Full text data of SUCO
SUCO
(C1orf9, CH1, OPT, SLP1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
SUN domain-containing ossification factor (Membrane protein CH1; Protein osteopotentia homolog; SUN-like protein 1; Flags: Precursor)
SUN domain-containing ossification factor (Membrane protein CH1; Protein osteopotentia homolog; SUN-like protein 1; Flags: Precursor)
hRBCD
IPI00003441
IPI00003441 Hypothetical protein ORF9 precursor Hypothetical protein ORF9 precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00003441 Hypothetical protein ORF9 precursor Hypothetical protein ORF9 precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
Q9UBS9
ID SUCO_HUMAN Reviewed; 1254 AA.
AC Q9UBS9; B2RNU4; Q9BQB9; Q9BXQ2; Q9UL04;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 89.
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=C1orf9, CH1, OPT, SLP1;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10673381; DOI=10.1006/bbrc.1999.2016;
RA Roesok O., Pedeutour F., Odeberg J., Lundeberg J., Aasheim H.-C.;
RT "The C1orf9 gene encodes a putative transmembrane member of a novel
RT protein family.";
RL Biochem. Biophys. Res. Commun. 267:855-862(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
RA Chen L.-C., Cheung J., Moore D., Ljung B.-M., Kuo W.-L., Collins C.,
RA Gray J.W., Smith H.S.;
RT "Cloning of an overexpressed gene on chromosome 1 in breast cancer
RT defines a new gene family.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Rhodes S.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-244.
RX PubMed=11158380;
RA Yu N., Zhao Z., Fu Y.-X., Sambuughin N., Ramsay M., Jenkins T.,
RA Leskinen E., Patthy L., Jorde L.B., Kuromori T., Li W.-H.;
RT "Global patterns of human DNA sequence variation in a 10-kb region on
RT chromosome 1.";
RL Mol. Biol. Evol. 18:214-222(2001).
RN [8]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Required for bone modeling during late embryogenesis.
CC Regulates type I collagen synthesis in osteoblasts during their
CC postnatal maturation (By similarity).
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane;
CC Single-pass type I membrane protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UBS9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBS9-2; Sequence=VSP_027921, VSP_027922, VSP_027923;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas and testis and to
CC a lower extent in prostate, ovary, heart, thymus, small intestine
CC and spleen.
CC -!- SIMILARITY: Contains 1 SUN domain.
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DR EMBL; AJ250075; CAB57360.1; -; mRNA.
DR EMBL; AF097535; AAF04619.1; -; mRNA.
DR EMBL; AL035291; CAA22894.1; -; mRNA.
DR EMBL; Z96050; CAI19034.1; -; Genomic_DNA.
DR EMBL; Z94054; CAI19034.1; JOINED; Genomic_DNA.
DR EMBL; Z94054; CAI19460.1; -; Genomic_DNA.
DR EMBL; Z96050; CAI19460.1; JOINED; Genomic_DNA.
DR EMBL; BC137125; AAI37126.1; -; mRNA.
DR EMBL; CH471067; EAW90931.1; -; Genomic_DNA.
DR EMBL; AF310265; AAK28742.1; -; Genomic_DNA.
DR EMBL; AF310266; AAK28743.1; -; Genomic_DNA.
DR EMBL; AF310267; AAK28744.1; -; Genomic_DNA.
DR EMBL; AF310268; AAK28745.1; -; Genomic_DNA.
DR EMBL; AF310269; AAK28746.1; -; Genomic_DNA.
DR EMBL; AF310270; AAK28747.1; -; Genomic_DNA.
DR EMBL; AF310271; AAK28748.1; -; Genomic_DNA.
DR EMBL; AF310272; AAK28749.1; -; Genomic_DNA.
DR EMBL; AF310273; AAK28750.1; -; Genomic_DNA.
DR EMBL; AF310274; AAK28751.1; -; Genomic_DNA.
DR EMBL; AF310275; AAK28752.1; -; Genomic_DNA.
DR EMBL; AF310276; AAK28753.1; -; Genomic_DNA.
