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SUCO_RAT
ID   SUCO_RAT                Reviewed;        1253 AA.
AC   Q710E6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=SUN domain-containing ossification factor;
DE   AltName: Full=Membrane protein CH1;
DE   AltName: Full=Protein osteopotentia homolog;
DE   AltName: Full=SUN-like protein 1;
DE   Flags: Precursor;
GN   Name=Suco; Synonyms=Dd25, Opt;
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 [MRNA].
RC   STRAIN=Wistar; TISSUE=Brain;
RA   Verlaet M., Lakaye B., Grisar T.;
RT   "Expression of mRNA encoding C1orf9 in brain structures of Rat.";
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for bone modeling during late embryogenesis.
CC       Regulates type I collagen synthesis in osteoblasts during their
CC       postnatal maturation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC   -!- PTM: O-glycosylated. O-mannosylated by POMT1 and POMT2 and elongated by
CC       POMGNT1. {ECO:0000250|UniProtKB:Q9UBS9}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8C341}.
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DR   EMBL; AJ421447; CAD13342.1; -; mRNA.
DR   RefSeq; NP_955435.1; NM_199403.1.
DR   AlphaFoldDB; Q710E6; -.
DR   SMR; Q710E6; -.
DR   STRING; 10116.ENSRNOP00000068027; -.
DR   GlyGen; Q710E6; 4 sites.
DR   iPTMnet; Q710E6; -.
DR   PhosphoSitePlus; Q710E6; -.
DR   PaxDb; Q710E6; -.
DR   PRIDE; Q710E6; -.
DR   GeneID; 360863; -.
DR   KEGG; rno:360863; -.
DR   UCSC; RGD:735185; rat.
DR   CTD; 51430; -.
DR   RGD; 735185; Suco.
DR   eggNOG; KOG1396; Eukaryota.
DR   InParanoid; Q710E6; -.
DR   OrthoDB; 890782at2759; -.
DR   PhylomeDB; Q710E6; -.
DR   PRO; PR:Q710E6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0046850; P:regulation of bone remodeling; ISS:UniProtKB.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR045120; Suco/Slp1-like.
DR   InterPro; IPR012919; SUN_dom.
DR   PANTHER; PTHR12953; PTHR12953; 1.
DR   Pfam; PF07738; Sad1_UNC; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   PROSITE; PS51469; SUN; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Developmental protein; Endoplasmic reticulum; Glycoprotein;
KW   Membrane; Osteogenesis; Phosphoprotein; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1253
FT                   /note="SUN domain-containing ossification factor"
FT                   /id="PRO_0000302719"
FT   TRANSMEM        1012..1032
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          284..453
FT                   /note="SUN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT   REGION          112..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          719..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1152..1171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          910..1010
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        115..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..748
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1082
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBS9"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        929
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        956
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1253 AA;  139260 MW;  4E21F2371612F8E1 CRC64;
     MKKYRRALAL VSCLSLCSLV WLPSWHVCCK ESSSASTSYY SQDDNCAVGS EDIQFQKKNE
     REEPSNAKVS EKSNSYLTIS PEENKLKDDY TVDECKIWKQ SKLSLPVVEA LPTVDSHEES
     SSVVVGSENI ENSSSSSTSE TSPISKLDEI ENSGTLSVAK PGDTEQPEAD CDAGEAADAD
     ASVEQPAFVS APESLVGQHI ENVSSSHGKE KVTKSEFESK VSVSEQDGGD PKSALNASDT
     LKNESSDYTK PRETDPTSVT SPKDPEDIPT FDEWKKKVME VEKEKSQSLH PSSNGGPHAT
     KKVQKNRNNY ASVECGAKIL AANPEAKSTS AILIENMDLY MLNPCSTKIW FVIELCEPIQ
     VKQFDIANYE LFSSTPKDFL VSISDRYPTN KWIKLGTFHG RDERTVQSFP LDEQMYAKYV
     KMFIKYIKVE LLSHFGSEHF CPLSLIRVFG TSMVEEYEEI ADSQYQSERQ ELFDEDYDYP
     LDYNTVEDKS SKNLLGSATN AILNMVNIAA NILGAKTEDL TEGDKSISEN ATATTEPKMP
     ESTGVSTPVP SPEYIIKEVH THDTEPPTSD PPKESPIVQL VQEEEEEASP STVTLLGSGE
     QEDESSSWFE SETQILCSEL TSICCISSFS EYLYKWCSVR IALYRQHSRT VSKGKDVSPQ
     PSLLPPVDSV EVSVLQPPSG NVDKEDMERE LETVALDDLS SVHQAHVRNH TVDTVELEPS
     YPQTLSQSLP LDVTPEMDSL STVEGSESVK SEGGHKPSQV MPQESSVEFD DETEKKPESF
     SSVAKLSVIY ETSKVNEVMD GPVKEDIVST HVVTKFPETK FPETVAPPPI NTAAVPESEG
     METKPSLADT LKHVVTPVTD PSLPEVKEDE QSPDDALLRG LQRTATDFYA ELQNSTDLGY
     GNGNLVHGSN QKESVFMRLN NRIKALEVNM SLSGRYLEEL SQRYRKQMEE MQKAFNKTIV
     KLQNTSRIAE EQDQRQTEAI HLLQAQLTNM TQIVSNLSAT VAELKREVSD RQSYLVMSLV
     LCVVLGLMLC MQRCRNTSQF DGDYTSKLPK SNQYPSPKRC FSSYDDMNLK RRTSFPLIRS
     KSLQFTGKED PNDLYIVEPL KFSPEKKKKR CKYKTEKIET IKPADPLHPI ANGDIKGRKP
     FTNQRDFSSM GEVYHSSYKG PPSEGSSETS SQSEESYFCG ISACTSLCNG QTQKTKLRRG
     LKRRRSKVQD QGKLIKALIQ TKSGSLPSLH DIIKGNKEIT VGAFGVTAVS GHI
 
 
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