLSA AQQMGFHLCL VGWLDNGTAG YPTAYPNPSC GANRVGIVDY
GSRSNLSETW DAFCYREKDL TCACRDGFVG DGYWCSGKLP DVLADHARFS TFYSMLLDFA
NDTEEGLDFF IYLSDDSAPK TLFVPLNSGF ADNETLTGEE LKLHVSSSNI VLFSFNLTTG
TIIPSRSGYD LHVSDLPVGN STEHADAKGI NDTMIVEWDI VAFNGIIHAI AEPLRIPP
//