DR EMBL; AF310277; AAK28754.1; -; Genomic_DNA.
DR EMBL; AF310278; AAK28755.1; -; Genomic_DNA.
DR EMBL; AF310279; AAK28756.1; -; Genomic_DNA.
DR EMBL; AF310280; AAK28757.1; -; Genomic_DNA.
DR EMBL; AF310281; AAK28758.1; -; Genomic_DNA.
DR EMBL; AF310282; AAK28759.1; -; Genomic_DNA.
DR EMBL; AF310283; AAK28760.1; -; Genomic_DNA.
DR EMBL; AF310284; AAK28761.1; -; Genomic_DNA.
DR EMBL; AF310285; AAK28762.1; -; Genomic_DNA.
DR EMBL; AF310286; AAK28763.1; -; Genomic_DNA.
DR EMBL; AF310287; AAK28764.1; -; Genomic_DNA.
DR EMBL; AF310288; AAK28765.1; -; Genomic_DNA.
DR EMBL; AF310289; AAK28766.1; -; Genomic_DNA.
DR EMBL; AF310290; AAK28767.1; -; Genomic_DNA.
DR EMBL; AF310291; AAK28768.1; -; Genomic_DNA.
DR EMBL; AF310292; AAK28769.1; -; Genomic_DNA.
DR EMBL; AF310293; AAK28770.1; -; Genomic_DNA.
DR EMBL; AF310294; AAK28771.1; -; Genomic_DNA.
DR EMBL; AF310295; AAK28772.1; -; Genomic_DNA.
DR EMBL; AF310296; AAK28773.1; -; Genomic_DNA.
DR EMBL; AF310297; AAK28774.1; -; Genomic_DNA.
DR EMBL; AF310298; AAK28775.1; -; Genomic_DNA.
DR EMBL; AF310299; AAK28776.1; -; Genomic_DNA.
DR EMBL; AF310300; AAK28777.1; -; Genomic_DNA.
DR EMBL; AF310301; AAK28778.1; -; Genomic_DNA.
DR EMBL; AF310302; AAK28779.1; -; Genomic_DNA.
DR EMBL; AF310303; AAK28780.1; -; Genomic_DNA.
DR EMBL; AF310304; AAK28781.1; -; Genomic_DNA.
DR EMBL; AF310305; AAK28782.1; -; Genomic_DNA.
DR EMBL; AF310306; AAK28783.1; -; Genomic_DNA.
DR EMBL; AF310307; AAK28784.1; -; Genomic_DNA.
DR EMBL; AF310308; AAK28785.1; -; Genomic_DNA.
DR EMBL; AF310309; AAK28786.1; -; Genomic_DNA.
DR EMBL; AF310310; AAK28787.1; -; Genomic_DNA.
DR EMBL; AF310311; AAK28788.1; -; Genomic_DNA.
DR EMBL; AF310312; AAK28789.1; -; Genomic_DNA.
DR EMBL; AF310313; AAK28790.1; -; Genomic_DNA.
DR EMBL; AF310314; AAK28791.1; -; Genomic_DNA.
DR EMBL; AF310315; AAK28792.1; -; Genomic_DNA.
DR EMBL; AF310316; AAK28793.1; -; Genomic_DNA.
DR EMBL; AF310317; AAK28794.1; -; Genomic_DNA.
DR EMBL; AF310318; AAK28795.1; -; Genomic_DNA.
DR EMBL; AF310319; AAK28796.1; -; Genomic_DNA.
DR EMBL; AF310320; AAK28797.1; -; Genomic_DNA.
DR EMBL; AF310321; AAK28798.1; -; Genomic_DNA.
DR EMBL; AF310322; AAK28799.1; -; Genomic_DNA.
DR EMBL; AF310323; AAK28800.1; -; Genomic_DNA.
DR EMBL; AF310324; AAK28801.1; -; Genomic_DNA.
DR EMBL; AF310325; AAK28802.1; -; Genomic_DNA.
DR PIR; JC7185; JC7185.
