ID A0A3Q1G199_9TELE Unreviewed; 777 AA.
AC A0A3Q1G199;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=HHIP-like protein 1 {ECO:0000313|Ensembl:ENSAPOP00000012155.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000012155.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000012155.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the HHIP family.
CC {ECO:0000256|ARBA:ARBA00010658}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR AlphaFoldDB; A0A3Q1G199; -.
DR Ensembl; ENSAPOT00000031904.1; ENSAPOP00000012155.1; ENSAPOG00000014879.1.
DR GeneTree; ENSGT00940000164056; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR018143; Folate_rcpt-like.
DR InterPro; IPR012938; Glc/Sorbosone_DH.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR19328; HEDGEHOG-INTERACTING PROTEIN; 1.
DR PANTHER; PTHR19328:SF58; HHIP-LIKE PROTEIN 1; 1.
DR Pfam; PF03024; Folate_rec; 1.
DR Pfam; PF07995; GSDH; 1.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR PROSITE; PS50287; SRCR_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..41
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 42..777
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018528951"
FT DOMAIN 674..777
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DISULFID 746..756
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 777 AA; 87469 MW; BC5442EED4B5FC20 CRC64;
MNVQTCNLVP RCILQPAFSR HLLLPVLLLL LLQAWWGSCH PQCLDYKPPF QPHQPLVFCK
EYSKFGCCDV EKDEQISQRF YTIMENFDHS GYSTCGRYIR SILCQECSPY AAHLYDAEDA
NTPMRILPGL CGDYCSDYWH QCRYTLSLLL EDSGSPQQFA NLTAIIEEDR RKFCDFLELK
DKQYCYPNVL TNAELNANLG LVREDPKGCL ELCLQEVANG LRNPVAMIHA DDGTHRFFVA
EQLGYVWVYL ANGSRIDRPF LNLTQAVLTS PWAGDERGFL CIALHPRFTT VRKAYVYYSV
SVKKEERIRI SEFTLSVLDD NQLDHSSERT IMEVVEPASN HNGGQLLFGH DGYLYIFIGD
GGRAGDPFGK FGNSQNKSVL LGKVLRIDVD NNDDSAPYSI PSDNPFLGEK ETRPEIYAYG
VRNMWRCSID RGDPATGAGR GRMFCGDVGQ NKYEEVDLIV KGGNYGWRAK EGFSCYDRKL
CQNSSLDDIL PIFAYPHKLG KSVTGGYIYR GCQMPNLNGL YIFGDFMSGR LMSLKENTTT
GEWQYTEICM GRGQTCRFPK LIDSHYKYII SFAEDEAGEL YFLATGVPSA TRRTGVIYKI
VDPSRRAAPG KCSIKPSPVK IKGKLVHFYP REGKGNPTIL VISFFFFFSV PKPRGKGRDY
KKGRDGRRLR GGSVRLVSTD GLLDRGRVEI FLRGEWGTVC DDLFSANAGS VVCRQLGFTK
ALAVMKRAVL GEADSSVRIL LDDVECEGGE RSLLECKRSR VGKHNCSHRE DVGVICG
//
