ID A0A3Q2V9E2_HAPBU Unreviewed; 682 AA.
AC A0A3Q2V9E2;
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-like {ECO:0000313|Ensembl:ENSHBUP00000007350.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000007350.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000007350.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; A0A3Q2V9E2; -.
DR STRING; 8153.ENSHBUP00000007350; -.
DR Ensembl; ENSHBUT00000003786.1; ENSHBUP00000007350.1; ENSHBUG00000008865.1.
DR GeneTree; ENSGT00940000156566; -.
DR OMA; TCKACSC; -.
DR Proteomes; UP000264840; 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; 2.
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; 2.
DR Pfam; PF00193; Xlink; 1.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00554; FAS1; 1.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF82153; FAS1 domain; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50213; FAS1; 2.
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:UP000264840};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 568..592
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..45
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DOMAIN 107..147
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 190..230
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 231..273
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 306..399
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 419..553
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DISULFID 137..146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 328..397
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 352..373
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 682 AA; 74778 MW; F90DC7A0AEB1748C CRC64;
MYQPVTIFLP SDGVMASLPQ EQKDFLFHQH NRPQLMEYLK YHILPIFNKL TASVRLSLEG
NVSVFCVQEV QKCDLPTFSF AKNTGCRPIC TFNMWEPKCC RGYYGRDCLG CPGGFRSPCN
NRGKCDDGQL GNGTCTCDTG FRGTSCELCS DGFYGPTCKA CNCSEHGSCD DGWKGTGLCF
CEAGWTGDRL VDICQIWNGG CAKGAKCSQN GGKVSCTCPK DHTGDGFTCQ PIDPCALGDN
GGCHEHAVCT MTAPGRRKCM CKNNYIGDGV TCEVRQLPIS RCLQNNGQCH RDAKCTDLHF
EDSMLGVFHY RSKKGQYKLN YTAAEQACAA EGGRLATYTQ LAYAQQGGLN MCAAGWLDQA
RVAYPTTYSN PKCGFGHVGI VDYGTRKNLS ETWDTFCYRM QEVKCECKRG YTGDGFSCTG
NLLQVLRSTP SFSNFLTQIL NCSQASESGK QLVQRLSNLT VQSTLFVPDN SGLPSNQTLS
LRDIEFHLSE GQAFPLSQLK NGSRIRTRVG SLTVLGVADQ LDPSSFRYIN DHFVSDSDIM
AANGIIHVIQ GPLKAPAPHP QMHVAHKAGM GIGVVLLIAL VGGAIFVGYR FYRNNTKPFQ
FHYFKEDDGE EEAPPTNSSR NICNPVYEAA PAAGESSASA VTVSHRRTFV QRRMKAVTND
QTAVCSRFTA RSVSFKPFRL SL
//