DR RefSeq; NP_001269679.1; NM_001282750.1.
DR RefSeq; NP_001269680.1; NM_001282751.1.
DR RefSeq; NP_055098.1; NM_014283.4.
DR RefSeq; NP_057311.3; NM_016227.3.
DR UniGene; Hs.204559; -.
DR ProteinModelPortal; Q9UBS9; -.
DR STRING; 9606.ENSP00000263688; -.
DR DMDM; 74761893; -.
DR PaxDb; Q9UBS9; -.
DR PRIDE; Q9UBS9; -.
DR Ensembl; ENST00000263688; ENSP00000263688; ENSG00000094975.
DR GeneID; 51430; -.
DR KEGG; hsa:51430; -.
DR UCSC; uc001giq.4; human.
DR CTD; 51430; -.
DR GeneCards; GC01P172502; -.
DR HGNC; HGNC:1240; SUCO.
DR HPA; HPA047251; -.
DR neXtProt; NX_Q9UBS9; -.
DR PharmGKB; PA25621; -.
DR eggNOG; NOG314762; -.
DR HOGENOM; HOG000070169; -.
DR HOVERGEN; HBG107549; -.
DR ChiTaRS; C1orf9; human.
DR GenomeRNAi; 51430; -.
DR NextBio; 54995; -.
DR PRO; PR:Q9UBS9; -.
DR ArrayExpress; Q9UBS9; -.
DR Bgee; Q9UBS9; -.
DR CleanEx; HS_C1orf9; -.
DR Genevestigator; Q9UBS9; -.
DR GO; GO:0016021; C:integral to 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:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
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 Gene3D; 2.60.120.260; -; 1.
DR InterPro; IPR008979; Galactose-bd-like.
DR InterPro; IPR012919; Sad1_UNC_C.
DR Pfam; PF07738; Sad1_UNC; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome;
KW Developmental protein; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Osteogenesis; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 29 Potential.
FT CHAIN 30 1254 SUN domain-containing ossification
FT factor.
FT /FTId=PRO_5000065707.
FT TRANSMEM 1011 1031 Helical; (Potential).
FT DOMAIN 284 453 SUN.
FT COILED 909 1009 Potential.
FT CARBOHYD 202 202 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 236 236 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 524 524 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 928 928 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 955 955 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 1 1 M -> MRGFLARPFLSTNQHLAQWGSPLPQGKGLVQLPSQH
FT TRHSRPFHELCSKEENSATVPKLISLVVSSETIDFSNKTMD
FT SRRDWEREKRILEGKLQLPKALARTQRARDEGRAWTSRWLQ
FT RRRSPESCEAPLSAPLWGPQRGLPGREPLRSRSASAIALRT
FT IGHILALLLRLLHLGLGSGGCREDVPPSGRGKKEEKM (in
FT isoform 2).
FT /FTId=VSP_027921.
FT VAR_SEQ 60 96 Missing (in isoform 2).
FT /FTId=VSP_027922.
FT VAR_SEQ 421 427 Missing (in isoform 2).
FT /FTId=VSP_027923.
FT CONFLICT 452 452 S -> N (in Ref. 2; AAF04619).
FT CONFLICT 811 811 V -> M (in Ref. 2; AAF04619).
