SYCP2_RAT
ID SYCP2_RAT Reviewed; 1505 AA.
AC O70608;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Synaptonemal complex protein 2;
DE Short=SCP-2;
DE AltName: Full=Synaptonemal complex lateral element protein;
DE Short=rnSCP2;
GN Name=Sycp2; Synonyms=Scp2;
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], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Testis;
RX PubMed=9592139; DOI=10.1093/nar/26.11.2572;
RA Offenberg H.H., Schalk J.A.C., Meuwissen R.L.J., van Aalderen M.,
RA Kester H.A., Dietrich A.J.J., Heyting C.;
RT "SCP2: a major protein component of the axial elements of synaptonemal
RT complexes of the rat.";
RL Nucleic Acids Res. 26:2572-2579(1998).
RN [2]
RP SUBCELLULAR LOCATION, SUBUNIT, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9933407; DOI=10.1007/s004120050340;
RA Schalk J.A.C., Dietrich A.J.J., Vink A.C.G., Offenberg H.H.,
RA van Aalderen M., Heyting C.;
RT "Localization of SCP2 and SCP3 protein molecules within synaptonemal
RT complexes of the rat.";
RL Chromosoma 107:540-548(1998).
RN [3]
RP INTERACTION WITH SYCP3; SMC1A AND SMC3.
RX PubMed=10652260; DOI=10.1242/jcs.113.4.673;
RA Eijpe M., Heyting C., Gross B., Jessberger R.;
RT "Association of mammalian SMC1 and SMC3 proteins with meiotic chromosomes
RT and synaptonemal complexes.";
RL J. Cell Sci. 113:673-682(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; THR-503; SER-516;
RP SER-651; SER-655; SER-1123; SER-1130; SER-1162; SER-1170; SER-1218;
RP SER-1221; SER-1237; SER-1280 AND SER-1283, AND IDENTIFICATION BY MASS
RP 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 -!- FUNCTION: Major component of the axial/lateral elements of synaptonemal
CC complexes (SCS) during meiotic prophase (PubMed:9592139,
CC PubMed:9933407). Plays a role in the assembly of synaptonemal
CC complexes. Required for normal meiotic chromosome synapsis during
CC oocyte and spermatocyte development and for normal male and female
CC fertility. Required for insertion of SYCP3 into synaptonemal complexes.
CC May be involved in the organization of chromatin by temporarily binding
CC to DNA scaffold attachment regions. Requires SYCP3, but not SYCP1, in
CC order to be incorporated into the axial/lateral elements.
CC {ECO:0000250|UniProtKB:Q9CUU3, ECO:0000269|PubMed:9592139,
CC ECO:0000269|PubMed:9933407}.
CC -!- SUBUNIT: Component of the lateral elements of synaptonemal complexes
CC (PubMed:9592139, PubMed:9933407). Interacts with TEX11 (By similarity).
CC Heterodimer with SYCP3. Interacts with SYCP3, SMC1A and SMC3
CC (PubMed:10652260). {ECO:0000250|UniProtKB:Q9CUU3,
CC ECO:0000269|PubMed:10652260, ECO:0000269|PubMed:9592139}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9933407}. Chromosome
CC {ECO:0000269|PubMed:9592139, ECO:0000269|PubMed:9933407}. Note=In
CC axial/lateral elements of the tripartite segments of synaptonemal
CC complexes. {ECO:0000269|PubMed:9933407}.
CC -!- TISSUE SPECIFICITY: Detected in spermatocytes and testis (at protein
CC level) (PubMed:9592139, PubMed:9933407). Spermatocytes and oocytes.
CC Meiotic prophase cells. {ECO:0000269|PubMed:9592139,
CC ECO:0000269|PubMed:9933407}.
CC -!- DEVELOPMENTAL STAGE: Meiosis-specific. Highly expressed in meiotic
CC prophase cells, low expression persists in spermatids.
CC {ECO:0000269|PubMed:9592139}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9CUU3}.
CC -!- SIMILARITY: Belongs to the SYCP2 family. {ECO:0000305}.
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DR EMBL; Y08981; CAA70170.1; -; mRNA.
DR PIR; T31418; T31418.
DR RefSeq; NP_570091.1; NM_130735.1.
DR RefSeq; XP_008760769.1; XM_008762547.2.
DR RefSeq; XP_017447562.1; XM_017592073.1.
DR RefSeq; XP_017447563.1; XM_017592074.1.
DR AlphaFoldDB; O70608; -.
DR SMR; O70608; -.
DR STRING; 10116.ENSRNOP00000006038; -.
DR iPTMnet; O70608; -.
DR PhosphoSitePlus; O70608; -.
DR PaxDb; O70608; -.
DR PRIDE; O70608; -.
DR GeneID; 83820; -.
DR KEGG; rno:83820; -.
DR CTD; 10388; -.
DR RGD; 69429; Sycp2.
DR VEuPathDB; HostDB:ENSRNOG00000061690; -.
DR eggNOG; ENOG502QVM5; Eukaryota.
DR HOGENOM; CLU_004101_0_0_1; -.
DR InParanoid; O70608; -.
DR OMA; MAHERNV; -.
DR OrthoDB; 285929at2759; -.
DR PRO; PR:O70608; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000061690; Expressed in testis and 3 other tissues.
