ID A0A340X4W6_LIPVE Unreviewed; 2549 AA.
AC A0A340X4W6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Stabilin-2 {ECO:0000313|RefSeq:XP_007454334.1};
GN Name=STAB2 {ECO:0000313|RefSeq:XP_007454334.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007454334.1};
RN [1] {ECO:0000313|RefSeq:XP_007454334.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_007454334.1; XM_007454272.1.
DR STRING; 118797.A0A340X4W6; -.
DR GeneID; 103080578; -.
DR KEGG; lve:103080578; -.
DR CTD; 55576; -.
DR InParanoid; A0A340X4W6; -.
DR OrthoDB; 2970631at2759; -.
DR Proteomes; UP000265300; Unplaced.
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 Gene3D; 2.30.180.10; FAS1 domain; 7.
DR Gene3D; 2.10.25.10; Laminin; 14.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
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; 9.
DR Pfam; PF02469; Fasciclin; 6.
DR Pfam; PF00193; Xlink; 1.
DR SMART; SM00181; EGF; 23.
DR SMART; SM00179; EGF_CA; 8.
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; 7.
DR PROSITE; PS01186; EGF_2; 12.
DR PROSITE; PS50026; EGF_3; 18.
DR PROSITE; PS50213; FAS1; 7.
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:UP000265300};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2549
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016398519"
FT TRANSMEM 2458..2481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 107..147
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 155..192
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 194..235
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 236..275
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 321..361
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 370..504
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 514..651
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 735..775
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 825..865
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 866..908
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 909..951
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 952..993
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 993..1126
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1136..1264
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1345..1383
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1431..1469
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1470..1511
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1512..1553
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1554..1593
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1595..1723
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1739..1880
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1957..1997
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2004..2041
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2122..2164
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2197..2290
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 2310..2444
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT REGION 2510..2549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2510..2526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 137..146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 163..180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 182..191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 765..774
