GenomeNet

Database: UniProt
Entry: Q96QV1
LinkDB: Q96QV1
Original site: Q96QV1 
ID   HHIP_HUMAN              Reviewed;         700 AA.
AC   Q96QV1; Q6PK09; Q8NCI7; Q9BXK3; Q9H1J4; Q9H7E7;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 3.
DT   13-FEB-2019, entry version 143.
DE   RecName: Full=Hedgehog-interacting protein;
DE            Short=HHIP;
DE            Short=HIP;
DE   Flags: Precursor;
GN   Name=HHIP; Synonyms=HIP; ORFNames=UNQ5825/PRO19644;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT ILE-341,
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Fetal brain;
RA   Huo L., Roessler E., Dutra A., Chuang P.-T., McMahon A.P., Muenke M.;
RT   "Determination of the chromosomal location and genomic structure of
RT   the Hedgehog-interacting protein gene, and analysis of its role in
RT   holoprosencephaly.";
RL   Gene Funct. Dis. 1:119-127(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=11435703;
RA   Bak M., Hansen C., Friis Henriksen K., Tommerup N.;
RT   "The human hedgehog-interacting protein gene: structure and chromosome
RT   mapping to 4q31.21-->q31.3.";
RL   Cytogenet. Cell Genet. 92:300-303(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   ILE-341.
RC   TISSUE=Coronary arterial endothelium, and Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=11472839; DOI=10.1016/S0925-4773(01)00427-0;
RA   Pathi S., Pagan-Westphal S., Baker D.P., Garber E.A., Rayhorn P.,
RA   Bumcrot D., Tabin C.J., Blake Pepinsky R., Williams K.P.;
RT   "Comparative biological responses to human Sonic, Indian, and Desert
RT   hedgehog.";
RL   Mech. Dev. 106:107-117(2001).
RN   [8]
RP   POLYMORPHISM.
RX   PubMed=18391950; DOI=10.1038/ng.125;
RA   Lettre G., Jackson A.U., Gieger C., Schumacher F.R., Berndt S.I.,
RA   Sanna S., Eyheramendy S., Voight B.F., Butler J.L., Guiducci C.,
RA   Illig T., Hackett R., Heid I.M., Jacobs K.B., Lyssenko V., Uda M.,
RA   Boehnke M., Chanock S.J., Groop L.C., Hu F.B., Isomaa B., Kraft P.,
RA   Peltonen L., Salomaa V., Schlessinger D., Hunter D.J., Hayes R.B.,
RA   Abecasis G.R., Wichmann H.-E., Mohlke K.L., Hirschhorn J.N.;
RT   "Identification of ten loci associated with height highlights new
RT   biological pathways in human growth.";
RL   Nat. Genet. 40:584-591(2008).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 193-667 IN COMPLEX WITH SHH,
RP   INTERACTION WITH SHH, FUNCTION, MUTAGENESIS OF GLU-380; MET-382;
RP   ASP-383 AND ASP-387, AND DISULFIDE BONDS.
RX   PubMed=19561609; DOI=10.1038/nsmb.1632;
RA   Bosanac I., Maun H.R., Scales S.J., Wen X., Lingel A., Bazan J.F.,
RA   de Sauvage F.J., Hymowitz S.G., Lazarus R.A.;
RT   "The structure of SHH in complex with HHIP reveals a recognition role
RT   for the Shh pseudo active site in signaling.";
RL   Nat. Struct. Mol. Biol. 16:691-697(2009).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 214-670 IN COMPLEX WITH SHH,
RP   INTERACTION WITH SHH AND DHH, DISULFIDE BONDS, MUTAGENESIS OF ASP-383,
RP   AND GLYCOSYLATION AT ASN-447.
RX   PubMed=19561611; DOI=10.1038/nsmb.1607;
RA   Bishop B., Aricescu A.R., Harlos K., O'Callaghan C.A., Jones E.Y.,
RA   Siebold C.;
RT   "Structural insights into hedgehog ligand sequestration by the human
RT   hedgehog-interacting protein HHIP.";
RL   Nat. Struct. Mol. Biol. 16:698-703(2009).