DR Genevisible; O70608; RN.
DR GO; GO:0000800; C:lateral element; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0000795; C:synaptonemal complex; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0007143; P:female meiotic nuclear division; ISO:RGD.
DR GO; GO:0009566; P:fertilization; ISO:RGD.
DR GO; GO:0048808; P:male genitalia morphogenesis; ISO:RGD.
DR GO; GO:0007140; P:male meiotic nuclear division; ISO:RGD.
DR GO; GO:0140013; P:meiotic nuclear division; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0051093; P:negative regulation of developmental process; IEA:Ensembl.
DR GO; GO:2000242; P:negative regulation of reproductive process; IEA:Ensembl.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024832; SYCP2.
DR InterPro; IPR024835; SYCP2-like.
DR InterPro; IPR041322; SYCP2_ARLD.
DR InterPro; IPR040560; SYCP2_SLD.
DR PANTHER; PTHR15607; PTHR15607; 1.
DR PANTHER; PTHR15607:SF12; PTHR15607:SF12; 1.
DR Pfam; PF18581; SYCP2_ARLD; 1.
DR Pfam; PF18584; SYCP2_SLD; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Coiled coil; DNA-binding; Meiosis;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1505
FT /note="Synaptonemal complex protein 2"
FT /id="PRO_0000072368"
FT REGION 439..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1384..1435
FT /evidence="ECO:0000255"
FT COMPBIAS 456..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 503
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 613
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 638
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 922
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1174
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1318
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
SQ SEQUENCE 1505 AA; 172593 MW; FD6FF99179B2A8C1 CRC64;
MPVRPDPQQL EKCIDDALRK NDFKPLVTLL QIDICEDVKI KCSKQFLRKL DDLICRELHK
KDIQTISNIL ISIGRCSKNI FILGQTGLQT MIKQGLVQKM VSWFENSKEI ILSQRQSKDE
AVMNMIEDLF DLLMVVYDVN DEGKNQVLES FIPHICALVI DSRVNFCIQQ EALKKMNLML
DRIPQDANKI LCNQEILTLM SNMGERILDV GDYELQVGIV EALCRMTTEK RRQELAYEWF
SMDFIANAFK KIKDCEFETD CRIFLNLVNG MLGDRRRVFT FPCLSAFLGK YELQIPSDEK
LEEFWIDFNL GSHTLSFYIA GDDDDHQWEA VTVPEEKVDM YNIEVRESKK LLTLTLKNIV
KISKKEGKEL LLYFDAALEI TNVTKKLFGG NKYKEFTRKQ DISVAKTSIH VLFDASGSQI
LVPESQPSPV KENLIHLKEK SNLQKKLTNP LEPDNSSSQR DRKNSQDEIT TPSRKKMSEA
SMIVPDTDRY TVRSPILLIN TSTPRRSRAP LQAIHSAEKA VSKTSESGVD YAVSLKSRQS
DGRNRGNNRA NHNKTATVQN KGHEHHESPD QTFNEIEETL SDAYAVEKVD KPVLPGVLDI
SKNKAHSRWA CWTPVTTIKL CNNQRSCALP GDTFTQDTGV NKKCTKQKSV SDDDSEETQR
VKYSKDVIKC NKSEEAEVCE RNIQEQNHPK YSQKKNTANA KKNDWHIESE TTYKSVLLNK
TTEESLIYKK TCVLSKDVNT TICDKSPSRK SMRSHTKSRK ELMSEVTSCE LDEIPVRENS
KGKRFTGTAE SLINLINKRY NSSDDMISTR KLKEPRDGSG FSKKPELQFN KVQRKSYRKL
KTVVNVTSEC PLNDVYNFSL NGADEPVIKL GIQEFQATTR EASMDNSIKL VDVRNRDERD
LSLKTKDERI LSHERKTLFS DTETECGWDD SKTDISWLRK PKSKRLMDYS RNKNTKKCKS
IKSRSSTEKG QPRSTVVLSK NIAKNDYEVI VDGRTRLPRR ATKTKKNYKD LSTSGSESES
EKEISYLFKD KLPTKEETVH SSAQTKKLPK KQQKVFNTEA LKGQPSEEQK NSSTLRNGRE
DSLYLSSASV SGSSSSVEVM RCTEKITERD FTQDYDYITK SLSPYPKAAS PEFLNRSNRV
VGHGKSPRIS ETSAVCVRKS CSPASGLPFS PRHTTKNNSV MNIKNTNSVI NNQRTQHCNS
YSDVSSNSSE KLYMEPESPD SCENHVQSKR EENHAASPFS LSSEKIEKIW FDMPNDNTHV
SGPSQRGSKR RMYLEEDELS NPSEAEVQEA EEREHLVSKK LCQREHFDQH TSETSLSTPE
FSVPKDWQQE LQGAGMFYDN INSDYKRKTD TQHKIMDDFT TKTLKLTQQH LLAMACQARG
HRDENIDKFQ VTLLDELEKV EKDSQTLRDL EKEFVDIEEK IVHKMRAFHQ SERERFRALK
TSLDKSLLVY NSVYEENVLT SEMCLMKANM KMLQDKLLKE MHEEELLNIR RGLESLFKDH
EGNNA
