ID L5KHT0_PTEAL Unreviewed; 2232 AA.
AC L5KHT0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Stabilin-2 {ECO:0000313|EMBL:ELK10321.1};
GN ORFNames=PAL_GLEAN10015473 {ECO:0000313|EMBL:ELK10321.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK10321.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB030754; ELK10321.1; -; Genomic_DNA.
DR STRING; 9402.L5KHT0; -.
DR eggNOG; KOG1218; Eukaryota.
DR InParanoid; L5KHT0; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd03515; Link_domain_TSG_6_like; 1.
DR Gene3D; 2.30.180.10; FAS1 domain; 7.
DR Gene3D; 2.10.25.10; Laminin; 8.
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; IPR000538; Link_dom.
DR PANTHER; PTHR24038; STABILIN; 1.
DR PANTHER; PTHR24038:SF0; STABILIN-2; 1.
DR Pfam; PF12947; EGF_3; 7.
DR Pfam; PF02469; Fasciclin; 7.
DR Pfam; PF00193; Xlink; 1.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00554; FAS1; 7.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF82153; FAS1 domain; 7.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 10.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2136..2159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 196..330
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 321..440
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 524..564
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 614..654
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 822..951
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1032..1070
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1077..1114
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1116..1157
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1158..1199
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1200..1239
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1253..1353
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1369..1558
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1635..1675
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1682..1719
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1800..1842
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1875..1968
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 1988..2122
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT REGION 2179..2211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2185..2199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 554..563
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1060..1069
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1085..1102
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1104..1113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1665..1674
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1709..1718
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1897..1966
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 1921..1942
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 2232 AA; 242069 MW; 51ACD239BA1E08D1 CRC64;
MNCPHRVSSV SDLQQGIPLR SERTRCLSPD VATSVGRPIS SLSAVQATGA QIAWSAQEER
VPPAAAEAVV QKAWEEMEAA HAKKGLVEQP VKPVLMTIYL DPTAQQPSIH AYKTSATLML
VAHTWDQIGT VAHAKKATTG MAMCAYQSTP AKLTLDTALR SLQCAYMMGL DRCTCQKGYV
GDGSMCYGNI MERLRELNTE PRGKWQGRLT SFISLLDKAY AWPLSNLGPF TVLLPTDKGL
KGLNVKELLM DNEATQYFVK LHIIAGQMNT EQMNNTDTFY TLSGRSGEIF NDDKDNQLTL
KLYGSKKNVK IIQGNIIASN GLLHILDRAM DKMAPTFESN SEKTNVGHAL DKDGVGGPYT
IFVPSNEALN NMKDGTLDYL LSPELEVASL ISTPHIRSMA NQIIQFKTTE NGQILANDVA
MEEIEVTAKN GRIYTLTGVL IPPSIVPILP HRCDETKREI KLGTCVSCSL VHWSKCPANS
EPTALFTHRC VYTGKTRSLK SGCAKYCNAT VKVPKCCKGF YGSDCNQCPG GFSNPCSGNG
QCADGLGGNG TCICQDGFQG SQCQFCSDPN KYGPRCDKKC LCIYGTCDNR IDGDGACLAG
TCRDGSTGRF CHKQTSACGP YVQFCHIHAT CEYSNGTASC VCKAGYEGDG SLCSESDPCS
GLTPGGCSRN NECECKEGFR GNGIDCEPIT SCLEQTEKCH PLATCQFTSS GIWSCVCQEG
YEGDGFLCYG NAAVNASLQP ILSAASNLTV LVPSQQAIED MDQDEKAFWL SKSNIPTLIK
YHTLRGTYGV ADLQTLSSSD VLATSLQGNF LRLAKKDGNI TIEGASIVDG DNAATNGVIH
IINKQFNLAN AIEAADAYTV FAPNNDAIEN YIREKKVTTL EEDILRYHVV LEEKLLKNDL
HNGMHRETML GVSYLLSFFL HGDQLYVNEA PINYTNVATD KGVIHGLGKV LEIQKNRCDN
SNTTIVRGKC GKCPQQPICP FGSKPLGEET MKCIYTIYFM GKRSVFIGCR VKCVKTVITR
ECCAGFFGPQ CQPCPGKAQN VCFGNGICLD GVNGTGVCEC GEGFSGTACE TCVEGKYGIH
CDQECSCVHG RCNQGPSGDG SCECDVGWRG VKCDRAINPC EISNGGCSAK ADCKRTMPGS
RTCVCKAGYT GDGIVCIEIN PCLENHGGCD KNAECTQTGP NQAVCNCLPK YTGDGKDCSL
INTCLTKNGG CSEFAICNHT GQEERTCTCK PNYIGDGFTC RGNIHQEHSV RDLVGSGPFT
VFAPLSTAFD EEPRIKDWDK QGLMPQVLRY HVIACHQLLL ENLKSTPNAT SLQGESIVIS
VSQDTVYINN KAKIISSDII STNGIIHIID KVLSPQNMLI TPQDASGRIL QNLTTVAINH
GYIKFNNLIQ GAGLLSIISD PIHTPVTLFW PTDQALQALP AEQRDFLFNQ DNKDKLKEYL
KFHVIRDAKV SAADLPRSTA WKTLQGSELS VKCGAGSDIP LCGLISSPLL AVRENQLRVP
PSQISQQICN FHLPWLVPEQ FYLPIQKGEL FLNDQTCRIV QRELLFDLGV AYGIDCLLID
PTLGGRCDTF ATFNVSGDCG SCVYTPSCPR WTKPKGVKQK CLYNLPFKRN LEGCRQQCAL
VIQLSRCCKG YFGRDCQACP GGPDTPCNNR GVCLDQYSAT GECKCNTGFN GTACELCWPG
RFGPDCQPCS CSDHGQCDEG ITGSGQCLCE AGWTGRFCDT RAVLPPVCTP PCSAHATCKE
NNTCECNLNY EGDGLTCTVV DFCKQNNGGC AKVAKCSQKG TKVSCSCSKG YQGDGHSCTE
IDPCADGLNG GCHEHATCKM TGPGKKKCEC KSHYVGDGLD CEPEQLPIDR CLQDNGQCHA
DASCADLHFQ DSTVGVFHLR SPLGQYKLTF DKAKEACANE AATMATYNQL SYAQKAKYHL
CSAGWLESGR VAYPTAYASQ NCGSGVVGIV DYGPRNNKSE MWDVFCYRMK DVNCTCKVGY
VGDGFSCSGN LLQVLMSFPS LTNFLMGVLA YSNSSARGRA FLKHLTDLST RSTLFVPQNS
GLGENETLSG RDIEHHFANV SIFFYNDLVN GTILQTRLGS QLLITSSQDQ GQLETRFVDG
RAILQWDIFA SNGIIHVISR PLKAPPAPVT AVHTGLGTGI FFAITLVIGA IALAAYSYFR
LHRRTTGFQR FESEEDIDVT ALGKRQPENV SNPMYESATS APPEPSYDPF TATLFQVSEE
QQLESGDPLG VQ
//
