SUCO_MOUSE
ID SUCO_MOUSE Reviewed; 1250 AA.
AC Q8C341; Q3TAG8; Q3V3T1; Q8CE34;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=SUN domain-containing ossification factor;
DE AltName: Full=Membrane protein CH1;
DE AltName: Full=Protein osteopotentia;
DE AltName: Full=SUN-like protein 1;
DE Flags: Precursor;
GN Name=Suco; Synonyms=Opt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cecum, Lung, Skin, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION,
RP GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=20440000; DOI=10.1083/jcb.201003006;
RA Sohaskey M.L., Jiang Y., Zhao J.J., Mohr A., Roemer F., Harland R.M.;
RT "Osteopotentia regulates osteoblast maturation, bone formation, and
RT skeletal integrity in mice.";
RL J. Cell Biol. 189:511-525(2010).
CC -!- FUNCTION: Required for bone modeling during late embryogenesis.
CC Regulates type I collagen synthesis in osteoblasts during their
CC postnatal maturation. {ECO:0000269|PubMed:20440000}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20440000}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:20440000}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C341-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C341-2; Sequence=VSP_027924;
CC -!- TISSUE SPECIFICITY: Present in chondrocytes, osteoblasts, osteoclasts
CC and osteocytes (at protein level). {ECO:0000269|PubMed:20440000}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 9.5 dpc and 13.5 dpc.
CC {ECO:0000269|PubMed:20440000}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20440000}.
CC -!- PTM: O-glycosylated. O-mannosylated by POMT1 and POMT2 and elongated by
CC POMGNT1. {ECO:0000250|UniProtKB:Q9UBS9}.
CC -!- DISRUPTION PHENOTYPE: Most mice die neonatally from respiratory
CC distress (50% on a mixed C57BL6/CD1 background and 100% on an inbred
CC C57BL6/129Ola background). Surviving mice fail to thrive and show
CC significantly reduced body weight, skeletal deformities and spontaneous
CC fractures. More than 80% die by postnatal day 10, and none survives to
CC weaning. {ECO:0000269|PubMed:20440000}.
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DR EMBL; AK029097; BAC26295.1; -; mRNA.
DR EMBL; AK033720; BAE43286.1; -; mRNA.
DR EMBL; AK087029; BAC39786.2; -; mRNA.
DR EMBL; AK171856; BAE42700.1; -; mRNA.
DR EMBL; AC164414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48415.1; -. [Q8C341-2]
DR RefSeq; XP_006496823.1; XM_006496760.2.
DR AlphaFoldDB; Q8C341; -.
DR SMR; Q8C341; -.
DR BioGRID; 230529; 1.
DR STRING; 10090.ENSMUSP00000044815; -.
DR GlyConnect; 2743; 6 N-Linked glycans (3 sites).
DR GlyGen; Q8C341; 6 sites, 6 N-linked glycans (3 sites).
DR iPTMnet; Q8C341; -.
DR PhosphoSitePlus; Q8C341; -.
DR EPD; Q8C341; -.
DR jPOST; Q8C341; -.
DR MaxQB; Q8C341; -.
DR PaxDb; Q8C341; -.
DR PRIDE; Q8C341; -.
DR ProteomicsDB; 257371; -. [Q8C341-1]
DR ProteomicsDB; 257372; -. [Q8C341-2]
DR Antibodypedia; 63320; 8 antibodies from 7 providers.
DR Ensembl; ENSMUST00000048377; ENSMUSP00000044815; ENSMUSG00000040297. [Q8C341-2]
DR MGI; MGI:2138346; Suco.
DR VEuPathDB; HostDB:ENSMUSG00000040297; -.
DR eggNOG; KOG1396; Eukaryota.
DR GeneTree; ENSGT00390000013502; -.
DR HOGENOM; CLU_006401_0_0_1; -.
DR InParanoid; Q8C341; -.
DR OMA; MNHTVDA; -.
DR TreeFam; TF105817; -.
DR BioGRID-ORCS; 226551; 9 hits in 73 CRISPR screens.
DR ChiTaRS; Suco; mouse.
