ID   RHG36_HUMAN             Reviewed;         547 AA.
AC   Q6ZRI8; B7Z234; B7Z439; Q5JRL9; Q5JRM0; Q5JRM1; Q96NU6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Rho GTPase-activating protein 36;
DE   Flags: Precursor;
GN   Name=ARHGAP36;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC   TISSUE=Adrenal gland, Amygdala, Testis, and Tongue;
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=PNS;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY, INTERACTION WITH RAC1, AND INVOLVEMENT IN BDCS.
RX   PubMed=35986704; DOI=10.1111/bjd.21842;
RA   Liu Y., Banka S., Huang Y., Hardman-Smart J., Pye D., Torrelo A.,
RA   Beaman G.M., Kazanietz M.G., Baker M.J., Ferrazzano C., Shi C., Orozco G.,
RA   Eyre S., van Geel M., Bygum A., Fischer J., Miedzybrodzka Z., Abuzahra F.,
RA   Ruebben A., Cuvertino S., Ellingford J.M., Smith M.J., Evans D.G.,
RA   Weppner-Parren L.J.M.T., van Steensel M.A.M., Chaudhary I.H., Mangham D.C.,
RA   Lear J.T., Paus R., Frank J., Newman W.G., Zhang X.;
RT   "Germline intergenic duplications at Xq26.1 underlie Bazex-Dupre-Christol
RT   basal cell carcinoma susceptibility syndrome.";
RL   Br. J. Dermatol. 187:948-961(2022).
CC   -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC       to an inactive GDP-bound state. {ECO:0000250}.
CC   -!- SUBUNIT: May interacts (via the Rho-GAP domain) with the active form of
CC       RAC1. {ECO:0000269|PubMed:35986704}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q6ZRI8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZRI8-2; Sequence=VSP_021358;
CC       Name=3;
CC         IsoId=Q6ZRI8-3; Sequence=VSP_021357;
CC       Name=4;
CC         IsoId=Q6ZRI8-4; Sequence=VSP_039236;
CC       Name=5;
CC         IsoId=Q6ZRI8-5; Sequence=VSP_039235;
CC   -!- TISSUE SPECIFICITY: Detected in the outer root sheath of hair follicles
CC       at the level of the stem cell bulge, during the anagen and telogen
CC       phases of hair growth (at protein level).
CC       {ECO:0000269|PubMed:35986704}.
CC   -!- DISEASE: Bazex-Dupre-Christol syndrome (BDCS) [MIM:301845]: An X-linked
CC       dominant disorder characterized by a triad of congenital hypotrichosis,
CC       follicular atrophoderma affecting the dorsa of the hands and feet, the
CC       face and extensor surfaces of the elbows or knees, and the development
CC       of basocellular neoplasms including basal cell nevi and basal cell
CC       carcinomas from the second decade onwards. Other reported features
CC       include associated hair shaft abnormalities (pili torti and
CC       trichorrhexis nodosa) admixed with hypotrichosis, prominent milia
CC       affecting the face, hypohidrosis, pinched nose with hypoplastic nasal
CC       alae and prominent columella, atopic diathesis with comedones,
CC       keratosis pilaris, joint hypermobility, lingua plicata and
CC       hyperpigmentation of the forehead. {ECO:0000269|PubMed:35986704}.
CC       Note=The gene represented in this entry may be involved in disease
CC       pathogenesis. In patients with Bazex-Dupre-Christol syndrome, ARHGAP36
CC       is overexpressed in hair follicles during telogen, in basal cell
CC       carcinomas, and in trichoepitheliomas. This is due to small
CC       duplications in an intergenic region on chromosome Xq26 that harbor
CC       non-coding enhancer elements that control ARHGAP36 expression, and are
CC       responsible for disease development. {ECO:0000269|PubMed:35986704}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH63790.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK054620; BAB70776.1; -; mRNA.
DR   EMBL; AK128203; BAC87322.1; -; mRNA.
DR   EMBL; AK294274; BAH11720.1; -; mRNA.
DR   EMBL; AK296748; BAH12425.1; -; mRNA.
DR   EMBL; AL590131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471107; EAX11793.1; -; Genomic_DNA.
DR   EMBL; BC063790; AAH63790.1; ALT_INIT; mRNA.
DR   CCDS; CCDS14628.1; -. [Q6ZRI8-1]
DR   CCDS; CCDS65320.1; -. [Q6ZRI8-4]
DR   CCDS; CCDS83489.1; -. [Q6ZRI8-3]
DR   RefSeq; NP_001269536.1; NM_001282607.1. [Q6ZRI8-4]
DR   RefSeq; NP_001317580.1; NM_001330651.1. [Q6ZRI8-3]
DR   RefSeq; NP_659404.2; NM_144967.3. [Q6ZRI8-1]
DR   RefSeq; XP_011529582.1; XM_011531280.1. [Q6ZRI8-3]
DR   AlphaFoldDB; Q6ZRI8; -.
DR   SMR; Q6ZRI8; -.
DR   BioGRID; 127703; 119.
DR   IntAct; Q6ZRI8; 72.
DR   STRING; 9606.ENSP00000276211; -.
DR   GlyCosmos; Q6ZRI8; 2 sites, 1 glycan.
DR   GlyGen; Q6ZRI8; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q6ZRI8; -.
DR   PhosphoSitePlus; Q6ZRI8; -.
DR   BioMuta; ARHGAP36; -.
DR   DMDM; 74722974; -.
DR   jPOST; Q6ZRI8; -.
DR   MassIVE; Q6ZRI8; -.
DR   PaxDb; 9606-ENSP00000276211; -.
DR   PeptideAtlas; Q6ZRI8; -.
