ID A0A1S3SZ67_SALSA Unreviewed; 1008 AA.
AC A0A1S3SZ67;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=HHIP-like protein 1 {ECO:0000313|RefSeq:XP_014069622.1};
GN Name=LOC106612713 {ECO:0000313|RefSeq:XP_014069622.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014069622.1};
RN [1] {ECO:0000313|RefSeq:XP_014069622.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014069622.1};
RG RefSeq;
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}.
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DR RefSeq; XP_014069622.1; XM_014214147.1.
DR AlphaFoldDB; A0A1S3SZ67; -.
DR STRING; 8030.ENSSSAP00000011389; -.
DR PaxDb; 8030-ENSSSAP00000011389; -.
DR GeneID; 106612713; -.
DR KEGG; sasa:106612713; -.
DR OMA; NNDDMDP; -.
DR OrthoDB; 344738at2759; -.
DR Proteomes; UP000087266; Chromosome ssa09.
DR Bgee; ENSSSAG00000005660; Expressed in muscle tissue and 1 other cell type or tissue.
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:UP000087266};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1008
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010360193"
FT DOMAIN 900..1001
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT REGION 642..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..820
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..898
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 926..990
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 939..1000
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 970..980
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 1008 AA; 112458 MW; F7845EFC84459E77 CRC64;
MSGVSVKGVE LLSQWLLVLL VLLAPRHGNT HPQCLDYKPP FQPREPLVFC KEYAKFGCCD
LEKDDKISQN FYKIMDYFDY SGYVTCAKYI RTILCQECSP YSAHLYDAED ANTPMRELPG
LCGDYCSEFW HQCRYTISLL TDNNATAGIE EDRNKFCNFL ELKDREYCYP NVLSDDKLNA
NLGDVRADPE GCLQLCLQEV ANGLRNPVAM VHADDGTHRF FVAEQLGYVW AYLANGSRID
RPFLNLTKAV LTSPWAGDER GFLCMALHPH FTVVRKAYVY YSVSVKKEER IRISEFTLSA
DDMNQLDHSS ERTILEVVEP ASNHNGGQLL FGHDGYLYIF IGDGGRAGDP FGKFGNSQNK
STLLGKVLRL DVDNNDDMDP YSIPSDNPFL GEKGSLPEIY AYGVRNMWRC SIDRGDPITG
QGRGRLFCGD VGQNKFEEVD LIIKGGNYGW RAKEGFSCYD NRLCRNSSLD DILPIFAYPH
KLGKSVTGGY IYRGCQMPNL NGLYIFGDFM SGRLMSLKEN QSTRKWEYKE ICMGKGQTCR
FPKLINSYYK YIISFAEDEA GELYFLATGA PSASARAGVI YKIVDPSRRA PPGKCSFKPT
LVKIKGKLIH FHPTEEFVID KKPMTTAVPT TTARTTATTT LRTPPTTMRS TTTRPTYRPP
TTTLKATAKP ATTRATVKPS TMRATIKPLT TRATVKPSTM RATIKPLTTR ATVKPSTIRA
TIKPLTTRAT VKTAATPSNP TSIQQRPTGT ATPALTTSWR QVMTARPGHA TTLSRQRTSL
SYTRPTVTPK SRPLLTTGAR RPSPPTARPL TRPQPHDTVR PPPLGVTTNR PQTTPRPMYC
TASTKPITQR PNFTLSKAQD KLLKGQSDKI DHSTRNRVNK KDRGSKPGKQ RRRKHRAGSV
RLISAEQLSD RGRVEIYIRG EWGTVCDDLF SSKAATVVCQ QLGFPVALRV AKRAELGGGS
GSILLDDVEC EGTERTLLDC KRAKVGKHNC VHDEDVGVVC GYHHDEDK
//