SQ SEQUENCE 1254 AA; 139430 MW; 4EBA1ABCC27DAAB1 CRC64;
MKKHRRALAL VSCLFLCSLV WLPSWRVCCK ESSSASASSY YSQDDNCALE NEDVQFQKKD
EREGPINAES LGKSGSNLPI SPKEHKLKDD SIVDVQNTES KKLSPPVVET LPTVDLHEES
SNAVVDSETV ENISSSSTSE ITPISKLDEI EKSGTIPIAK PSETEQSETD CDVGEALDAS
APIEQPSFVS PPDSLVGQHI ENVSSSHGKG KITKSEFESK VSASEQGGGD PKSALNASDN
LKNESSDYTK PGDIDPTSVA SPKDPEDIPT FDEWKKKVME VEKEKSQSMH ASSNGGSHAT
KKVQKNRNNY ASVECGAKIL AANPEAKSTS AILIENMDLY MLNPCSTKIW FVIELCEPIQ
VKQLDIANYE LFSSTPKDFL VSISDRYPTN KWIKLGTFHG RDERNVQSFP LDEQMYAKYV
KMFIKYIKVE LLSHFGSEHF CPLSLIRVFG TSMVEEYEEI ADSQYHSERQ ELFDEDYDYP
LDYNTGEDKS SKNLLGSATN AILNMVNIAA NILGAKTEDL TEGNKSISEN ATATAAPKMP
ESTPVSTPVP SPEYVTTEVH THDMEPSTPD TPKESPIVQL VQEEEEEASP STVTLLGSGE
QEDESSPWFE SETQIFCSEL TTICCISSFS EYIYKWCSVR VALYRQRSRT ALSKGKDYLV
LAQPPLLLPA ESVDVSVLQP LSGELENTNI EREAETVVLG DLSSSMHQDD LVNHTVDAVE
LEPSHSQTLS QSLLLDITPE INPLPKIEVS ESVEYEAGHI PSPVIPQESS VEIDNETEQK
SESFSSIEKP SITYETNKVN ELMDNIIKED VNSMQIFTKL SETIVPPINT ATVPDNEDGE
AKMNIADTAK QTLISVVDSS SLPEVKEEEQ SPEDALLRGL QRTATDFYAE LQNSTDLGYA
NGNLVHGSNQ KESVFMRLNN RIKALEVNMS LSGRYLEELS QRYRKQMEEM QKAFNKTIVK
LQNTSRIAEE QDQRQTEAIQ LLQAQLTNMT QLVSNLSATV AELKREVSDR QSYLVISLVL
CVVLGLMLCM QRCRNTSQFD GDYISKLPKS NQYPSPKRCF SSYDDMNLKR RTSFPLMRSK
SLQLTGKEVD PNDLYIVEPL KFSPEKKKKR CKYKIEKIET IKPEEPLHPI ANGDIKGRKP
FTNQRDFSNM GEVYHSSYKG PPSEGSSETS SQSEESYFCG ISACTSLCNG QSQKTKTEKR
ALKRRRSKVQ DQGKLIKTLI QTKSGSLPSL HDIIKGNKEI TVGTFGVTAV SGHI
//
ID SUCO_HUMAN Reviewed; 1254 AA.
AC Q9UBS9; B2RNU4; Q9BQB9; Q9BXQ2; Q9UL04;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 89.
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=C1orf9, CH1, OPT, SLP1;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10673381; DOI=10.1006/bbrc.1999.2016;
RA Roesok O., Pedeutour F., Odeberg J., Lundeberg J., Aasheim H.-C.;
RT "The C1orf9 gene encodes a putative transmembrane member of a novel
RT protein family.";
RL Biochem. Biophys. Res. Commun. 267:855-862(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
RA Chen L.-C., Cheung J., Moore D., Ljung B.-M., Kuo W.-L., Collins C.,
RA Gray J.W., Smith H.S.;
RT "Cloning of an overexpressed gene on chromosome 1 in breast cancer
RT defines a new gene family.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Rhodes S.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-244.
RX PubMed=11158380;
RA Yu N., Zhao Z., Fu Y.-X., Sambuughin N., Ramsay M., Jenkins T.,
RA Leskinen E., Patthy L., Jorde L.B., Kuromori T., Li W.-H.;
RT "Global patterns of human DNA sequence variation in a 10-kb region on
RT chromosome 1.";
RL Mol. Biol. Evol. 18:214-222(2001).
RN [8]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Required for bone modeling during late embryogenesis.
CC Regulates type I collagen synthesis in osteoblasts during their
CC postnatal maturation (By similarity).
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane;
CC Single-pass type I membrane protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UBS9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBS9-2; Sequence=VSP_027921, VSP_027922, VSP_027923;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas and testis and to
CC a lower extent in prostate, ovary, heart, thymus, small intestine
CC and spleen.