DR   ProteomicsDB; 68137; -. [Q6ZRI8-1]
DR   ProteomicsDB; 68138; -. [Q6ZRI8-2]
DR   ProteomicsDB; 68139; -. [Q6ZRI8-3]
DR   ProteomicsDB; 68140; -. [Q6ZRI8-4]
DR   ProteomicsDB; 68141; -. [Q6ZRI8-5]
DR   TopDownProteomics; Q6ZRI8-1; -. [Q6ZRI8-1]
DR   Antibodypedia; 423; 130 antibodies from 23 providers.
DR   DNASU; 158763; -.
DR   Ensembl; ENST00000276211.10; ENSP00000276211.5; ENSG00000147256.12. [Q6ZRI8-1]
DR   Ensembl; ENST00000370921.1; ENSP00000359959.1; ENSG00000147256.12. [Q6ZRI8-3]
DR   Ensembl; ENST00000370922.5; ENSP00000359960.1; ENSG00000147256.12. [Q6ZRI8-4]
DR   Ensembl; ENST00000412432.6; ENSP00000408515.2; ENSG00000147256.12. [Q6ZRI8-2]
DR   Ensembl; ENST00000639280.1; ENSP00000492307.1; ENSG00000147256.12. [Q6ZRI8-3]
DR   GeneID; 158763; -.
DR   KEGG; hsa:158763; -.
DR   MANE-Select; ENST00000276211.10; ENSP00000276211.5; NM_144967.4; NP_659404.2.
DR   UCSC; uc004evz.5; human. [Q6ZRI8-1]
DR   AGR; HGNC:26388; -.
DR   CTD; 158763; -.
DR   DisGeNET; 158763; -.
DR   GeneCards; ARHGAP36; -.
DR   HGNC; HGNC:26388; ARHGAP36.
DR   HPA; ENSG00000147256; Group enriched (adrenal gland, brain, pituitary gland).
DR   MIM; 300937; gene.
DR   MIM; 301845; phenotype.
DR   neXtProt; NX_Q6ZRI8; -.
DR   OpenTargets; ENSG00000147256; -.
DR   PharmGKB; PA165756384; -.
DR   VEuPathDB; HostDB:ENSG00000147256; -.
DR   eggNOG; KOG2710; Eukaryota.
DR   GeneTree; ENSGT00940000153904; -.
DR   HOGENOM; CLU_012874_1_1_1; -.
DR   InParanoid; Q6ZRI8; -.
DR   OMA; NTFEKWF; -.
DR   OrthoDB; 5482290at2759; -.
DR   PhylomeDB; Q6ZRI8; -.
DR   TreeFam; TF316710; -.
DR   PathwayCommons; Q6ZRI8; -.
DR   SignaLink; Q6ZRI8; -.
DR   BioGRID-ORCS; 158763; 13 hits in 764 CRISPR screens.
DR   GenomeRNAi; 158763; -.
DR   Pharos; Q6ZRI8; Tbio.
DR   PRO; PR:Q6ZRI8; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q6ZRI8; Protein.
DR   Bgee; ENSG00000147256; Expressed in adrenal tissue and 95 other cell types or tissues.
DR   ExpressionAtlas; Q6ZRI8; baseline and differential.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd04376; RhoGAP_ARHGAP6; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR041852; ARHGAP6_RhoGAP.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR037863; RHOGAP6/36.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR12635:SF8; RHO GTPASE-ACTIVATING PROTEIN 36; 1.
DR   PANTHER; PTHR12635; RHO-GTPASE-ACTIVATING PROTEIN 6 FAMILY MEMBER; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   Genevisible; Q6ZRI8; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; GTPase activation; Hypotrichosis; Reference proteome;
KW   Signal.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..547
FT                   /note="Rho GTPase-activating protein 36"
FT                   /id="PRO_0000256699"
FT   DOMAIN          226..426
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          485..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..520
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..136
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_021357"
FT   VAR_SEQ         1..48
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_039235"
FT   VAR_SEQ         1..32
FT                   /note="MGGCIPFLKAARALCPRIMPPLLLLSAFIFLV -> M (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021358"
FT   VAR_SEQ         1..31
FT                   /note="MGGCIPFLKAARALCPRIMPPLLLLSAFIFL -> MAWILDCLFASAFEPRP
FT                   RR (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_039236"
FT   CONFLICT        340
FT                   /note="H -> R (in Ref. 1; BAH12425)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   547 AA;  61664 MW;  28EB8168F3928DF9 CRC64;
     MGGCIPFLKA ARALCPRIMP PLLLLSAFIF LVSVLGGAPG HNPDRRTKMV SIHSLSELER
     LKLQETAYHE LVARHFLSEF KPDRALPIDR PNTLDKWFLI LRGQQRAVSH KTFGISLEEV
     LVNEFTRRKH LELTATMQVE EATGQAAGRR RGNVVRRVFG RIRRFFSRRR NEPTLPREFT
     RRGRRGAVSV DSLAELEDGA LLLQTLQLSK ISFPIGQRLL GSKRKMSLNP IAKQIPQVVE
     ACCQFIEKHG LSAVGIFTLE YSVQRVRQLR EEFDQGLDVV LDDNQNVHDV AALLKEFFRD
     MKDSLLPDDL YMSFLLTATL KPQDQLSALQ LLVYLMPPCH SDTLERLLKA LHKITENCED
     SIGIDGQLVP GNRMTSTNLA LVFGSALLKK GKFGKRESRK TKLGIDHYVA SVNVVRAMID
     NWDVLFQVPP HIQRQVAKRV WKSSPEALDF IRRRNLRKIQ SARIKMEEDA LLSDPVETSA
     EARAAVLAQS KPSDEGSSEE PAVPSGTARS HDDEEGAGNP PIPEQDRPLL RVPREKEAKT
     GVSYFFP
//