IGS10_RAT
ID IGS10_RAT Reviewed; 2597 AA.
AC Q6WRH9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Immunoglobulin superfamily member 10;
DE Short=IgSF10;
DE AltName: Full=Calvaria mechanical force protein 608;
DE Short=CMF608;
DE Flags: Precursor;
GN Name=Igsf10; Synonyms=Cmf608;
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], FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=14962803; DOI=10.1016/j.bone.2003.10.003;
RA Segev O., Samach A., Faerman A., Kalinski H., Beiman M., Gelfand A.,
RA Turam H., Boguslavsky S., Moshayov A., Gottlieb H., Kazanov E., Nevo Z.,
RA Robinson D., Skaliter R., Einat P., Binderman I., Feinstein E.;
RT "CMF608 -- a novel mechanical strain-induced bone-specific protein
RT expressed in early osteochondroprogenitor cells.";
RL Bone 34:246-260(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2577, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: Involved in the control of early migration of neurons
CC expressing gonadotropin-releasing hormone (GNRH neurons) (By
CC similarity). May be involved in the maintenance of
CC osteochondroprogenitor cells pool (PubMed:14962803).
CC {ECO:0000250|UniProtKB:Q3V1M1, ECO:0000269|PubMed:14962803}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6WRI0}.
CC -!- TISSUE SPECIFICITY: Expressed in bone. Main expression is present in
CC mesenchymal osteochondroprogenitors with fibroblast-like morphology
CC abundant in the regions of active bone modeling and remodeling.
CC {ECO:0000269|PubMed:14962803}.
CC -!- INDUCTION: By estrogen and blood loss. {ECO:0000269|PubMed:14962803}.
CC -!- PTM: N-terminally cleaved to produce a form of around 663 residues.
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DR EMBL; AY273816; AAQ16157.1; -; mRNA.
DR RefSeq; NP_942063.1; NM_198768.2.
DR AlphaFoldDB; Q6WRH9; -.
DR STRING; 10116.ENSRNOP00000018629; -.
DR GlyGen; Q6WRH9; 11 sites.
DR iPTMnet; Q6WRH9; -.
DR PhosphoSitePlus; Q6WRH9; -.
DR PaxDb; Q6WRH9; -.
DR PRIDE; Q6WRH9; -.
DR GeneID; 310448; -.
DR KEGG; rno:310448; -.
DR UCSC; RGD:735030; rat.
DR CTD; 285313; -.
DR RGD; 735030; Igsf10.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; Q6WRH9; -.
DR PhylomeDB; Q6WRH9; -.
DR PRO; PR:Q6WRH9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001503; P:ossification; IDA:MGI.
DR GO; GO:2001222; P:regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0042246; P:tissue regeneration; IDA:RGD.
DR Gene3D; 2.60.40.10; -; 12.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF07679; I-set; 8.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00409; IG; 12.
DR SMART; SM00408; IGc2; 12.
DR SMART; SM00406; IGv; 5.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48726; SSF48726; 12.
DR PROSITE; PS50835; IG_LIKE; 12.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Leucine-rich repeat; Osteogenesis; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..2597
FT /note="Immunoglobulin superfamily member 10"
FT /id="PRO_0000286819"
FT DOMAIN 29..56
FT /note="LRRNT"
FT REPEAT 58..79
FT /note="LRR 1"
FT REPEAT 82..103
FT /note="LRR 2"
FT REPEAT 106..127
FT /note="LRR 3"
FT REPEAT 130..151
FT /note="LRR 4"
FT REPEAT 154..175
FT /note="LRR 5"
FT REPEAT 186..207
FT /note="LRR 6"
FT DOMAIN 219..281
FT /note="LRRCT"
FT DOMAIN 461..567
FT /note="Ig-like C2-type 1"
FT DOMAIN 571..661
FT /note="Ig-like C2-type 2"
FT DOMAIN 1622..1713
FT /note="Ig-like C2-type 3"
FT DOMAIN 1718..1810
FT /note="Ig-like C2-type 4"
FT DOMAIN 1815..1907
FT /note="Ig-like C2-type 5"
FT DOMAIN 1915..2008
FT /note="Ig-like C2-type 6"
FT DOMAIN 2011..2109
FT /note="Ig-like C2-type 7"
FT DOMAIN 2115..2203
FT /note="Ig-like C2-type 8"
FT DOMAIN 2208..2305
FT /note="Ig-like C2-type 9"
FT DOMAIN 2311..2401
FT /note="Ig-like C2-type 10"
FT DOMAIN 2406..2492
FT /note="Ig-like C2-type 11"
FT DOMAIN 2502..2597
FT /note="Ig-like C2-type 12"
FT REGION 667..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1463
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2577
