ID A0A3Q1IHZ3_ANATE Unreviewed; 2329 AA.
AC A0A3Q1IHZ3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Stabilin 1 {ECO:0000313|Ensembl:ENSATEP00000003916.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000003916.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000003916.2}
RP IDENTIFICATION.
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:PRU00076}.
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DR Ensembl; ENSATET00000003951.2; ENSATEP00000003916.2; ENSATEG00000002289.2.
DR GeneTree; ENSGT00940000157928; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; 9.
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; 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:SF8; STABILIN-1; 1.
DR Pfam; PF12947; EGF_3; 6.
DR Pfam; PF02469; Fasciclin; 5.
DR Pfam; PF00193; Xlink; 1.
DR SMART; SM00181; EGF; 22.
DR SMART; SM00554; FAS1; 5.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF82153; FAS1 domain; 6.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 13.
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|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2242..2262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..99
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 107..144
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 307..430
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 444..578
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 652..692
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 785..827
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 865..905
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 925..1053
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1145..1177
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1225..1264
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1265..1306
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1346..1386
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1379..1518
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1515..1661
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 1746..1786
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1793..1830
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1864..1904
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1905..1947
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1981..2074
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 2094..2226
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DISULFID 89..98
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 115..132
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 134..143
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 682..691
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1167..1176
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1229..1239
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1233..1250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1776..1785
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1820..1829
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2003..2072
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 2027..2048
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 2329 AA; 254749 MW; 4E045738BBF65C0A CRC64;
MSTFWNFPFI SLASLSKHNT SADCNVYIVV LQFIRRLSHN LIYKHIIIIS DFIFRFTCLS
AACPSWSGKT CNFHGTCLDG DLGNGTCVCD DGFSGFACQE CKNQNAFGEK CDKECDCEHG
VCNKGPEGDG QCLCQPPYTG QRCDKVSDRC SNCSPYSYCK GEGDTAVCEC LPGYRKTSQG
KCASFCSGRD CDVNAMCSTQ GSKLSCACKP NYEGDGKICV PRNPCSENNG GCPINSTVCV
FNGPNKSSCE CMFGMSPIGG NPELGCQLVS ACSADTCDPT AVCMTELDGQ PRCLCEPAQI
GDGRRCYGNL MERLIELDRS GNHQENLTGA VALFEKGCSL VLSHSGPFTA FIPLLKTPLT
EVVCKNHLIL GQYLYKDIEG QVFRLYGGAI FRSKDNKKFI LWEDPRKLYT VIQEDLPAAN
GIIHIIDQPI TISEKPPRDE KFADKTIYEI LTKDAKYNRF LSLVDNCGSA PPLRGRGPLT
VFVPTNQAVD QARDGSILYM LNDAKHKLQE LLRHHVFSLA VLTVDELAAF PQIQTMANQI
VTITVSDGEI LLGEKGVHLV STNIMASNGI IHMIDGLLYP PSILPILPHR CDIIESKITG
PCVHCSYLNE TECPEGSTEM VKHLHFYFHV SALLRLCVKQ VAECCKGFYG PDCKPCIGGF
QHPCYDKGAC FDGIRGNGQC SCQSGFRGIA CHICSDPTKH GQNCNEECRC VHGVCDNRPG
SGGVCRRGSC LKGYSGENCD KMAMPCNSDG LQEHCHIHAY CTFQGLQTTC VCRNGYEGDG
HSCSPINPCL KSNRGGCDTN ADCVYVGPGN VSCVCVEGWT GDGRVCVEIN NCQLESRGGC
SPNADCNHIG PGQSECVCKQ GYMGNGIVCD LINPCLKKNG GCHELVNSGS HTCTCPDGYA
GDGAICYGSL LDVLYPPLSD LPPEPLTLMA FLSSSSNFTL FRQYALMYNL SGNLTTTDFT
LLLPTDDAIR QHLSNTNSSI LDSDVFMYHV IINELLFPDH LVDGMLKNTL LGSDYQVQFH
LNSNNQTLVN EVLLDGSFIE TQYGVLIVLP QVLKVRRNRC SKQITLQVNG RCTDCDGPPR
CLFNYKPVRY QFPANMRPNC NYRKRVGSRR KSVAGCVMKC LRFTTDHSCC PGYYGHECFK
CPGDVGKWCS NHGECQDGNH GNGECRCYEG FHGTACENCE PGRFGVNCSS KCVCDHGKCE
DGLAGSGRCM CYKGWKGASC SIEIKDDACG GVCDENANCV TGPKGSAPAC VCVAGYEGNG
TYCNELDVCS RSNGGCSEFA FCVRVSVGER TCTCKEGYTG DGVVCLGFLF FSSQYIKYCS
HVPPNDYYSV IVYGITFSRR VCVFTEIDGC LNNGGCSRHA RCEYMGQGQR NCSCFRGYSG
DGIDCRGNTR MVSRVTSDLC LHTSMPSTLH LSDIGGLYGD GPFTVFVPVA ENNNQSYVSI
EEWKLCGRLN DLVRYHIVSC ETLTSSDLKT TERAVSLSGH TLHFSLQQGS VWVNNRSRIV
KSDYTTANGI IHYVDLILFS FLCSLNSFLC TNSNMYCQCF LQDAGLLPVL KMSIHQPFTV
FWPTDKALNS LPAERQQWLS SPDHQEQLAA IVKAHIVRSR SMSILQPDII SKLRTMHGST
ITYNCDKNLV GAIRINDNSA SVVERYLTFK EGVAYGIDQL LEPPGLGAFC DSIENKTTYG
LCGQCLFPPS CPGKTEPCLN SRYRHRHSYP YWYHSLDDHF SRMGCKRVCQ FPFWDQKCCK
NHYGRDCQVC PGGVEAPCGN KGYCNDGLRG SGMCMCQKGF RGKACELCVV GHYGPNCTAC
SCEKQGVCDE GIEGSGKCVC NKGWQGDRCS IPEECRQCHD QADCVPGVGC QCKSGFQGNG
TFCTPDLCSE YNGGCHQNAI CNQTELVVNC TCRTGYQGDG YICEPINRCV EEQNGGCSDF
ASCKFTGPNE RECECLPGYV GNGVQCLEKV VPPVDRCLED NGGCHPVASC RDLHYHTNTA
GVFHLRSPEG KYKMNFSQAD AACQAEGATL ANFKQLGDAQ QLGMHLCTAG WMEGGKVGYP
TRFPSVKCGD NHVGLVIYKD PVEQSSQYDA YCYRLKDVSC ECPAGYIGNG DYCNGVLSNI
LATYSNFSIF YKVSVTYSDS SSEGKQLVDV LSHRKSEVTL FVPHNAGFAQ NQTLSGRDIE
YHISANHSRR AFKDLRHDDV ITSMLGLNLT VTHGNNESCK LVNKRLLLEW DIPAVNGIIH
VIEGPLTAPP TPVSKAGFKP TVGILMLVLL VCVLAAFGYY VFKHKTDAFR FHYFKNDDDN
AAGGNNKPTL VSIPNPLYSG SRAFAEPFGV TACFSPTATV SRTDTVSFL
//
