ID FSD1L_HUMAN Reviewed; 530 AA.
AC Q9BXM9; A2A338; A6NKH7; B7Z5S6; B7Z5W3; Q5T879; Q5T880;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 24-JAN-2024, entry version 157.
DE RecName: Full=FSD1-like protein;
DE AltName: Full=Coiled-coil domain-containing protein 10;
DE AltName: Full=FSD1 N-terminal-like protein;
GN Name=FSD1L; Synonyms=CCDC10, CSDUFD1, FSD1CL, FSD1NL;
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 [MRNA] (ISOFORM 3).
RX PubMed=11267680; DOI=10.1016/s0167-4781(01)00178-6;
RA Carim-Todd L., Escarceller M., Estivill X., Sumoy L.;
RT "Characterization of human FSD1, a novel brain specific gene on chromosome
RT 19 with paralogy to 9q31.";
RL Biochim. Biophys. Acta 1518:200-203(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 2 AND 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BXM9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXM9-2; Sequence=VSP_039645;
CC Name=3;
CC IsoId=Q9BXM9-3; Sequence=VSP_039645, VSP_039646, VSP_039647;
CC -!- MISCELLANEOUS: [Isoform 3]: Due to intron retention. {ECO:0000305}.
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DR EMBL; AF316830; AAK26748.1; -; mRNA.
DR EMBL; AK299350; BAH13012.1; -; mRNA.
DR EMBL; AK299491; BAH13049.1; -; mRNA.
DR EMBL; AL158070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS47999.1; -. [Q9BXM9-1]
DR CCDS; CCDS6764.1; -. [Q9BXM9-3]
DR RefSeq; NP_001138785.1; NM_001145313.2. [Q9BXM9-1]
DR RefSeq; NP_001274120.1; NM_001287191.1.
DR RefSeq; NP_001274121.1; NM_001287192.1.
DR RefSeq; NP_114125.1; NM_031919.4. [Q9BXM9-3]
DR RefSeq; XP_016870672.1; XM_017015183.1. [Q9BXM9-2]
DR AlphaFoldDB; Q9BXM9; -.
DR BioGRID; 123772; 5.
DR IntAct; Q9BXM9; 2.
DR STRING; 9606.ENSP00000417492; -.
DR iPTMnet; Q9BXM9; -.
DR PhosphoSitePlus; Q9BXM9; -.
DR BioMuta; FSD1L; -.
DR DMDM; 302393701; -.
DR EPD; Q9BXM9; -.
DR jPOST; Q9BXM9; -.
DR MassIVE; Q9BXM9; -.
DR MaxQB; Q9BXM9; -.
DR PaxDb; 9606-ENSP00000417492; -.
DR PeptideAtlas; Q9BXM9; -.
DR ProteomicsDB; 79458; -. [Q9BXM9-1]
DR ProteomicsDB; 79459; -. [Q9BXM9-2]
DR ProteomicsDB; 79460; -. [Q9BXM9-3]
DR Antibodypedia; 29292; 93 antibodies from 22 providers.
DR DNASU; 83856; -.
DR Ensembl; ENST00000469022.5; ENSP00000487223.1; ENSG00000106701.13. [Q9BXM9-3]
DR Ensembl; ENST00000481272.6; ENSP00000417492.1; ENSG00000106701.13. [Q9BXM9-1]
DR GeneID; 83856; -.
DR KEGG; hsa:83856; -.
DR MANE-Select; ENST00000481272.6; ENSP00000417492.1; NM_001145313.3; NP_001138785.1.
DR UCSC; uc011lvv.3; human. [Q9BXM9-1]
DR AGR; HGNC:13753; -.
DR CTD; 83856; -.
DR DisGeNET; 83856; -.
DR GeneCards; FSD1L; -.
DR HGNC; HGNC:13753; FSD1L.
DR HPA; ENSG00000106701; Tissue enhanced (retina).
DR MIM; 609829; gene.
DR neXtProt; NX_Q9BXM9; -.
DR OpenTargets; ENSG00000106701; -.
DR PharmGKB; PA26931; -.
DR VEuPathDB; HostDB:ENSG00000106701; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000157979; -.
DR InParanoid; Q9BXM9; -.
DR OMA; SSWCIHV; -.
DR OrthoDB; 5386672at2759; -.
DR PhylomeDB; Q9BXM9; -.
DR TreeFam; TF333654; -.
DR PathwayCommons; Q9BXM9; -.
DR SignaLink; Q9BXM9; -.
DR BioGRID-ORCS; 83856; 14 hits in 1145 CRISPR screens.
DR ChiTaRS; FSD1L; human.
DR GenomeRNAi; 83856; -.
DR Pharos; Q9BXM9; Tdark.
DR PRO; PR:Q9BXM9; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9BXM9; Protein.
DR Bgee; ENSG00000106701; Expressed in endothelial cell and 160 other cell types or tissues.
DR ExpressionAtlas; Q9BXM9; baseline and differential.
DR Genevisible; Q9BXM9; HS.
DR CDD; cd00063; FN3; 1.
DR CDD; cd12901; SPRY_PRY_FSD1; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR035742; SPRY/PRY_FSD1.
DR InterPro; IPR003877; SPRY_dom.
DR PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR PANTHER; PTHR24099:SF8; FSD1-LIKE PROTEIN; 1.
DR Pfam; PF00622; SPRY; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..530
FT /note="FSD1-like protein"
FT /id="PRO_0000089405"
FT DOMAIN 137..194
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT DOMAIN 196..300
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 300..506
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 322..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 102..141
FT /evidence="ECO:0000255"
FT COMPBIAS 328..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 6..37
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11267680,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_039645"
FT VAR_SEQ 148..177
FT /note="AARQIKDRVTMASAFRLSLKPKVSDNMTHL -> VHKNCINTLNKGSCIFKK
FT AFLFFFSFGFLY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11267680"
FT /id="VSP_039646"
FT VAR_SEQ 178..530
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11267680"
FT /id="VSP_039647"
FT CONFLICT 39
FT /note="A -> S (in Ref. 2; BAH13012)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="Missing (in Ref. 2; BAH13049)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9BXM9-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q9BXM9-3:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 530 AA; 59578 MW; B2AC94D87F6B6DA1 CRC64;
MDSQKYCFKE NENVTVDKAC FLISNITIGP ESINLQQEAL QRIISTLANK NDEIQNFIDT
LHHTLKGVQE NSSNILSELD EEFDSLYSIL DEVKESMINC IKQEQARKSQ ELQSQISQCN
NALENSEELL EFATRSLDIK EPEEFSKAAR QIKDRVTMAS AFRLSLKPKV SDNMTHLMVD
FSQERQMLQT LKFLPVPKAP EIDPVECLVA DNSVTVAWRM PEEDNKIDHF ILEHRKTNFD
GLPRVKDERC WEIIDNIKGT EYTLSGLKFD SKYMNFRVRA CNKAVAGEYS DPVTLETKAL
NFNLDNSSSH LNLKVEDTCV EWDPTGGKGQ ESKIKGKENK GRSGTPSPKR TSVGSRPPAV
RGSRDRFTGE SYTVLGDTAI ESGQHYWEVK AQKDCKSYSV GVAYKTLGKF DQLGKTNTSW
CIHVNNWLQN TFAAKHNNKV KALDVTVPEK IGVFCDFDGG QLSFYDANSK QLLYSFKTKF
TQPVLPGFMV WCGGLSLSTG MQVPSAVRTL QKSENGMTGS ASSLNNVVTQ
//