CC   -!- FUNCTION: Modulates hedgehog signaling in several cell types
CC       including brain and lung through direct interaction with members
CC       of the hedgehog family. {ECO:0000269|PubMed:11472839,
CC       ECO:0000269|PubMed:19561609}.
CC   -!- SUBUNIT: Interacts with all three hedgehog family members, SHH,
CC       IHH and DHH. {ECO:0000269|PubMed:11472839,
CC       ECO:0000269|PubMed:19561609, ECO:0000269|PubMed:19561611}.
CC   -!- INTERACTION:
CC       O43323:DHH; NbExp=4; IntAct=EBI-15791478, EBI-11667804;
CC       Q15465:SHH; NbExp=10; IntAct=EBI-6598521, EBI-11666886;
CC       Q62226:Shh (xeno); NbExp=4; IntAct=EBI-15791478, EBI-15610166;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}. Secreted {ECO:0000250}. Note=The
CC       last 22 C-terminal amino acids may participate in cell membrane
CC       attachment.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96QV1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96QV1-2; Sequence=VSP_013192, VSP_013193;
CC         Note=Potentially soluble form.;
CC   -!- TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues.
CC       Highest expression in adult heart, liver and pancreas, and in
CC       fetal kidney. {ECO:0000269|PubMed:11435703, ECO:0000269|Ref.1}.
CC   -!- DOMAIN: A flexible loop interacts with the SHH zinc binding site
CC       and contributes to zinc binding.
CC   -!- POLYMORPHISM: Genetic variations in HHIP define the stature
CC       quantitative trait locus 12 (STQTL12) [MIM:612224]. Adult height
CC       is an easily observable and highly heritable complex continuous
CC       trait. Because of this, it is a model trait for studying genetic
CC       influence on quantitative traits. {ECO:0000269|PubMed:18391950}.
CC   -!- SIMILARITY: Belongs to the HHIP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB14945.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; AY009951; AAG34731.1; -; mRNA.
DR   EMBL; AF326471; AAK18182.1; -; Genomic_DNA.
DR   EMBL; AF326459; AAK18182.1; JOINED; Genomic_DNA.
DR   EMBL; AF326460; AAK18182.1; JOINED; Genomic_DNA.
DR   EMBL; AF326462; AAK18182.1; JOINED; Genomic_DNA.
DR   EMBL; AF326464; AAK18182.1; JOINED; Genomic_DNA.
DR   EMBL; AF326466; AAK18182.1; JOINED; Genomic_DNA.
DR   EMBL; AF326468; AAK18182.1; JOINED; Genomic_DNA.
DR   EMBL; AF326470; AAK18182.1; JOINED; Genomic_DNA.
DR   EMBL; AF326469; AAK18182.1; JOINED; Genomic_DNA.
DR   EMBL; AF326467; AAK18182.1; JOINED; Genomic_DNA.
DR   EMBL; AF326465; AAK18182.1; JOINED; Genomic_DNA.
DR   EMBL; AF326463; AAK18182.1; JOINED; Genomic_DNA.
DR   EMBL; AF326461; AAK18182.1; JOINED; Genomic_DNA.
DR   EMBL; AY009317; AAG35411.1; -; mRNA.
DR   EMBL; AY358747; AAQ89107.1; -; mRNA.
DR   EMBL; AK024645; BAB14945.1; ALT_INIT; mRNA.
DR   EMBL; AK074711; BAC11154.1; -; mRNA.
DR   EMBL; AC098588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC009298; AAH09298.1; -; mRNA.
DR   EMBL; BC025311; AAH25311.1; -; mRNA.
DR   CCDS; CCDS3762.1; -. [Q96QV1-1]
DR   RefSeq; NP_071920.1; NM_022475.2. [Q96QV1-1]
DR   UniGene; Hs.507991; -.
DR   PDB; 2WFT; X-ray; 2.80 A; A/B=214-671.
DR   PDB; 2WFX; X-ray; 3.20 A; B=214-670.
DR   PDB; 2WG3; X-ray; 2.60 A; C/D=214-670.
DR   PDB; 2WG4; X-ray; 3.15 A; B=214-670.
DR   PDB; 3HO3; X-ray; 2.90 A; A=193-667.
DR   PDB; 3HO4; X-ray; 3.10 A; A/B=193-667.
