SPAG4_RAT
ID SPAG4_RAT Reviewed; 444 AA.
AC O55034;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Sperm-associated antigen 4 protein;
DE AltName: Full=Outer dense fiber-associated protein SPAG4;
DE AltName: Full=SUN domain-containing protein 4;
GN Name=Spag4; Synonyms=Sun4;
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], CHARACTERIZATION, DEVELOPMENTAL STAGE,
RP HOMODIMERIZATION, AND INTERACTION WITH ODF1.
RC TISSUE=Testis;
RX PubMed=10373309; DOI=10.1006/dbio.1999.9297;
RA Shao X., Tarnasky H.A., Lee J.P., Oko R., van der Hoorn F.A.;
RT "Spag4, a novel sperm protein, binds outer dense-fiber protein Odf1 and
RT localizes to microtubules of manchette and axoneme.";
RL Dev. Biol. 211:109-123(1999).
CC -!- FUNCTION: Involved in spermatogenesis. Required for sperm head
CC formation but not required to establish and maintain general polarity
CC of the sperm head. Required for anchoring and organization of the
CC manchette. Required for targeting of SUN3 and probably SYNE1 through a
CC probable SUN1:SYNE3 LINC complex to the nuclear envelope and involved
CC in accurate posterior sperm head localization of the complex. May
CC anchor SUN3 the nuclear envelope. Involved in maintenance of the
CC nuclear envelope integrity (By similarity). May assist the organization
CC and assembly of outer dense fibers (ODFs), a specific structure of the
CC sperm tail (PubMed:10373309). {ECO:0000250|UniProtKB:Q9JJF2,
CC ECO:0000305|PubMed:10373309}.
CC -!- SUBUNIT: Self-associates. Interacts with ODF1. May associate with
CC microtubules (PubMed:10373309). Interacts with SUN3 and SYNE1;
CC suggesting the formation of a LINC complexs; a SUN domain-based
CC heterotrimer of SPAG4 and SUN3 may associate with SYNE1 (By
CC similarity). Interacts with SEPT12 and LMNB1; during spermatogenesis
CC (By similarity). {ECO:0000250|UniProtKB:Q9JJF2,
CC ECO:0000250|UniProtKB:Q9NPE6, ECO:0000269|PubMed:10373309}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10373309}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000269|PubMed:10373309}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q9JJF2}. Nucleus inner membrane
CC {ECO:0000250|UniProtKB:Q9JJF2}. Note=In spermatids, it is localized in
CC the transient manchette and in the axoneme of elongating spermatids and
CC epididymal sperm. {ECO:0000269|PubMed:10373309}.
CC -!- TISSUE SPECIFICITY: Testis specific. Exclusively expressed in
CC spermatids.
CC -!- DEVELOPMENTAL STAGE: Exclusively expressed in spermatids. Not present
CC in mature sperm. Localized with both the manchette and the axoneme in
CC step 10-11 spermatids. Detected on manchette microtubules of step 12
CC spermatids. Associates with the tail in steps 18-19 spermatids and
CC epididymal sperm. {ECO:0000269|PubMed:10373309}.
CC -!- CAUTION: Although transmembrane domains are strongly predicted, they
CC may rather represent hydrophobic globular domains associated with
CC microtubules. {ECO:0000305}.
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DR EMBL; AF043345; AAC32053.2; -; mRNA.
DR RefSeq; NP_113980.1; NM_031792.1.
DR AlphaFoldDB; O55034; -.
DR SMR; O55034; -.
DR STRING; 10116.ENSRNOP00000026578; -.
DR PhosphoSitePlus; O55034; -.
DR PaxDb; O55034; -.
DR GeneID; 83623; -.
DR KEGG; rno:83623; -.
DR UCSC; RGD:620151; rat.
DR CTD; 6676; -.
DR RGD; 620151; Spag4.
DR eggNOG; KOG2687; Eukaryota.
DR InParanoid; O55034; -.
DR OrthoDB; 1569602at2759; -.
DR PhylomeDB; O55034; -.
DR PRO; PR:O55034; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IEA:InterPro.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IDA:RGD.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR027776; SPAG4/SUN4.
DR InterPro; IPR045119; SUN1-5.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12911; PTHR12911; 1.
DR PANTHER; PTHR12911:SF16; PTHR12911:SF16; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Differentiation; Flagellum; Membrane; Nucleus; Reference proteome;
KW Spermatogenesis; Transmembrane; Transmembrane helix.
FT CHAIN 1..444
FT /note="Sperm-associated antigen 4 protein"
FT /id="PRO_0000218918"
FT TRANSMEM 137..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 267..428
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 204..241
FT /evidence="ECO:0000255"
FT COMPBIAS 8..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 48693 MW; DA05493E8F87C46B CRC64;
MRRNPRPGSA ASSHNHTPNF YSENSNSSHS ATSGDSNGRR SAGPELGEPD GRMARGSSCG
EPALSSGVPG GDTWAGSSRP KLAPRSHNGQ TACGAATVRG GASEPSGSPA VLEEQLNLLP
ILDLRQEMPP PPVSKSFLSL FFQVLSVFLS LVADGLVCVY REICSIRFLF TAVSLLSIFL
AALWWGLLYL IPPLENEPKE MLTLSQYHHR VHSQGQQLQQ LQAELSKLHK EVTSVRAAHS
ERVAKLVFQR LNEDFVRKPD YALSSVGASI DLEKTSSDYE DRNTAYFWNR LSFWNYARPP
SVILEPDVFP GNCWAFEGEQ GQVVIRLPGH VQLSDITLQH PPPTVAHTGG ASSAPRDFAV
FGLQADDDET EVFLGKFIFE VQKSEIQTFH LQNDPPSAFP KVKIQILSNW GHPRFTCLYR
VRAHGVRISE SAEDNAMGVT GGPH