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1049
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1783
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1873
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1936
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2075
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 497..551
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 595..645
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1644..1697
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1741..1794
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1838..1891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1937..1990
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2034..2093
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2137..2187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2235..2287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2333..2385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2428..2480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2524..2579
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 2597 AA; 284743 MW; C6A284BBFCE2C5D2 CRC64;
MQVRGREVSG LLISLTAVCL VVTPGSRACP RRCACYVPTE VHCTFRYLTS IPDGIPANVE
RINLGYNSLT RLTENDFDGL SKLELLMLHS NGIHRVSDKT FSGLQSLQVL KMSYNKVQII
RKDTFYGLGS LVRLHLDHNN IEFINPEAFY GLTSLRLVHL EGNRLTKLHP DTFVSLSYLQ
IFKTSFIKYL FLSDNFLTSL PKEMVSYMPN LESLYLHGNP WTCDCHLKWL SEWMQGNPDI
IKCKKDRSSS SPQQCPLCMN PRISKGRPFA MVPSGAFLCT KPTIDPSLKS KSLVTQEDNG
SASTSPQDFI EPFGSLSLNM TDLSGNKADM VCSIQKPSRT SPTAFTEEND YIMLNASFST
NLVCSVDYNH IQPVWQLLAL YSDSPLILER KPQLTETPSL SSRYKQVALR PEDIFTSIEA
DVRADPFWFQ QEKIVLQLNR TATTLSTLQI QFSTDAQIAL PRAEMRAERL KWTMILMMNN
PKLERTVLVG GTIALSCPGK GDPSPHLEWL LADGSKVRAP YVSEDGRILI DKNGKLELQM
ADSFDAGLYH CISTNDADAD VLTYRITVVE PYGESTHDSG VQHTVVTGET LDLPCLSTGV
PDASISWILP GNTVFSQPSR DRQILNNGTL RILQVTPKDQ GHYQCVAANP SGADFSSFKV
SVQKKGQRMV EHDREAGGSG LGEPNSSVSL KQPASLKLSA SALTGSEAGK QVSGVHRKNK
HRDLIHRRRG DSTLRRFREH RRQLPLSARR IDPQRWAALL EKAKKNSVPK KQENTTVKPV
PLAVPLVELT DEEKDASGMI PPDEEFMVLK TKASGVPGRS PTADSGPVNH GFMTSIASGT
EVSTVNPQTL QSEHLPDFKL FSVTNGTAVT KSMNPSIASK IEDTTNQNPI IIFPSVAEIR
DSAQAGRASS QSAHPVTGGN MATYGHTNTY SSFTSKASTV LQPINPTESY GPQIPITGVS
RPSSSDISSH TTADPSFSSH PSGSHTTASS LFHIPRNNNT GNFPLSRHLG RERTIWSRGR
VKNPHRTPVL RRHRHRTVRP AIKGPANKNV SQVPATEYPG MCHTCPSAEG LTVATAALSV
PSSSHSALPK TNNVGVIAEE STTVVKKPLL LFKDKQNVDI EIITTTTKYS GGESNHVIPT
EASMTSAPTS VSLGKSPVDN SGHLSMPGTI QTGKDSVETT PLPSPLSTPS IPTSTKFSKR
KTPLHQIFVN NQKKEGMLKN PYQFGLQKNP AAKLPKIAPL LPTGQSSPSD STTLLTSPPP
ALSTTMAATQ NKGTEVVSGA RSLSAGKKQP FTNSSPVLPS TISKRSNTLN FLSTETPTVT
SPTATASVIM SETQRTRSKE AKDQIKGPRK NRNNANTTPR QVSGYSAYSA LTTADTPLAF
SHSPRQDDGG NVSAVAYHST TSLLAITELF EKYTQTLGNT TALETTLLSK SQESTTVKRA
SDTPPPLLSS GAPPVPTPSP PPFTKGVVTD SKVTSAFQMT SNRVVTIYES SRHNTDLQQP
SAEASPNPEI ITGTTDSPSN LFPSTSVPAL RVDKPQNSKW KPSPWPEHKY QLKSYSETIE
KGKRPAVSMS PHLSLPEAST HASHWNTQKH AEKSVFDKKP GQNPTSKHLP YVSLPKTLLK
KPRIIGGKAA SFTVPANSDV FLPCEAVGDP LPIIHWTRVS SGLEISQGTQ KSRFHVLPNG
TLSIQRVSIQ DRGQYLCSAF NPLGVDHFHV SLSVVFYPAR ILDRHVKEIT VHFGSTVELK
CRVEGMPRPT VSWILANQTV VSETAKGSRK VWVTPDGTLI IYNLSLYDRG FYKCVASNPS
GQDSLLVKIQ VITAPPVIIE QKRQAIVGVL GGSLKLPCTA KGTPQPSVHW VLYDGTELKP
LQLTHSRFFL YPNGTLYIRS IAPSVRGTYE CIATSSSGSE RRVVILTVEE GETIPRIETA
SQKWTEVNLG EKLLLNCSAT GDPKPRIIWR LPSKAVIDQW HRMGSRIHVY PNGSLVVGSV
TEKDAGDYLC VARNKMGDDL VLMHVRLRLT PAKIEQKQYF KKQVLHGKDF QVDCKASGSP
VPEVSWSLPD GTVLNNVAQA DDSGYRTKRY TLFHNGTLYF NNVGMAEEGD YICSAQNTLG
KDEMKVHLTV LTAIPRIRQS YKTTMRLRAG ETAVLDCEVT GEPKPNVFWL LPSNNVISFS
NDRFTFHANR TLSIHKVKPL DSGDYVCVAQ NPSGDDTKTY KLDIVSKPPL INGLYANKTV
IKATAIRHSK KYFDCRADGI PSSQVTWIMP GNIFLPAPYF GSRVTVHPNG TLEMRNIRLS
DSADFTCVVR SEGGESVLVV QLEVLEMLRR PTFRNPFNEK VIAQAGKPVA LNCSVDGNPP
PEITWILPDG TQFANRPHNS PYLMAGNGSL ILYKATRNKS GKYRCAARNK VGYIEKLILL
EIGQKPVILT YEPGMVKSVS GEPLSLHCVS DGIPKPNVKW TTPGGHVIDR PQVDGKYILH
ENGTLVIKAT TAHDQGNYIC RAQNSVGQAV ISVSVMVVAY PPRIINYLPR NMLRRTGEAM
QLHCVALGIP KPKVTWETPR HSLLSKATAR KPHRSEMLHP QGTLVIQNLQ TSDSGVYKCR
AQNLLGTDYA TTYIQVL