CC -!- SIMILARITY: Contains 1 SUN domain.
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DR EMBL; AJ250075; CAB57360.1; -; mRNA.
DR EMBL; AF097535; AAF04619.1; -; mRNA.
DR EMBL; AL035291; CAA22894.1; -; mRNA.
DR EMBL; Z96050; CAI19034.1; -; Genomic_DNA.
DR EMBL; Z94054; CAI19034.1; JOINED; Genomic_DNA.
DR EMBL; Z94054; CAI19460.1; -; Genomic_DNA.
DR EMBL; Z96050; CAI19460.1; JOINED; Genomic_DNA.
DR EMBL; BC137125; AAI37126.1; -; mRNA.
DR EMBL; CH471067; EAW90931.1; -; Genomic_DNA.
DR EMBL; AF310265; AAK28742.1; -; Genomic_DNA.
DR EMBL; AF310266; AAK28743.1; -; Genomic_DNA.
DR EMBL; AF310267; AAK28744.1; -; Genomic_DNA.
DR EMBL; AF310268; AAK28745.1; -; Genomic_DNA.
DR EMBL; AF310269; AAK28746.1; -; Genomic_DNA.
DR EMBL; AF310270; AAK28747.1; -; Genomic_DNA.
DR EMBL; AF310271; AAK28748.1; -; Genomic_DNA.
DR EMBL; AF310272; AAK28749.1; -; Genomic_DNA.
DR EMBL; AF310273; AAK28750.1; -; Genomic_DNA.
DR EMBL; AF310274; AAK28751.1; -; Genomic_DNA.
DR EMBL; AF310275; AAK28752.1; -; Genomic_DNA.
DR EMBL; AF310276; AAK28753.1; -; Genomic_DNA.
DR EMBL; AF310277; AAK28754.1; -; Genomic_DNA.
DR EMBL; AF310278; AAK28755.1; -; Genomic_DNA.
DR EMBL; AF310279; AAK28756.1; -; Genomic_DNA.
DR EMBL; AF310280; AAK28757.1; -; Genomic_DNA.
DR EMBL; AF310281; AAK28758.1; -; Genomic_DNA.
DR EMBL; AF310282; AAK28759.1; -; Genomic_DNA.
DR EMBL; AF310283; AAK28760.1; -; Genomic_DNA.
DR EMBL; AF310284; AAK28761.1; -; Genomic_DNA.
DR EMBL; AF310285; AAK28762.1; -; Genomic_DNA.
DR EMBL; AF310286; AAK28763.1; -; Genomic_DNA.
DR EMBL; AF310287; AAK28764.1; -; Genomic_DNA.
DR EMBL; AF310288; AAK28765.1; -; Genomic_DNA.
DR EMBL; AF310289; AAK28766.1; -; Genomic_DNA.
DR EMBL; AF310290; AAK28767.1; -; Genomic_DNA.
DR EMBL; AF310291; AAK28768.1; -; Genomic_DNA.
DR EMBL; AF310292; AAK28769.1; -; Genomic_DNA.
DR EMBL; AF310293; AAK28770.1; -; Genomic_DNA.
DR EMBL; AF310294; AAK28771.1; -; Genomic_DNA.
DR EMBL; AF310295; AAK28772.1; -; Genomic_DNA.
DR EMBL; AF310296; AAK28773.1; -; Genomic_DNA.
DR EMBL; AF310297; AAK28774.1; -; Genomic_DNA.
DR EMBL; AF310298; AAK28775.1; -; Genomic_DNA.
DR EMBL; AF310299; AAK28776.1; -; Genomic_DNA.
DR EMBL; AF310300; AAK28777.1; -; Genomic_DNA.
DR EMBL; AF310301; AAK28778.1; -; Genomic_DNA.
DR EMBL; AF310302; AAK28779.1; -; Genomic_DNA.
DR EMBL; AF310303; AAK28780.1; -; Genomic_DNA.
DR EMBL; AF310304; AAK28781.1; -; Genomic_DNA.
DR EMBL; AF310305; AAK28782.1; -; Genomic_DNA.
