ID A0A096NQ75_PAPAN Unreviewed; 411 AA.
AC A0A096NQ75;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Hedgehog protein {ECO:0000256|RuleBase:RU280812};
GN Name=IHH {ECO:0000313|Ensembl:ENSPANP00000015169.3};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000015169.3, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000015169.3, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000015169.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog
CC protein N-product is a morphogen which is essential for a variety of
CC patterning events during development. {ECO:0000256|RuleBase:RU280812}.
CC -!- FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog
CC protein precursor displays an autoproteolysis activity that results in
CC the cleavage of the full-length protein into two parts (N-product and
CC C-product). In addition, the C-terminal part displays a cholesterol
CC transferase activity that results by the covalent attachment of a
CC cholesterol moiety to the C-terminal of the newly generated N-product.
CC {ECO:0000256|RuleBase:RU280812}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-
CC C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-
CC [protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-
CC COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135,
CC ChEBI:CHEBI:143140; Evidence={ECO:0000256|ARBA:ARBA00034065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505;
CC Evidence={ECO:0000256|ARBA:ARBA00034065};
CC -!- SUBUNIT: Multimer. {ECO:0000256|ARBA:ARBA00034131}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SUBCELLULAR LOCATION: [Sonic hedgehog protein]: Endoplasmic reticulum
CC membrane {ECO:0000256|RuleBase:RU280812}. Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU280812}.
CC -!- SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane
CC {ECO:0000256|RuleBase:RU280812}; Lipid-anchor
CC {ECO:0000256|RuleBase:RU280812}.
CC -!- SIMILARITY: Belongs to the hedgehog family.
CC {ECO:0000256|ARBA:ARBA00010649, ECO:0000256|RuleBase:RU280812}.
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DR AlphaFoldDB; A0A096NQ75; -.
DR SMR; A0A096NQ75; -.
DR STRING; 9555.ENSPANP00000015169; -.
DR Ensembl; ENSPANT00000002631.3; ENSPANP00000015169.3; ENSPANG00000017463.3.
DR eggNOG; KOG3638; Eukaryota.
DR GeneTree; ENSGT00940000159207; -.
DR HOGENOM; CLU_034686_1_0_1; -.
DR OMA; APAVRGC; -.
DR Proteomes; UP000028761; Chromosome 10.
DR Bgee; ENSPANG00000017463; Expressed in ascending colon and 24 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005113; F:patched binding; IEA:Ensembl.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0045453; P:bone resorption; IEA:Ensembl.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0060220; P:camera-type eye photoreceptor cell fate commitment; IEA:Ensembl.
DR GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
DR GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR GO; GO:0003413; P:chondrocyte differentiation involved in endochondral bone morphogenesis; IEA:Ensembl.
DR GO; GO:0035988; P:chondrocyte proliferation; IEA:Ensembl.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0009880; P:embryonic pattern specification; IEA:Ensembl.
DR GO; GO:0072498; P:embryonic skeletal joint development; IEA:Ensembl.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IEA:Ensembl.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0060323; P:head morphogenesis; IEA:Ensembl.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0046639; P:negative regulation of alpha-beta T cell differentiation; IEA:Ensembl.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0048074; P:negative regulation of eye pigmentation; IEA:Ensembl.
DR GO; GO:0033088; P:negative regulation of immature T cell proliferation in thymus; IEA:Ensembl.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0031016; P:pancreas development; IEA:Ensembl.
DR GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IEA:Ensembl.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0016540; P:protein autoprocessing; IEA:InterPro.
DR GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl.
DR GO; GO:0040008; P:regulation of growth; IEA:Ensembl.
DR GO; GO:0003406; P:retinal pigment epithelium development; IEA:Ensembl.
DR GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0061053; P:somite development; IEA:Ensembl.
DR GO; GO:0030704; P:vitelline membrane formation; IEA:Ensembl.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 3.30.1380.10; -; 1.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR InterPro; IPR001657; Hedgehog.
DR InterPro; IPR001767; Hedgehog_Hint.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR000320; Hedgehog_signalling_dom.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR006141; Intein_N.
DR PANTHER; PTHR11889; HEDGEHOG; 1.
DR PANTHER; PTHR11889:SF39; INDIAN HEDGEHOG PROTEIN; 1.
DR Pfam; PF01085; HH_signal; 1.
DR Pfam; PF01079; Hint; 1.
DR PIRSF; PIRSF009400; Peptidase_C46; 1.
DR PRINTS; PR00632; SONICHHOG.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813,
KW ECO:0000256|RuleBase:RU280812};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR009400-2};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU280812};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW ECO:0000256|RuleBase:RU280812};
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU280812};
KW Golgi apparatus {ECO:0000256|RuleBase:RU280812};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU280812};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280812};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR009400-2};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU280812};
KW Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU280812};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR009400-2}.
FT DOMAIN 201..308
FT /note="Hint"
FT /evidence="ECO:0000259|SMART:SM00306"
FT DOMAIN 309..353
FT /note="Hint"
FT /evidence="ECO:0000259|SMART:SM00305"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-2"
FT SITE 202..203
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
FT SITE 248
FT /note="Involved in cholesterol transfer"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
FT SITE 272
FT /note="Involved in auto-cleavage"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
FT SITE 275
FT /note="Essential for auto-cleavage"
FT /evidence="ECO:0000256|PIRSR:PIRSR009400-1"
SQ SEQUENCE 411 AA; 45293 MW; 01696F8D076248AD CRC64;
MSPARLRPRL HFCLLLLLLL VVPAAWGCGP GRVVGSRRRP PRKLVPLAYK QFSPNVPEKT
LGASGRYEGK IARSSERFKE LTPNYNPDII FKDEENTGAD RLMTQRCKDR LNSLAISVMN
QWPGVKLRVT EGWDEDGHHS EESLHYEGRA VDITTSDRDR NKYGLLARLA VEAGFDWVYY
ESKAHVHCSV KSEHSAAAKT GGCFPAGAQV RLESGARVAL SAVRPGDRVL AMGEDGSPTF
SDVLIFLDRE PHRLRAFQVI ETQDPPRRLA LTPAHLLFTA DNHTEPAARF RATFASHVQP
GQYVLVAGVP GLQPARVAAV STHVALGAYA PLTRHGTLVV EDVVASCFAA VADHHLAQLA
FWPLRLFHSL AWGSWTPGEG VHWYPQLLYR LGRLLLEEGS FHPLGMSGAG S
//
