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SPAG1_RAT
ID   SPAG1_RAT               Reviewed;         893 AA.
AC   Q5U2X2;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Sperm-associated antigen 1;
DE   AltName: Full=HSD-3.8;
DE   AltName: Full=Infertility-related sperm protein Spag-1;
GN   Name=Spag1;
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].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=11517287; DOI=10.1093/molehr/7.9.811;
RA   Lin W., Zhou X.F., Zhang M.L., Li Y., Miao S.Y., Wang L.F., Zong S.D.,
RA   Koide S.S.;
RT   "Expression and function of the HSD-3.8 gene encoding a testis-specific
RT   protein.";
RL   Mol. Hum. Reprod. 7:811-818(2001).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; SER-703; SER-739 AND
RP   SER-740, AND IDENTIFICATION BY MASS 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: May play a role in the cytoplasmic assembly of the ciliary
CC       dynein arms (By similarity). Binds GTP and has GTPase activity (By
CC       similarity). Plays a role in fertilization (PubMed:11517287).
CC       {ECO:0000250|UniProtKB:Q07617, ECO:0000269|PubMed:11517287}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q07617}. Dynein
CC       axonemal particle {ECO:0000250|UniProtKB:Q07617}. Note=Colocalizes with
CC       tubulin. {ECO:0000250|UniProtKB:Q07617}.
CC   -!- TISSUE SPECIFICITY: Testis and sperm.
CC   -!- MISCELLANEOUS: Antibodies against SPAG1 interfere with fertilization.
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DR   EMBL; BC085828; AAH85828.1; -; mRNA.
DR   RefSeq; NP_001012116.1; NM_001012116.1.
DR   AlphaFoldDB; Q5U2X2; -.
DR   SMR; Q5U2X2; -.
DR   STRING; 10116.ENSRNOP00000013801; -.
DR   iPTMnet; Q5U2X2; -.
DR   PhosphoSitePlus; Q5U2X2; -.
DR   PaxDb; Q5U2X2; -.
DR   PRIDE; Q5U2X2; -.
DR   Ensembl; ENSRNOT00000013801; ENSRNOP00000013801; ENSRNOG00000010078.
DR   GeneID; 315033; -.
DR   KEGG; rno:315033; -.
DR   UCSC; RGD:1310702; rat.
DR   CTD; 6674; -.
DR   RGD; 1310702; Spag1.
DR   eggNOG; KOG1124; Eukaryota.
DR   GeneTree; ENSGT00940000154697; -.
DR   HOGENOM; CLU_008405_1_0_1; -.
DR   InParanoid; Q5U2X2; -.
DR   OMA; QLHRWDG; -.
DR   OrthoDB; 1070087at2759; -.
DR   PhylomeDB; Q5U2X2; -.
DR   TreeFam; TF106251; -.
DR   PRO; PR:Q5U2X2; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000010078; Expressed in testis and 19 other tissues.
DR   GO; GO:0101031; C:chaperone complex; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0120293; C:dynein axonemal particle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070286; P:axonemal dynein complex assembly; ISS:UniProtKB.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; -; 3.
DR   InterPro; IPR025986; RPAP3-like_C.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF13877; RPAP3_C; 1.
DR   Pfam; PF00515; TPR_1; 2.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 8.
DR   SUPFAM; SSF48452; SSF48452; 3.
DR   PROSITE; PS50005; TPR; 5.
DR   PROSITE; PS50293; TPR_REGION; 4.
PE   1: Evidence at protein level;
KW   Cytoplasm; Fertilization; GTP-binding; Hydrolase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..893
FT                   /note="Sperm-associated antigen 1"
FT                   /id="PRO_0000106326"
FT   REPEAT          213..246
FT                   /note="TPR 1"
FT   REPEAT          247..279
FT                   /note="TPR 2"
FT   REPEAT          280..313
FT                   /note="TPR 3"
FT   REPEAT          429..463
FT                   /note="TPR 4"
FT   REPEAT          471..504
FT                   /note="TPR 5"
FT   REPEAT          506..538
FT                   /note="TPR 6"
FT   REPEAT          605..638
FT                   /note="TPR 7"
FT   REPEAT          639..672
FT                   /note="TPR 8"
FT   REGION          112..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          324..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          704..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..367
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..431
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..736
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         630..637
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         703
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         739
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         740
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         758
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07617"
SQ   SEQUENCE   893 AA;  100615 MW;  E95507EFF0B3A49F CRC64;
     MTAKVKDHPP LWGFGTTKTF KIPIEHLDFK YIENCSDVKQ LEKILCVLRS GEEGYYPELT
     EFCEKRLTGL APRSRALRKD KPAATASSFS AEEWEKIDSD LKSWVSEIKR EENTRHFHDP
     EKHPGVEDPL PPVRGSNSCP RGGKETSSKS KTAKKRIPRD YAEWDKFDVE KECSKIDEDY
     KEKTVINNKA HLSKIETKID TAGLTEKEKN FLANREKGKG NEAFYSGDYE EAVMYYTRSL
     SALPTATAYN NRAQAEIKLQ RWSSALEDCE KALELEPGNI KALLRRATTY KHQNKFLEAV
     DDLRKVLQAE PDNDLAKKTL SEVERELKNS EPASELQTKG KRMVIEEVEN SGDEGGKGDE
     DDHEDDGVDM AAMGNIQKKL MVRSQGGRRS RRARTPMPGA EQQEGQPETG TASTSDNHDL
     EERRAADSPG DLKSRGNELF RGGQFAEAAV QYSGAIAQLE PTGSENADEL SILYSNRAAC
     YLKEGNCRGC IQDCDRALEL QPFAVKPLLR RAMAYETLEQ YRSAYVDYIT VLKIDCRIQL
     ASDSVNRITR ILTELDGPKW RERLPPIPAV PASEPLRVWH PAAETPDQDP CPNSCTPTIT
     DEKMFQALKE EGNQLVKDKN YKDAISKYNE CLKINSKACA IYTNRALCYL KLGQFEEAKL
     DCDKALQIDS KNVKASYRLE LAQKGLENCR ERVADPSQVV LLSPDSSEAA RHLDTKNDTA
     PPSRERERRR IEIQEVDDSS DEEPERPAEA SAVEEGWSAE RAGKIEVCKP RNAYEFGQVL
     STISARKDEE ACAQLLVFTA PQDLPVLLSN KLEGDMLLLI MQSLKSHLVA KDPSLVCKHL
     LYLSKAERFE MMLALTSKDQ KEQMAQLFDD LSDAQADCLT AEDIQALRRQ YVL
 
 
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