ID F1SH51_PIG Unreviewed; 1233 AA.
AC F1SH51;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 24-JAN-2024, entry version 90.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN Name=SMC4 {ECO:0000313|Ensembl:ENSSSCP00000012502.4,
GN ECO:0000313|VGNC:VGNC:93240};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000012502.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000012502.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000012502.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000012502.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC {ECO:0000256|ARBA:ARBA00006005}.
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DR AlphaFoldDB; F1SH51; -.
DR PaxDb; 9823-ENSSSCP00000012502; -.
DR PeptideAtlas; F1SH51; -.
DR Ensembl; ENSSSCT00000012842.5; ENSSSCP00000012502.4; ENSSSCG00000011731.5.
DR VGNC; VGNC:93240; SMC4.
DR GeneTree; ENSGT00900000141094; -.
DR HOGENOM; CLU_001042_4_1_1; -.
DR TreeFam; TF101158; -.
DR Proteomes; UP000008227; Chromosome 13.
DR Bgee; ENSSSCG00000011731; Expressed in tonsil and 43 other cell types or tissues.
DR ExpressionAtlas; F1SH51; baseline and differential.
DR Genevisible; F1SH51; SS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF172; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 2.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR SUPFAM; SSF57997; Tropomyosin; 2.
PE 1: Evidence at protein level;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1SH51};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 558..673
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 486..520
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 714..948
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1233 AA; 140795 MW; BFCD06D03932ACAC CRC64;
MPRKGTQPST ARRREEGPPQ SPDRTSSDAQ PESPPGCSES RAPATAETPS EEIDNRSLEE
ILSSIPPPPP PAMTNEAGAP RLMITHIVNQ NFKSYAGEKI LGPFHKRFSC IIGPNGSGKS
NVIDSMLFVF GYRAQKIRSK KLSVLIHNSD EHKDIQSCTV EVHFQKIIDK EGNDYEVVPN
SNFYVSRTAY RDNTSVYHIS GKKKTFKDVG NLLRSHGIDL DHNRFLILQG EVEQIAMMKP
KGQTEHDEGM LEYLEDIIGS GRLNEPIKVL CRRVEILNEH RGEKLNRVKM VEKEKDALEG
EKNIAIEFLT LENEIFRKKN HVCQYYIYDL QKRIAEMETQ KEKIHEDTKE INEKSNILSN
EMKAKNKAVK DVEKKLNKIT KFIEENKEKF TKLDLEDVQV REKLKHATSK AKKLEKQLQK
DKEKSQEKEL MGFSKSVNEA RSKMDVAQSE LDIYLSRYNT AVSQLSKAKD ALMAASETLK
ERKAAIGDIE AKLPQTECEL KEKEKELQKL TQEEINFKSL VRDLFQKVEE AKSSLAMNRS
RGKVLDAIIQ EKKTGRIPGI YGRLGDLGAI DEKYDVAISS CCHALDYIVV DSIDTAQECV
NFLKRQNIGV ATFIGLDKMA VWAKKMTQIQ TPENTPRLFD LVKVKDEKIR QAFYFALRDT
LVADNLDQAT RVAYQKDRRW RVVTLQGQII EQSGTMTGGG SKVMKGRMGS SVVVEISEEE
VNKMESQLQR DSQKAVQIQE HKVQLEETVV KLRHSEREMR NTLEKFTASI QRLSEQEEYL
RVQVKELEAN VLATAPDQKK QKLLEENVNA FKAEYDSVAE KAGKVEAEVK RLHNIIVEIN
NHKLKAQQDK LDKINKQLDE CASAITKAQV AIKTADRNLK KAQDSVFRTE KEIKDTEKEV
DDLTTELKSL EDKAAEVIKN TNAAEESLPE IQKEHRSLLQ ELKVIQENEH ALQKDALSIK
LKLEQIDGHI GEHNSKIKYW QKEISKISLH PIEDNPVEEI AVLTPEDLEA IKNPDSITNQ
IALLEAQCHE MKPNLGAIVE YKKKEELYLQ RVAELDKITY ERDNFRQAYE DLRKQRLNEF
MAGFYIITNK LKENYQMLTL GGDAELELVD SLDPFAEGIM FSVRPPKKSW KKIFNLSGGE
KTLSSLALVF ALHHYKPTPL YFMDEIDAAL DFKNVSIVAF YIYEQTKNAQ FIIISLRNNM
FEISDRLIGI YKTYNITKSV AVNPKEIASK GLC
//