DR EMBL; AF310306; AAK28783.1; -; Genomic_DNA.
DR EMBL; AF310307; AAK28784.1; -; Genomic_DNA.
DR EMBL; AF310308; AAK28785.1; -; Genomic_DNA.
DR EMBL; AF310309; AAK28786.1; -; Genomic_DNA.
DR EMBL; AF310310; AAK28787.1; -; Genomic_DNA.
DR EMBL; AF310311; AAK28788.1; -; Genomic_DNA.
DR EMBL; AF310312; AAK28789.1; -; Genomic_DNA.
DR EMBL; AF310313; AAK28790.1; -; Genomic_DNA.
DR EMBL; AF310314; AAK28791.1; -; Genomic_DNA.
DR EMBL; AF310315; AAK28792.1; -; Genomic_DNA.
DR EMBL; AF310316; AAK28793.1; -; Genomic_DNA.
DR EMBL; AF310317; AAK28794.1; -; Genomic_DNA.
DR EMBL; AF310318; AAK28795.1; -; Genomic_DNA.
DR EMBL; AF310319; AAK28796.1; -; Genomic_DNA.
DR EMBL; AF310320; AAK28797.1; -; Genomic_DNA.
DR EMBL; AF310321; AAK28798.1; -; Genomic_DNA.
DR EMBL; AF310322; AAK28799.1; -; Genomic_DNA.
DR EMBL; AF310323; AAK28800.1; -; Genomic_DNA.
DR EMBL; AF310324; AAK28801.1; -; Genomic_DNA.
DR EMBL; AF310325; AAK28802.1; -; Genomic_DNA.
DR PIR; JC7185; JC7185.
DR RefSeq; NP_001269679.1; NM_001282750.1.
DR RefSeq; NP_001269680.1; NM_001282751.1.
DR RefSeq; NP_055098.1; NM_014283.4.
DR RefSeq; NP_057311.3; NM_016227.3.
DR UniGene; Hs.204559; -.
DR ProteinModelPortal; Q9UBS9; -.
DR STRING; 9606.ENSP00000263688; -.
DR DMDM; 74761893; -.
DR PaxDb; Q9UBS9; -.
DR PRIDE; Q9UBS9; -.
DR Ensembl; ENST00000263688; ENSP00000263688; ENSG00000094975.
DR GeneID; 51430; -.
DR KEGG; hsa:51430; -.
DR UCSC; uc001giq.4; human.
DR CTD; 51430; -.
DR GeneCards; GC01P172502; -.
DR HGNC; HGNC:1240; SUCO.
DR HPA; HPA047251; -.
DR neXtProt; NX_Q9UBS9; -.
DR PharmGKB; PA25621; -.
DR eggNOG; NOG314762; -.
DR HOGENOM; HOG000070169; -.
DR HOVERGEN; HBG107549; -.
DR ChiTaRS; C1orf9; human.
DR GenomeRNAi; 51430; -.
DR NextBio; 54995; -.
DR PRO; PR:Q9UBS9; -.
DR ArrayExpress; Q9UBS9; -.
DR Bgee; Q9UBS9; -.
DR CleanEx; HS_C1orf9; -.
DR Genevestigator; Q9UBS9; -.
DR GO; GO:0016021; C:integral to 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:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
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 Gene3D; 2.60.120.260; -; 1.
DR InterPro; IPR008979; Galactose-bd-like.
DR InterPro; IPR012919; Sad1_UNC_C.
DR Pfam; PF07738; Sad1_UNC; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome;
KW Developmental protein; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Osteogenesis; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 29 Potential.
FT CHAIN 30 1254 SUN domain-containing ossification
FT factor.
FT /FTId=PRO_5000065707.
FT TRANSMEM 1011 1031 Helical; (Potential).
FT DOMAIN 284 453 SUN.
FT COILED 909 1009 Potential.
