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Database: UniProt
Entry: A0A3Q0R8D5_AMPCI
LinkDB: A0A3Q0R8D5_AMPCI
Original site: A0A3Q0R8D5_AMPCI 
ID   A0A3Q0R8D5_AMPCI        Unreviewed;       663 AA.
AC   A0A3Q0R8D5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Stabilin 2 {ECO:0000313|Ensembl:ENSACIP00000006133.1};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000006133.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000006133.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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DR   Ensembl; ENSACIT00000006315.1; ENSACIP00000006133.1; ENSACIG00000004189.1.
DR   GeneTree; ENSGT00940000156566; -.
DR   Proteomes; UP000261340; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   CDD; cd00055; EGF_Lam; 1.
DR   Gene3D; 2.30.180.10; FAS1 domain; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
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; 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:SF0; STABILIN-2; 1.
DR   Pfam; PF12947; EGF_3; 2.
DR   Pfam; PF02469; Fasciclin; 1.
DR   Pfam; PF00193; Xlink; 1.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00445; LINK; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF82153; FAS1 domain; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS50213; FAS1; 1.
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        569..593
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          103..143
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          150..187
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          191..229
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          232..274
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          307..400
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          420..554
FT                   /note="FAS1"
FT                   /evidence="ECO:0000259|PROSITE:PS50213"
FT   DISULFID        133..142
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        177..186
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        329..398
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        353..374
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ   SEQUENCE   663 AA;  71828 MW;  7967D4E392055FCD CRC64;
     LIKNDCQNIP LIITQTAQNG VSILNWWKTV RHSMQLGLSP SFIKHSECVA LSFAANISVL
     FCVQEVQKCD LPTIHFAKNT GCRPVCTITI WQPKCCRGYY GRDCLVCPGG VGSLCNNRGK
     CDDGHLGNGT CTCDAGFRGT ACELCSDGFY GPTCKACNCS ERGSCDDGWR GTGLCFCEAG
     WTGDRCDIQL TDDVCQIWNG GCAKGAKCSQ KGGKVSCTCP KGHTGDGFTC LPIDPCASGD
     NGGCHEHATC TMTAPGRRKC SCKDNYIGDG VTCEVKQLPI SRCLQDNGQC HLDAKCTDLH
     FEDAMLGVFH YRSKKGQYKL NYTAAQQACA AEEGCLATYT QLAYAQQGGL NMCAAGWLDQ
     ARVAYPTTYS NPNCGFGHVG IVDYGIRKNL SETWDTFCYR LKEVKCECKA GYVGDGFSCT
     GNLLQVLRST PTFSNFLTQI LNCSLASESG KQFVQRLSNL TVQSTLFVPD NSGLPGNQTL
     SLRDIEFHLS EGRAFPLSQL KNGSRIRTRV GSLTVLGVAD QLNPSSSRYI NDRFVTDSDI
     LAANGIIHVL QAPLKAPSPH PQMHAAHKAG MGIGVVLLMA LMGGAXFVGY RFYSHSTKPF
     QFHYFKEDDG EEEAPPANCS RSICNPVYEA APEAAESGEP AVTVSQQHVV GMKHLKQQLQ
     LQH
//
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