FSIP1_RAT
ID FSIP1_RAT Reviewed; 438 AA.
AC Q66H16;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Fibrous sheath-interacting protein 1;
GN Name=Fsip1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-88 AND SER-89, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SIMILARITY: Belongs to the FSIP1 family. {ECO:0000305}.
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DR EMBL; BC082080; AAH82080.1; -; mRNA.
DR RefSeq; NP_001013096.1; NM_001013078.1.
DR AlphaFoldDB; Q66H16; -.
DR SMR; Q66H16; -.
DR STRING; 10116.ENSRNOP00000007808; -.
DR iPTMnet; Q66H16; -.
DR PhosphoSitePlus; Q66H16; -.
DR PaxDb; Q66H16; -.
DR GeneID; 296074; -.
DR KEGG; rno:296074; -.
DR UCSC; RGD:1306874; rat.
DR CTD; 161835; -.
DR RGD; 1306874; Fsip1.
DR VEuPathDB; HostDB:ENSRNOG00000005888; -.
DR eggNOG; ENOG502RXFB; Eukaryota.
DR HOGENOM; CLU_031884_1_0_1; -.
DR InParanoid; Q66H16; -.
DR OMA; PCKVETA; -.
DR OrthoDB; 608640at2759; -.
DR PhylomeDB; Q66H16; -.
DR TreeFam; TF351151; -.
DR PRO; PR:Q66H16; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000005888; Expressed in testis and 14 other tissues.
DR InterPro; IPR026246; Fsip1.
DR PANTHER; PTHR22012; PTHR22012; 1.
DR Pfam; PF15554; FSIP1; 1.
DR PRINTS; PR02075; FIBSHEATHIP1.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..438
FT /note="Fibrous sheath-interacting protein 1"
FT /id="PRO_0000314921"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 131..157
FT /evidence="ECO:0000255"
FT COMPBIAS 13..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 438 AA; 49568 MW; 47361C2C0CC12A30 CRC64;
MSMDIIKGNL DGISKPASSS RSRPGSRSSN GSLEVLSPEP GPVKIDMVNK LNSGKEGHTS
DSRVEERRKI SDDEWADNPR STEPAQESSD EDSNLSQPQG TPEHSDDPKL EGTDAVLQNA
IHKMHRLDKI LAKRRIREKE IKKQGLEMRI KLWEELKSAK NTEDLENDEE LENTKKFLYL
TSKSAGTAAE PLHCKFEDDL FSVFHTQIPQ ETYENHTEKD FTCDVEKNGP LIKTEKQPFS
NTEAIEPRSE HSQVFIIRNA EHSQDFIKRN IELAKSSRSP VVMVEGEKKR LDELLKGLED
TDSGLSSSEG DQCAWLVPGE GYTLAATESQ QLAEIDIKLQ ELSVDSPAVF SLESQSNKGD
MEHDSNEERN TEPTPGEKIL RDNKEQRDRE SRLRAIDGKL KEINEQVEEC PVITPGKRNE
RITWRWLLAK ILEPECKV