DR   PDB; 3HO5; X-ray; 3.01 A; A/B=193-667.
DR   PDBsum; 2WFT; -.
DR   PDBsum; 2WFX; -.
DR   PDBsum; 2WG3; -.
DR   PDBsum; 2WG4; -.
DR   PDBsum; 3HO3; -.
DR   PDBsum; 3HO4; -.
DR   PDBsum; 3HO5; -.
DR   ProteinModelPortal; Q96QV1; -.
DR   SMR; Q96QV1; -.
DR   BioGrid; 122156; 1.
DR   DIP; DIP-48536N; -.
DR   IntAct; Q96QV1; 6.
DR   STRING; 9606.ENSP00000296575; -.
DR   iPTMnet; Q96QV1; -.
DR   PhosphoSitePlus; Q96QV1; -.
DR   BioMuta; HHIP; -.
DR   DMDM; 118572655; -.
DR   EPD; Q96QV1; -.
DR   PaxDb; Q96QV1; -.
DR   PeptideAtlas; Q96QV1; -.
DR   PRIDE; Q96QV1; -.
DR   ProteomicsDB; 77909; -.
DR   ProteomicsDB; 77910; -. [Q96QV1-2]
DR   DNASU; 64399; -.
DR   Ensembl; ENST00000296575; ENSP00000296575; ENSG00000164161. [Q96QV1-1]
DR   Ensembl; ENST00000434550; ENSP00000408587; ENSG00000164161. [Q96QV1-2]
DR   GeneID; 64399; -.
DR   KEGG; hsa:64399; -.
DR   UCSC; uc003ijr.3; human. [Q96QV1-1]
DR   CTD; 64399; -.
DR   DisGeNET; 64399; -.
DR   EuPathDB; HostDB:ENSG00000164161.9; -.
DR   GeneCards; HHIP; -.
DR   HGNC; HGNC:14866; HHIP.
DR   HPA; HPA012616; -.
DR   MIM; 606178; gene.
DR   MIM; 612224; phenotype.
DR   neXtProt; NX_Q96QV1; -.
DR   OpenTargets; ENSG00000164161; -.
DR   PharmGKB; PA29276; -.
DR   eggNOG; ENOG410IEIH; Eukaryota.
DR   eggNOG; ENOG410ZT1I; LUCA.
DR   GeneTree; ENSGT00940000158660; -.
DR   HOGENOM; HOG000008644; -.
DR   HOVERGEN; HBG051901; -.
DR   InParanoid; Q96QV1; -.
DR   KO; K06231; -.
DR   OMA; FYYTCRG; -.
DR   OrthoDB; 728630at2759; -.
DR   PhylomeDB; Q96QV1; -.
DR   TreeFam; TF329059; -.
DR   Reactome; R-HSA-5632681; Ligand-receptor interactions.
DR   SignaLink; Q96QV1; -.
DR   SIGNOR; Q96QV1; -.
DR   ChiTaRS; HHIP; human.
DR   EvolutionaryTrace; Q96QV1; -.
DR   GeneWiki; HHIP; -.
DR   GenomeRNAi; 64399; -.
DR   PRO; PR:Q96QV1; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000164161; Expressed in 149 organ(s), highest expression level in corpus callosum.
DR   Genevisible; Q96QV1; HS.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0060170; C:ciliary membrane; TAS:Reactome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:BHF-UCL.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0097108; F:hedgehog family protein binding; IPI:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR   GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IDA:UniProtKB.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR   GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0048705; P:skeletal system morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR   Gene3D; 2.120.10.30; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR018143; Folate_rcpt-like.
DR   InterPro; IPR012938; Glc/Sorbosone_DH.
DR   InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR   Pfam; PF03024; Folate_rec; 1.
DR   Pfam; PF07995; GSDH; 1.
DR   SMART; SM00181; EGF; 2.
DR   SUPFAM; SSF50952; SSF50952; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Complete proteome;
KW   Cytoplasm; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Metal-binding; Polymorphism; Reference proteome; Repeat; Secreted;
KW   Signal; Zinc.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   CHAIN        18    700       Hedgehog-interacting protein.
FT                                /FTId=PRO_0000007623.
FT   DOMAIN      607    634       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      635    667       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REGION      376    388       Interaction with SHH zinc binding site.
