SMC2_CHICK
ID SMC2_CHICK Reviewed; 1189 AA.
AC Q90988;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Structural maintenance of chromosomes protein 2;
DE Short=SMC protein 2;
DE Short=SMC-2;
DE AltName: Full=Chromosome scaffold protein ScII;
GN Name=SMC2; Synonyms=SCII, SMC2L1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=7929577; DOI=10.1083/jcb.127.2.303;
RA Saitoh N., Goldberg I.G., Wood E.R., Earnshaw W.C.;
RT "ScII: an abundant chromosome scaffold protein is a member of a family of
RT putative ATPases with an unusual predicted tertiary structure.";
RL J. Cell Biol. 127:303-318(1994).
CC -!- FUNCTION: Central component of the condensin complex, a complex
CC required for conversion of interphase chromatin into mitotic-like
CC condense chromosomes. The condensin complex probably introduces
CC positive supercoils into relaxed DNA in the presence of type I
CC topoisomerases and converts nicked DNA into positive knotted forms in
CC the presence of type II topoisomerases.
CC -!- SUBUNIT: Forms a heterodimer with SMC4. Component of the condensin
CC complex, which contains the SMC2 and SMC4 heterodimer, and probably
CC some non SMC subunits that regulate the complex.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In
CC interphase cells, the majority of the condensin complex is found in the
CC cytoplasm, while a minority of the complex is associated with
CC chromatin. A subpopulation of the complex however remains associated
CC with chromosome foci in interphase cells. During mitosis, most of the
CC condensin complex is associated with the chromatin. At the onset of
CC prophase, condensin associates with chromosome arms and to chromosome
CC condensation. Dissociation from chromosomes is observed in late
CC telophase.
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterodimerization with
CC SMC4, forming a V-shaped heterodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily. {ECO:0000305}.
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DR EMBL; X80792; CAA56767.1; -; mRNA.
DR PIR; A54817; A54817.
DR RefSeq; NP_990561.1; NM_205230.1.
DR AlphaFoldDB; Q90988; -.
DR SMR; Q90988; -.
DR STRING; 9031.ENSGALP00000036816; -.
DR GeneID; 396156; -.
DR KEGG; gga:396156; -.
DR CTD; 10592; -.
DR VEuPathDB; HostDB:geneid_396156; -.
DR eggNOG; KOG0933; Eukaryota.
DR InParanoid; Q90988; -.
DR OrthoDB; 119789at2759; -.
DR PhylomeDB; Q90988; -.
DR PRO; PR:Q90988; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000793; C:condensed chromosome; IBA:GO_Central.
DR GO; GO:0000796; C:condensin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; IBA:GO_Central.
DR CDD; cd03273; ABC_SMC2_euk; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR027120; Smc2_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Chromosome; Coiled coil; Cytoplasm;
KW DNA condensation; Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1189
FT /note="Structural maintenance of chromosomes protein 2"
FT /id="PRO_0000118997"
FT DOMAIN 522..639
FT /note="SMC hinge"
FT REGION 782..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 211..503
FT /evidence="ECO:0000255"
FT COILED 674..1030
FT /evidence="ECO:0000255"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1189 AA; 134941 MW; 905EBC89EC45AD5C CRC64;
MYIKSIVLEG FKSYAQRTEI RDFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS
SLQDLVYKNG QAGVNKATVS ITFDNSDKKN SPLGFENNDE ITITRQVIVG GRNKYLINGM
NASNNRVQDL FGSVGLNVNN PHFLIMQGQI TKVLNMKPTE ILAMIEEAAG TRMYECKKIT
AHKTIEKKES KLDEIRRIIT EEISPTLEKL KEARASYLEY QKMTREVENL RRIYVAFQYV
RAEEIKDRST NALKEAQANK KKIFESMAEN EKKVKELAQQ IEETEKKNNE EFGAKLHSLE
AAFSELQRVD AKVRSDLDHR KQNLNSEENR LKELIKIMQE EFKAFTSKEK EIKKIKEGLN
GLQEESKKDA EALASAQQHF NAVSAGLSSN DSGQGTSLAD QMMTCKNEIS KAATEAKQAQ
MKLKYAQQEL KTKQAEVKKM DGSYKEDQEA FEAIRKTKEK LQDEMKKLKY EEAEQEAHLA
KKKQLSSEIS SLRELCESIE AKHPYLRFEY KNPEKNWNPN CVKGLVVTLI TVKDISTSKA
LEAVAGGKLY NIVVDTEATG KKILEKGQLK HRYTIIPLSK ISANSIGHEI ISLAKNLIGH
REVHIAISLI DYNSELQKAM EYVFGTTLVC SSMDNAKKVT FDKRIMRKTV TLQGDIFDPQ
GTLSGGASSH VTPILSKLKT MRDAEDELKI KTSQLEATEK ELANLKNMAE KYQHLKQQWE
MKSEEAELLQ TKIQQSAYHK QQEDLLALKK TIAECEETLK KTEESQRKAE EEYKALENKM
KNAEAERGKE IKNAQQKLNS AKKKADDSSR KMKEKQQEVE ALVLELEQLK QEQASYKQQS
EAAQQAIASL KEQVSALEAE AVKTRESLKN AENELSSEKG LMEERTKDIK AKSAKIEKYR
EQNNELQLSI NALEHDINKY QQETADASST LDKLLKEYKW IASEKELFGQ ADTTYDFEAN
NPKETGQKLQ KLLTKKEKLE KSLNMRAMNL LSEAEERYND LMKKKRMVEN DKIKILATIE
ELDRKKNKAL HIAWEKVNKD FGSIFSMLLP GAKAMLVPSK KQNILDGLEF RVGLGDIWKE
NLTELSGGQR SLAALSLILA ILLFKPAPIY ILDEVDAALD LSHTQNIGQM LHAHFKQSQF
LVVSLKDGMF NNANVLYRTK FVDGISTVSR HCQLKKKQPL SEASNNKDE