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1373..1382
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1435..1445
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1987..1996
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2031..2040
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2219..2288
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 2243..2264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 2549 AA; 276581 MW; FA07B6326DB9CC58 CRC64;
MLQISILLFL GLAAQNLCSL PETAEQAKRC DKKSLLTIRT ECRSCSLNFG MKCPDGYAKI
TNGTVGIRDC RYTFEVRTYS LSLPGCRHIC RKDYLQPQCC PGHWGPDCME CPGGARAPCA
GRGSCADGME GNGSCSCQEG FGGTACETCT DDNVFGPSCS AMCSCVHGIC NSGIRGDGTC
ECYSGYTGPS CDKPIPECAA LLCPENSRCS PSSEDETKLE CKCLPSYKGD GQRCEPINPC
SQNMCHPHAR CAYLGPNQHS CTCQEGYHGD GQVCLPVDPC QVNFGNCPTE STVCRYDGPG
QAHCECAEHY HNFVPGVGCS VIDVCESKNP CHRDANCTTI APGHTKCTCR KGYVGDGSTC
YGNIMERLRE LNTEPGGKWQ GRLTSFISLL DKAYAWPLSN LGPFTVLLPT DKRLKGFNVK
ELLLNNEAAQ YFVKLHIIAG QMSTEQMNNT DTFYTLTGKS GEIFSDDKDS HLKLKLYGGK
KKVKILQGNI IASNGLLHIL DRAMDKVAPT FESNIEQTIM TMLQPRYSKF RSLLEETGVG
HVLDEDGIGG PYTVFVPSDE ALNNMKDGTL DYLLSSEGSR KLLELVRYHV VPFTQLEVAA
LISTPHIRSM ANQIIRFNTT DNGQILANDV AMEEMEVIAK NGQIYTLTGV LIPPSIIPIL
PHRCDETKRE MKLGTCVSCS LVYWSKCPAD SEPTTLFIRK CVYTGRIRSL KNGCARYCNA
TVKIPKCCNG FYGPDCNQCP GGFSNPCSGN GQCTDGLDGN GTCVCQDGFH GSQCQFCSDP
NKYGPRCEKR CLCSFGTCDN RIDSDGACLP GTCRDGSAGR FCHKQTSACG PYVQFCHIHA
TCEYSNGTAR CVCKAGYEGD GSLCSEMDPC SGLTRGGCSR NAECIKTGRG TPICVCHQGW
TGDGRDCSEI NTCLLPSAGS CHHNATCLYI GPGQNECECK KGFRGNGIDC EPVTSCLEQT
GKCHPLATCQ FTSSGVWSCV CQEGYEGDGL LCYGNAAVEL SFLSAAAIFN QWINNASLQP
MLSAASNLTI LVPSQQAIED MDQDEKAFWL TKSNIPALIK YHTLLGTYGV ADLQALSPSD
MLATSLQGNF LHLAKADGNI TIEGACVIDG DNAATNGVIH IINKVLVPQR GLTGSLPNLL
TRLDQMPDYS IFRGYIIQHN LASSIEAADT YTVFAPNNDA IESYIREKKV TTLEEDVLKY
HVVLEEKLLK NDLHNGMHRE TMLGFSYLLG FFLRNGQLYV NEALINYTNV ATDKGVIHGL
GKVLEIQKNR CDINDTTILR GKCGKCPQQP ICPFGTKPLG AEMKKCLYTI YFMGKRSLFI
GCQPKCVKTV ITRECCAGYF GPQCRPCPGK AENICFGNGI CLDGVNGTGM CVCGEGFSGT
ACETCVEGKY GIHCDQACTC VHGRCSQGPA GDGSCDCDVG WRGVKCDDEI TKDECNGTCH
TSANCLLNPD GTPSCKCAAG FQGNGTVCTA INACEISNGG CSGRAVCKRT TPGSRVCVCK
AGYTGDGIVC IEINPCLENH GGCHQHAECT QTGPNQAACN CLSKYTGDGK VCTLINVCLT
KNGGCSEFAL CNHTGEDERT CTCKPNYIGD GFTCRGNIHQ ELPKNPRTSQ YYFQLLEHSV
RDLVGPGPFT VLAPLSAAFD EEPQIKDWDK QGLMPQVLRY HVIACHQLLL ENLKLTPNAT
SLQGESIVIS VSQDTVLINN KAKIISSDII STNGIIHIID KLLSPQNLLV TPKDASGRIL
QNLTTVAINH GYIKFSNLIQ DSGLLNVITD PIHTPVTLFW PSDQALQALP PEQQDFLFNQ
DNKEKLKEYL KFHVIRDSKV LAVDLPRSAT WKTLQGSELS VKCGAGSDIG ELFLNGQMCR
IVQRELLFDL GVAYGIDCLL IDPTLGGRCD TFTTFDVSGN CGSCVHTPSC PRWTKPKGEK
RKCLYDLPFR RNLEGCKQQC TLVIQLPKCC KGYFWPDCQA CPGGPDTPCN NRGVCLDQYS
PAGQCKCNTG FNGTACELCW PGRFGPDCQP CGCSDHGQCN DGITGSGQCV CETGWTGRFC
DTQTVLPLVC MPPCSAHATC KENNTCECNL NYEGDGITCT VVDFCKQNNG GCAKVAKCSQ
KGTKVSCSCQ KGYQGDGHSC TEIDPCADGL NGGCHEHATC QMTGPGKHKC ECKRHYVGDG
LDCELEQLPI DRCLQDNGQC HADADCADLH FQDTTAGVFH LRSPLGQYKL TFDKAREACT
KEAATMATYN QLSYAQKAKY HLCSAGWLDS GRVAYPTSYS SQNCGSGIIG IVDYGTRNNK
SEMWDVFCYR MKDVNCTCKV GYVGDGFSCS GNLLQVLTSF PSLTNFLMEV LAYSNSSARG
RAFLKHLTDL SIRSTLFVPQ NSGLGENETL SGRDIEHHLA NVSIFFYNDL VNGTVLHTRL
GSQLLITSSQ DQRQLETRFV DGRAILQWDI FASNGIIHVI SRPLKAPPTP VTSGRAGLGT
GTFFATILVI GAIALAAYSY FRLNRRTTGF QHFESEEDID VAALGKQQPE SISNPMYENT
ASATPEPSYD PFMDPEDQQL DSIDPLGAL
//