FT   COMPBIAS     35     54       Arg-rich.
FT   METAL       383    383       Zinc; shared with SHH.
FT   CARBOHYD     99     99       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    416    416       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    447    447       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19561611}.
FT   CARBOHYD    459    459       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    216    536
FT   DISULFID    218    543
FT   DISULFID    402    624
FT   DISULFID    435    452
FT   DISULFID    500    594
FT   DISULFID    608    617
FT   DISULFID    612    623
FT   DISULFID    625    634
FT   DISULFID    639    649
FT   DISULFID    643    655
FT   DISULFID    657    666
FT   VAR_SEQ     278    320       GGDERGLLSLAFHPNYKKNGKLYVSYTTNQERWAIGPHDHI
FT                                LR -> VGFLNFIYFCAGYVNFILVLPSSLKVFLCNKRKNL
FT                                AGENKGAT (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_013192.
FT   VAR_SEQ     321    700       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_013193.
FT   VARIANT     341    341       V -> I. {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|Ref.1}.
FT                                /FTId=VAR_021518.
FT   MUTAGEN     380    380       E->A: Abolishes SHH binding.
FT                                {ECO:0000269|PubMed:19561609}.
FT   MUTAGEN     382    382       M->A: Abolishes SHH binding.
FT                                {ECO:0000269|PubMed:19561609}.
FT   MUTAGEN     383    383       D->A,R: Abolishes SHH binding.
FT                                {ECO:0000269|PubMed:19561609,
FT                                ECO:0000269|PubMed:19561611}.
FT   MUTAGEN     387    387       D->A: Abolishes SHH binding.
FT                                {ECO:0000269|PubMed:19561609}.
FT   CONFLICT    126    126       P -> L (in Ref. 4; BAC11154).
FT                                {ECO:0000305}.
FT   CONFLICT    135    135       L -> I (in Ref. 1; AAG34731).
FT                                {ECO:0000305}.
FT   CONFLICT    173    173       R -> G (in Ref. 4; BAC11154).
FT                                {ECO:0000305}.
FT   STRAND      217    233       {ECO:0000244|PDB:2WG3}.
FT   STRAND      236    239       {ECO:0000244|PDB:2WG3}.
FT   STRAND      242    246       {ECO:0000244|PDB:2WG3}.
FT   TURN        247    249       {ECO:0000244|PDB:2WG3}.
FT   STRAND      250    254       {ECO:0000244|PDB:2WG3}.
FT   STRAND      256    258       {ECO:0000244|PDB:2WG4}.
FT   STRAND      265    267       {ECO:0000244|PDB:2WG3}.
FT   TURN        269    271       {ECO:0000244|PDB:2WG3}.
FT   STRAND      277    279       {ECO:0000244|PDB:2WG3}.
FT   STRAND      283    289       {ECO:0000244|PDB:2WG3}.
FT   HELIX       293    296       {ECO:0000244|PDB:2WG3}.
FT   STRAND      298    305       {ECO:0000244|PDB:2WG3}.
FT   STRAND      312    315       {ECO:0000244|PDB:2WG3}.
FT   STRAND      317    326       {ECO:0000244|PDB:2WG3}.
FT   HELIX       336    338       {ECO:0000244|PDB:2WG3}.
FT   STRAND      340    352       {ECO:0000244|PDB:2WG3}.
FT   STRAND      354    359       {ECO:0000244|PDB:2WG3}.
FT   HELIX       361    363       {ECO:0000244|PDB:3HO5}.
FT   STRAND      365    369       {ECO:0000244|PDB:2WG3}.
FT   HELIX       376    381       {ECO:0000244|PDB:2WG3}.
FT   STRAND      391    396       {ECO:0000244|PDB:2WG3}.
FT   STRAND      402    405       {ECO:0000244|PDB:2WFT}.
FT   TURN        413    416       {ECO:0000244|PDB:2WG3}.
FT   STRAND      418    420       {ECO:0000244|PDB:2WG3}.
FT   STRAND      424    427       {ECO:0000244|PDB:2WG3}.
FT   STRAND      430    432       {ECO:0000244|PDB:3HO3}.
FT   STRAND      434    440       {ECO:0000244|PDB:2WG3}.
