ID A0A3Q3B8W9_KRYMA Unreviewed; 813 AA.
AC A0A3Q3B8W9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=HHIP-like protein 1 {ECO:0000313|Ensembl:ENSKMAP00000026118.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000026118.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000026118.1}
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; A0A3Q3B8W9; -.
DR Ensembl; ENSKMAT00000026445.1; ENSKMAP00000026118.1; ENSKMAG00000019323.1.
DR GeneTree; ENSGT00940000164056; -.
DR OMA; IHINGEW; -.
DR Proteomes; UP000264800; 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:UP000264800};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..813
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018764376"
FT DOMAIN 710..813
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT REGION 640..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..706
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 782..792
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 813 AA; 90430 MW; 622EED9814571F3F CRC64;
MTPQASVLVP PNISWPALFS KLLPLVLLLL LQARWGCCHP QCLDYKPPFG PQQPLVFCKE
YTKFGCCDLS KDEEISSRFY TIMDNFDHSG FTTCGKYIRS ILCQECSPYA AHLYDAEDAN
TPMRVLPGLC RDYCSDYWWE CRYTLSLLLE DLGNPPQFAN LTSAIEEDHK RFCDVLELKD
KQYCYPNVLT NAELNANLGL VREDPKGCLE LCLQEVANGL RNPVAMIHAD DGSHRFFVAE
QLGYVWVYLA NGSRIDRPFL NLTQAVLTSP WAGDERGFLC IALHPRITTV RKAYVYYSVS
VKKEERIRIS EFTLSAHDDN QLDHSSERTI LEVVEPASNH NGGQLLFGHD GYLYIFIGDG
GRAGDPFGKF GNAQNKSALL GKVLRIDVDN NDDGAPYSIP SDNPFIGESG AWPEIYAFGV
RNMWRCSIDR GDPATGAGRG RMFCGDVGQN KYEEIDLIVK GGNYGWRAKE GFSCYDRKLC
QNSSLDDVLP IFAYPHKLGK SVTGGYVYRG CQMPNLNGLY IFGDFMSGRL MSLKEDVATG
EWQYNEICMG RDQTCRFPKL INSYYRYIIS FAEDEAGELY FLATRVASAT ARAGVIYKIV
DPSRRAPPGK CSIKPLPVKI KGKLIHFYPK EALTTTWAPY SSQKPTVTPT QKQKTPASTT
APGARDDKPS PGKKLASAAE GNQVHKRPRG RGGHGSKKRR GGKRRPAGTV RLVSADGSSD
RGRVEIFIRG EWGTVCDDLF TGKAGSVVCR QLGFTTALAV MKRAVLGAAD RRVRILLDDV
ECDGGERSLL DCKRSRVGKH NCSHEEDVGV ICA
//