FT CARBOHYD 202 202 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 236 236 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 524 524 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 928 928 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 955 955 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 1 1 M -> MRGFLARPFLSTNQHLAQWGSPLPQGKGLVQLPSQH
FT TRHSRPFHELCSKEENSATVPKLISLVVSSETIDFSNKTMD
FT SRRDWEREKRILEGKLQLPKALARTQRARDEGRAWTSRWLQ
FT RRRSPESCEAPLSAPLWGPQRGLPGREPLRSRSASAIALRT
FT IGHILALLLRLLHLGLGSGGCREDVPPSGRGKKEEKM (in
FT isoform 2).
FT /FTId=VSP_027921.
FT VAR_SEQ 60 96 Missing (in isoform 2).
FT /FTId=VSP_027922.
FT VAR_SEQ 421 427 Missing (in isoform 2).
FT /FTId=VSP_027923.
FT CONFLICT 452 452 S -> N (in Ref. 2; AAF04619).
FT CONFLICT 811 811 V -> M (in Ref. 2; AAF04619).
SQ SEQUENCE 1254 AA; 139430 MW; 4EBA1ABCC27DAAB1 CRC64;
MKKHRRALAL VSCLFLCSLV WLPSWRVCCK ESSSASASSY YSQDDNCALE NEDVQFQKKD
EREGPINAES LGKSGSNLPI SPKEHKLKDD SIVDVQNTES KKLSPPVVET LPTVDLHEES
SNAVVDSETV ENISSSSTSE ITPISKLDEI EKSGTIPIAK PSETEQSETD CDVGEALDAS
APIEQPSFVS PPDSLVGQHI ENVSSSHGKG KITKSEFESK VSASEQGGGD PKSALNASDN
LKNESSDYTK PGDIDPTSVA SPKDPEDIPT FDEWKKKVME VEKEKSQSMH ASSNGGSHAT
KKVQKNRNNY ASVECGAKIL AANPEAKSTS AILIENMDLY MLNPCSTKIW FVIELCEPIQ
VKQLDIANYE LFSSTPKDFL VSISDRYPTN KWIKLGTFHG RDERNVQSFP LDEQMYAKYV
KMFIKYIKVE LLSHFGSEHF CPLSLIRVFG TSMVEEYEEI ADSQYHSERQ ELFDEDYDYP
LDYNTGEDKS SKNLLGSATN AILNMVNIAA NILGAKTEDL TEGNKSISEN ATATAAPKMP
ESTPVSTPVP SPEYVTTEVH THDMEPSTPD TPKESPIVQL VQEEEEEASP STVTLLGSGE
QEDESSPWFE SETQIFCSEL TTICCISSFS EYIYKWCSVR VALYRQRSRT ALSKGKDYLV
LAQPPLLLPA ESVDVSVLQP LSGELENTNI EREAETVVLG DLSSSMHQDD LVNHTVDAVE
LEPSHSQTLS QSLLLDITPE INPLPKIEVS ESVEYEAGHI PSPVIPQESS VEIDNETEQK
SESFSSIEKP SITYETNKVN ELMDNIIKED VNSMQIFTKL SETIVPPINT ATVPDNEDGE
AKMNIADTAK QTLISVVDSS SLPEVKEEEQ SPEDALLRGL QRTATDFYAE LQNSTDLGYA
NGNLVHGSNQ KESVFMRLNN RIKALEVNMS LSGRYLEELS QRYRKQMEEM QKAFNKTIVK
LQNTSRIAEE QDQRQTEAIQ LLQAQLTNMT QLVSNLSATV AELKREVSDR QSYLVISLVL
CVVLGLMLCM QRCRNTSQFD GDYISKLPKS NQYPSPKRCF SSYDDMNLKR RTSFPLMRSK
SLQLTGKEVD PNDLYIVEPL KFSPEKKKKR CKYKIEKIET IKPEEPLHPI ANGDIKGRKP
FTNQRDFSNM GEVYHSSYKG PPSEGSSETS SQSEESYFCG ISACTSLCNG QSQKTKTEKR
ALKRRRSKVQ DQGKLIKTLI QTKSGSLPSL HDIIKGNKEI TVGTFGVTAV SGHI
//