FT   STRAND      442    445       {ECO:0000244|PDB:2WG4}.
FT   STRAND      447    453       {ECO:0000244|PDB:2WG3}.
FT   STRAND      457    459       {ECO:0000244|PDB:3HO3}.
FT   STRAND      463    468       {ECO:0000244|PDB:2WG3}.
FT   STRAND      481    483       {ECO:0000244|PDB:3HO3}.
FT   STRAND      491    496       {ECO:0000244|PDB:2WG3}.
FT   TURN        503    507       {ECO:0000244|PDB:2WG3}.
FT   STRAND      509    513       {ECO:0000244|PDB:2WG3}.
FT   STRAND      514    516       {ECO:0000244|PDB:3HO3}.
FT   STRAND      518    522       {ECO:0000244|PDB:2WG3}.
FT   STRAND      525    528       {ECO:0000244|PDB:2WG3}.
FT   STRAND      531    535       {ECO:0000244|PDB:2WG3}.
FT   STRAND      537    539       {ECO:0000244|PDB:2WG3}.
FT   STRAND      543    545       {ECO:0000244|PDB:2WFT}.
FT   STRAND      549    556       {ECO:0000244|PDB:2WG3}.
FT   STRAND      558    560       {ECO:0000244|PDB:3HO3}.
FT   STRAND      562    569       {ECO:0000244|PDB:2WG3}.
FT   HELIX       571    573       {ECO:0000244|PDB:2WG3}.
FT   STRAND      575    583       {ECO:0000244|PDB:2WG3}.
FT   STRAND      587    590       {ECO:0000244|PDB:2WFT}.
FT   HELIX       592    594       {ECO:0000244|PDB:2WG3}.
FT   HELIX       607    611       {ECO:0000244|PDB:2WG3}.
FT   STRAND      614    617       {ECO:0000244|PDB:2WG3}.
FT   STRAND      623    625       {ECO:0000244|PDB:2WG3}.
FT   STRAND      629    631       {ECO:0000244|PDB:2WG3}.
FT   STRAND      644    646       {ECO:0000244|PDB:2WFX}.
FT   STRAND      648    651       {ECO:0000244|PDB:2WFT}.
FT   STRAND      654    656       {ECO:0000244|PDB:2WFT}.
FT   STRAND      661    663       {ECO:0000244|PDB:2WFT}.
SQ   SEQUENCE   700 AA;  78851 MW;  CC1CB3435E29303A CRC64;
     MLKMLSFKLL LLAVALGFFE GDAKFGERNE GSGARRRRCL NGNPPKRLKR RDRRMMSQLE
     LLSGGEMLCG GFYPRLSCCL RSDSPGLGRL ENKIFSVTNN TECGKLLEEI KCALCSPHSQ
     SLFHSPEREV LERDLVLPLL CKDYCKEFFY TCRGHIPGFL QTTADEFCFY YARKDGGLCF
     PDFPRKQVRG PASNYLDQME EYDKVEEISR KHKHNCFCIQ EVVSGLRQPV GALHSGDGSQ
     RLFILEKEGY VKILTPEGEI FKEPYLDIHK LVQSGIKGGD ERGLLSLAFH PNYKKNGKLY
     VSYTTNQERW AIGPHDHILR VVEYTVSRKN PHQVDLRTAR VFLEVAELHR KHLGGQLLFG
     PDGFLYIILG DGMITLDDME EMDGLSDFTG SVLRLDVDTD MCNVPYSIPR SNPHFNSTNQ
     PPEVFAHGLH DPGRCAVDRH PTDININLTI LCSDSNGKNR SSARILQIIK GKDYESEPSL
     LEFKPFSNGP LVGGFVYRGC QSERLYGSYV FGDRNGNFLT LQQSPVTKQW QEKPLCLGTS
     GSCRGYFSGH ILGFGEDELG EVYILSSSKS MTQTHNGKLY KIVDPKRPLM PEECRATVQP
     AQTLTSECSR LCRNGYCTPT GKCCCSPGWE GDFCRTAKCE PACRHGGVCV RPNKCLCKKG
     YLGPQCEQVD RNIRRVTRAG ILDQIIDMTS YLLDLTSYIV
//
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