DR PRO; PR:Q8C341; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8C341; protein.
DR Bgee; ENSMUSG00000040297; Expressed in epithelium of lens and 226 other tissues.
DR ExpressionAtlas; Q8C341; baseline and differential.
DR Genevisible; Q8C341; MM.
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; IDA:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA: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; IMP:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:UniProtKB.
DR GO; GO:0046850; P:regulation of bone remodeling; IMP: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 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Developmental protein;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Osteogenesis;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1250
FT /note="SUN domain-containing ossification factor"
FT /id="PRO_0000302718"
FT TRANSMEM 1007..1027
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 283..452
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT REGION 55..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 905..1005
FT /evidence="ECO:0000255"
FT COMPBIAS 119..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1077
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS9"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 924
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 951
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 285
FT /note="S -> SLSTG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027924"
FT CONFLICT 4
FT /note="Y -> N (in Ref. 1; BAE42700)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="T -> K (in Ref. 1; BAC26295)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1250 AA; 139169 MW; 8713115267891629 CRC64;
MKKYRRALAL VSCLSLCSLV WLPSWHVCCK ESSSASTSYY SQDDNCAIGS EDTQFQKKNE
REEPSNAELS GKSNSYLTIS PEGNKIKDDY TVDVQDLETT KLSLPVVEAL PTVDLHEESS
SVVVGSETIE NSSSSSTSER TPVSELDEVE KSGTLSIAKP GEVEQPEADC DAGEAPDADA
PVEQPAFVSP PESLVGQHIE NVSSSHGKEK VTKSEFESKV SVSEQDGGDP KSALNTSDTL
KNESSDYTKP GETDPTSVTS PKDPEDIPTF DEWKKKVMEV EKEKSQSLHP SSNGGPHATK
KVQKNRNNYA SVECGAKILA ANPEAKSTSA ILIENMDLYM LNPCSTKIWF VIELCEPIQV
KQFDIANYEL FSSTPKDFLV SISDRYPTNK WIKLGTFHGR DERNVQSFPL DEQMYAKYVK
MFIKYIKVEL LSHFGSEHFC PLSLIRVFGT SMVEEYEEIA DSQYQSERQE LFDEDYDYPL
DYNTVEDKSS KNLLGSATNA ILNMVNIAAN ILGAKTEDLT EGNKSISENA TATTEPKMTE
STRVSTPVPS PEYVIKEVHT HDREPSTSDP PKESPIVQLV QEEEEEASPS TVTLLGSGEQ
EDESSSWFES ETHILCSELT SICCISSFSE YIYKWCSVRI ALYRQRSRTV SKGKDFVPPQ
PSLLLPVESV EVSVPQPPSG DVDSENMERE AETVDLDDLS SVHQGHLINH TVDTIELEPS
YPQTLSQSLL LDVTPEMNSL SKVEGSESVK SEGGYIPSQL MTQESSVEFD DKTEKKTESF
SSAEKLSVIY ETSKVNEVMD NTVKEDILST EVVTKFPETV VPPPMNTATV PEGESVETKP
SIADTLKHTV TPVMDPSLPE VKEDEQSPED ALLRGLQRTA TDFYAELQNS TDLGYGNGNL
VHGSNQKESV FMRLNNRIKA LEVNMSLSGR YLEELSQRYR KQMEEMQKAF NKTIVKLQNT
SRIAEEQDQR QTEAIHLLQA QLTNMTQLVS NLSATVAELK REVSDRQSYL VMSLVLCVVL
GLMLCMQRCR TTSQFDGDYI SKLPKSNQYP SPKRCFSSYD DMNLKRRTSF PLIRSKSLQF
TGKEVDPNDL YIVEPLKFSP EKKKKRCKYK TEKIETIKPA DPLHPIANGD IKGRKPFTNQ
RDFSNMGEVY HSSYKGPPSE GSSETSSQSE ESYFCGISAC TSLCNGQTQK TKTEKRALKR
RRSKVQDQGK LIKALIQTKS GSLPSLHDII KGNKEITVGA FGVTAVSGHI
